See discussions, stats, and author profiles for this publication at: https://www.researchgate.

net/publication/353917547

An Apodictic Review on Recent Approaches in Enzyme Technology

Article  in  Biointerface Research in Applied Chemistry · August 2021

DOI: 10.33263/BRIAC123.34463471

CITATION READS

1 158

6 authors, including:

Chithra Ashok Dinesh Palanimuthu

Bannari Amman Institute of Technology Bannari Amman Institute of Technology
2 PUBLICATIONS   0 CITATIONS    1 PUBLICATION   0 CITATIONS   

SEE PROFILE SEE PROFILE

Sharmila Devi V S Rudha Varshini Ammasai

Bannari Amman Institute of Technology Bannari Amman Institute of Technology
1 PUBLICATION   0 CITATIONS    1 PUBLICATION   0 CITATIONS   

SEE PROFILE SEE PROFILE

Some of the authors of this publication are also working on these related projects:

Molecular interactions in Microbe integrated phytoremediation View project

All content following this page was uploaded by Chithra Ashok on 16 August 2021.

The user has requested enhancement of the downloaded file.

 Review
Volume 12, Issue 3, 2022, 3446 - 3471
https://doi.org/10.33263/BRIAC123.34463471

An Apodictic Review on Recent Approaches in Enzyme

Technology
1 1 1
Chithra Ashok , Dinesh Palanimuthu , Sharmila Devi Velusamy Selvadurai , Rudha Varshini
1 1 1,*
Ammasai , Preethi Pethappampatti Senthilkumar , Rajaseetharama Sekar
1 Department of Biotechnology, Bannari Amman Institute of Technology, Sathyamangalam, Erode, Tamil Nadu, India-
638401
* Correspondence: [email protected] (R.S.);
Scopus Author ID 57222124942
Received: 21.06.2021; Revised: 25.07.2021; Accepted: 29.07.2021; Published: 8.08.2021

Abstract: Enzymes are the most powerful biochemical moieties, predominantly the working tools in
all living systems. Many studies have revealed the usage of various enzymes even in the pre-historical
periods. Enzymes are known to be the extremely active biocatalyst that is widely involved in many
metabolisms. Living systems explore these biomolecules for their metabolism and are exhaustively
explored for various industrial and clinical applications. Due to the increasing need for enzyme-based
products, various recent research focuses on exploring distinct enzymes & enzyme sources with
relatively enhanced characteristics. The elegant motive of this review is to enable the readers and
enzyme researchers to compend the basics of enzymes, explore the enormous recent clinical & industrial
applications of enzymes like amylase, cellulase, protease, lipase, and esterase. And also, the review
highly emphasizes the various enzyme source and their enriched properties like enzyme activity,
annotated by recent research works carried out by various research teams across the globe. The review
also accentuates the recent advancements in production technologies and high throughput activity
prediction assays for the above-mentioned industrially important enzymes.

Keywords: enzymes; enzyme sources; therapeutical enzymes; industrial enzymes; high throughput
enzyme assays.
© 2021 by the authors. This article is an open-access article distributed under the terms and conditions of the Creative
Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

1. Introduction

Enzymes are the most basic biocatalyst for the catalysis reaction of the substrate. It is a
globular protein of high molecular weight with a long linear chain of amino acids like other
proteins and having specific properties that depend on the structure. They are made up of a
three-dimensional complex of polypeptide chains [1]. Enzymes are available in a wide source
such as plants, animal tissues, and several microorganisms, and they are used in the textile and
manufacturing industries as an alternative to toxic chemicals for many processing procedures
[2]. Nowadays, they are rapidly important in some sectors like pharma, green chemistry, and
sustainable technology. The global enzyme market in 2020 was around USD 7.5 billion, and
the annual growth rate between 2016 to 2021 is 8.2% [3,4]. The global enzyme market is
planned to show high profitable growth of enzymes in the field of detergent, pharmaceutical,
and even in the chemical sectors. Enzymes are more sensitive to various entities; they get
inactive in high temperatures, acids, radiation and are also easily denatured by some biological
factors [5]. Enzymes are powerful biocatalysts. Lowering the activation energy can increase
https://biointerfaceresearch.com/ 3446
 https://doi.org/10.33263/BRIAC123.34463471

the reaction rate in lower concentration and carry out the reaction without consuming and
undergoing any changes [6]. They are specific in their function and reaction, with that different
enzyme performs various mechanism including covalent-catalysis, acid-base, electrostatic
[7,8]. The biochemical reaction carried out by plants, microbes, and animals is the result
directly produced by the enzyme catalysis. Mostly, the biochemistry background is indirectly
or directly related to enzyme history. The basic building blocks of the living system have the
capability to use biocatalyst known as enzyme effectively [9]. Enzymes have vast applications
in the pharmaceutical industry to treat various ailments like cancer, etc. They are used to reduce
tumor tissue inflammation, infectious pathogens prevention from tumor tissues, and so forth
[10]. Not only in the pharma sector, but they also have more applications in other fields like
food processing, textile processing, paper industry, etc. The enzymes reviewed in this study
are amylase, cellulase, protease, lipase, and esterase. These enzymes have more therapeutic
potential [11-13]. Amylase has been considered important among the other enzymes, and the
amylase produced from pineapple stem is about 34.4% and from the lotus stem is about 20-
30% [14]. Amylase is produced by animals, fungi, molds, bacteria, and plants but bacteria and
fungi are the most important sources for amylase production in the industries [15]. It is used to
degrade the starch into oligosaccharides; also, it will improve the yield of the product. The raw
starch hydrolysis by amylase was a major breakthrough in the starch processing industry,
reducing the cost of starch-based products [16]. It can be used in fruit drinks, textile, detergent,
and alcohol & beverages industries [17]. It is also used as functional biomaterials such as
adsorbent, cosmetic, carrier, agriculture, or structure-directing agent in food, pharmaceutical,
paper, and tissue engineering [18]. Cellulase is an essential industrial enzyme in the global
enzyme market [19]. In oil & petroleum, food processing fields, the cellulase enzyme plays a
major role. The most abundant biomass (lignocellulose) acts as a renewable source for biofuels
& other value-added products. And efficiently hydrolyzed by the microbial cellulases. So, it
was the most important research field for researchers and industrialists [20,21]. The protease
enzymes are also known as proteolytic, peptidase, or proteinase, which are present in bacteria,
plants, animals, some kind of algae, and also viruses. Approximately 40% of total worldwide
sales in the industrial enzyme are protease. Protease enzymes are available from many
organisms, even though some are only considered for commercial uses [22]. Protease can
degrade the proteins which are mainly used in the animal feed and leather industry [6]. Lipase
plays an important role in dairy product fermentation since ancient days [23]. Lipid metabolism
in the way of in-situ and the multifaceted ex-situ application in industries were carried out by
lipase. Lipase can degrade oil and fatty acids. It is mostly used in the detergent and dairy
industries. Due to their interesting properties, lipase plays a role in different modern areas, for
example, agro-substance, paper assembling, cosmetics, etc. [24]. Esterase can degrade the ester
into alcohol and acid, which is also considered an important enzyme in biotechnology. Due to
its capability, esterase can survive in the environment, and it is distributed widely in animals,
microorganisms, and plants. In organic solvents, they can be active and stable. It is one of the
tremendous properties of the esterase [25,26]. It plays an important role in industries like
oleochemical, dairy, and biodiesel. Also, thermostable esterase are suited for industries due to
their stabilization in high temperature [27,28]. Hence, the various enzyme plays several
commercially and clinically significant role in this industrial era. This review completely
focuses on highlighting recent diverse application, source, bioprocess approaches, and high
throughput assay techniques.

https://biointerfaceresearch.com/ 3447
 https://doi.org/10.33263/BRIAC123.34463471

2. Materials and Methods

This review gives the cumulative idea about the basis of the enzyme, sources of
enzyme, application, high throughput techniques used for enzyme assays, and advanced
bioprocess approaches. Various recent scientific researches and reviews have supplemented
this article. This review is comprised of 175 references covering the above-mentioned topics.
Among these references, the most cited papers are recent published articles (around the years
of 2018-2021, about 61.71%). This is to bring out the enzyme importance in recent years and
its novel application around the multidisciplinary fields. The second most cited reference
belongs between 2011-2017, around 26.29%. After that, 10.29% of sources were cited between
2001 and 2010, and the remaining 1.71% is below 2000. The details are graphically explained
in Figure 1.

Year wise citation detail

61.71
60

50
Number of papers

40

30
26.29

20

10.29
10

1.71
0
<2000 2001-2010 2011-2017 2018-2021
Publications years Number of papers

Figure 1. Year-wise citation detail.

Figure 2. Enzyme Stratification.

https://biointerfaceresearch.com/ 3448
 https://doi.org/10.33263/BRIAC123.34463471

3. Enzyme basics & Stratification

Enzymes have exhibited increased effectiveness and efficiency in many industrial

processes and products, which has environmental benefits. This enzyme represents the protein
groups and widely plays an important role in various processes like cell division, expression of
genes, important immune system reactions, and metabolic activities. Enzymes are classified
into seven classes, as shown in Figure 2 [29].
The enzyme oxidoreductase catalyzes the oxidation and reduction reaction by
transferring the electron from one particle to another particle also removing the hydrogen atom
utilizing the enzymes. These enzyme groups mainly utilize cofactors such as NADP+ and
NAD+. This enzyme is found in algae, bacteria, fungi, plants, and animals. Thermoascus
aurantiacus, Neurospora crassa, Lentinus similis like some fungi and bacteria such as
Enterococcus faecalis, and Lactobacillus kefir are used to catalyze the lytic polysaccharide
monooxygenases (LPMOs) substrates. It has applications in various sectors such as the
immunological sector, medicine, and industries like fruit ripening and growth, cell wall
metabolism, pathogens defense mechanism, etc., [30]. Examples are dehydrogenases,
peroxidases, oxidases, reductases.
The enzyme class transferases catalyzed the transfer of a particular functional group
(e.g., phosphate, acyl, and amino groups) from one substance to another. This enzyme is
involved in the hundreds of various pathways in the biological reaction. It also involves the
myriad cell reaction [29]. The Cytosolic Glutathione transferases (GSTs), which is a common
transferase enzyme, are present in insects, plants, fungi, bacteria, and mammals. It is helpful in
cancer monitoring and diagnostics, drug metabolism, drug, and pro-drug design, which is also
used in the field biosensor for detecting the herbicide. The examples are trans aldolases,
methyltransferases, kinase, transaminases.
Hydrolase enzymes catalyze the cleavage of the hydrolytic bond such as C-O, C-C, and
C-N. This enzyme also transfers the water molecules; that is, the hydrolysis of the substrate
can be catalyzed by the hydrolases enzymes. Few important examples of hydrolase enzymes
are included below. This enzyme is mostly found in bacteria and filamentous fungi, like
Aspergillus niger, Trichoderma reesei, and Bacillus, which are also present in some high-order
organisms like gastropods, arthropods, plants, insects, and marine algae [29]. Hydrolase
enzyme is used in all major industrial fields. Examples of hydrolase are protease, amylase,
cellulase, and lipase.
Lyases enzymes catalyze the C-C, C-O, C-S, and C-N bond cleavage by eliminating
the other bonds. Lyases can remove or add water, carbon dioxide, and ammonia elements from
double bonds through the non-hydrolytic bond-breaking reaction. These enzymes are involved
in the signal transduction pathways, anabolic and metabolic pathways, and DNA repair
mechanisms [29]. It plays a key role in the food and chemical industries, preparation of natural
products, and pharmaceutical intermediates. This enzyme presence was observed in plants,
animals, and some microorganism's genera like Fusarium, Aspergillus, Penicillium [31].
Aldolases, decarboxylases, and synthases are examples of lyases enzymes.
The isomerase is the enzyme class that comes under the fifth group of enzyme
commission (EC) classification (EC - 5). The isomerases catalyzed the isomerization reactions
or intermolecular rearrangements. It is categorized into seven sub-classes: They were,
racemases and epimerases, intramolecular oxidoreductases, intramolecular transferases,
intramolecular lyases, cis-trans isomerases, isomerases altering macromolecular conformation.
https://biointerfaceresearch.com/ 3449
 https://doi.org/10.33263/BRIAC123.34463471

The enzyme helps in interconversions which occurs in most organisms. For example,
alanine racemase catalyzes the racemization of amino acids. Isomerases are subdivided into,
cis-trans isomerases, intramolecular oxidoreductases, racemases & epimerases, intramolecular
transferases, intramolecular lyases [32]. In most living organisms, the isomerase catalyzes the
biochemical reaction, particularly carbohydrate metabolism, up to 4% [33]. They have
important uses in biotechnology, drug discovery, and organic synthesis. For example, a novel
glucose isomerase enzyme extracted from Caldicoprobacter algeriensis, has excellent
thermostable property and gained industrial importance in recent years. And also, protein
disulfide isomerase (PDI) had been overexpressed and helps in the proliferation of cancer cells.
The anti-cancerous activity has been elicited on the Epithelial ovarian cancer models by
targeting the PDI [34,35]. Examples are glucose isomerase, sucrose isomerase & D- arabinose
isomerase.
The ligase is the class of enzyme that constitutes the sixth group of classification (EC -
6). It was further divided into six sub-classes based on the formation of bonds. They are
phosphoric-ester, Carbon-oxygen, Carbon-nitrogen, Carbon-Sulphur, Carbon-carbon, and
Nitrogen metal. The ligase catalyzes the joining of two or more molecules together, which are
connected to the hydrolysis of analogous or ATP molecules. As they catalyze the reaction that
generates the new molecule, they are termed Synthetases [36]. It involves biologically essential
reactions, and it was about 81 ligases that play an important role in central metabolism [37].
For Example, DNA ligase is commonly used to join DNA fragments [38]. DNA ligase is an
example of ligase.
An enzyme translocase can catalyze the molecules or ions translocation across the cell
or separation in membranes which frequently hydrolysis the ATP, called translocases (EC - 7).
The translocase is the new class of enzyme that catalyzes the translocation of ions/molecules
within membranes or across the cell with the hydrolysis of ATP. It is also subdivided into six
subclasses. By the translocated ion/molecule, they are divided into six subclasses. The enzyme
catalyzing the translocation of hydrons, catalyzing the translocation of amino acids and
peptides, catalyzing the translocation of inorganic cations, catalyzing the translocation of
carbohydrates and their derivatives, catalyzing the translocation of other compounds,
catalyzing the inorganic anions and their chelates belongs to this class [39]. It plays an essential
role in the mitochondrial transport system. Its deficiency may lead to a disorder (i.e.) Carnitine-
acylcarnitine translocase deficiency [40]. An example of a translocase enzyme is amino
phospholipid translocase.

4. Enzymes in Industries

Amylase enzyme has very significant importance in the industrial sector. It is

extensively used in detergent industries. The crude enzyme obtained from Bacillus
mojavensis is used in laundry industries because of its alkaline conditions activity and stability
at a wide temperature range & with other detergent components such as anionic & non-ionic
surfactants and other oxidizing agents [41]. The Amylase soap-nut extract combination can de-
stain the blood-stained cloth in 30 minutes [42]. Amylase is used in the detergent industry
because of its sustainability and high stain-removing efficiency. At low temperatures, amylase,
which is cold-active like amy175, is produced, and it has increased the power of stain removing
efficiency [43]. Cold active amylases are used as an eco-friendly additive in detergents. Low
temperature and higher pH are the suitable conditions for using amylase as a detergent additive
https://biointerfaceresearch.com/ 3450
 https://doi.org/10.33263/BRIAC123.34463471

[44]. In the food industry, amylase will increase the quality and texture of the bread. The
addition of microbial amylase with a specific volume (7.7%), reduces the hardness &
chewiness by 11.5% and 17.2%, respectively. It also increased the texture profile by increasing
the size and number of holes [45,46]. Amylase enzyme extracted from Rhizomucor miehei is
used as a high potential candidate in food industries [45]. Multiple amylases from microbes
and fungi were used in industries. Bacterial amylases are mostly used in many industrial
processes due to their higher stability[47].
Amylase is used broadly in the production of bio-fuel. The second-wide application of
amylase in the industry is bioethanol production. Initially, the slurry was gelatinized with a jet
cooker. Then, it liquified using thermally stable α-amylase, which results in the saccharification
and the release of fermentable sugars. It is subsequently fermented, and bioethanol is produced
[48]. Using corn amylase instead of yeast in the process of dry-grind reduces enzyme usage,
and it is combined and used in bioethanol production [49]. Bioethanol is produced from the
biorefinery waste stream by treating enzymes like amylase with wheat bran using
saccharification and fermentation methods [50].
Cellulase has an application in the pulp processing industry. Due to their potentials in
paper pulp modification, the paper-making industries relied on lignocellulosic enzymes such
as cellulase and xylanase. In combination with other enzymes, cellulase was used in bio-
bleaching, deinking of waste papers, and in the modification of paper & pulp characteristics
[51]. Cellulase is the third-highest enzyme used in industries for various applications. It is used
in applications like bio pulping, bio stoning, bio bleaching, etc. In bio pulping, enzymes are
made to break down, and by bio bleaching, the brightness of paper is increased [52]. Recycling
cellulase with fresh cellulase helps to dissolve the pulp more effectively [53]. Lycopene &
soluble dietary fibers (SDF) extraction using cellulase can reduce coronary heart disease risk,
obesity, stroke, diabetes, and other diseases. Lycopene has antioxidant & anti-tumor properties.
The enzymatic approach in the lycopene & SDF extraction from tomato will be considered safe
when compared to chemical means. The use of cellulase and laccase will increase the yield of
lycopene and SDF by 23.8% and 72.3%, respectively [54]. Cellulase was a cell wall degrading
enzyme which has an application in the extraction of lycopene from tomatoes [55]. Extraction
of soluble dietary fiber from potato pulp is first pre-treated with cellulase and xylanase, which
gives better yield and also enhances the physiological and functional properties of SDF [56].
The enzyme protease is broadly used in leather industries. Leather industries follow the
conventional process that uses hazardous chemicals such as sodium sulfide and lime. It results
in issues such as effluent disposal and pollution. The protease is used to hydrolyze the non-
collagenous protein of the skin and remove globulins & albumins [57]. Keratinolytic protease
is an environmentally friendly biocatalyst that is used in the production of high-quality leather
[58]. Proteases are used in place of traditional chemical agents, which reduces pollution [59].
Protease has important applications in the food and food processing industries. It is used in
cheese ripening, flavor development, and milk coagulation in dairy industries and is also used
in meat processing industries. In the cheese production process, proteases are added to milk in
order to hydrolyze cheese. Proteases are also used in tenderizing meat [60]. In the baking
industry, it is used in dough preparations and gluten development. In seafood processing, it is
used in the production of fishmeal and enhances oil recovery [61]. Aspartic proteases are used
in food and beverages [62].

https://biointerfaceresearch.com/ 3451
 https://doi.org/10.33263/BRIAC123.34463471

Lipase plays an important role in degrading lipid pollutants. The presence of lipid
pollutants in the water can cause severe problems like the formation of the lipid layer over the
water, which affects the aquatic ecosystem. Similarly, the lipid pollutants present in the soil
can cause difficulties in water movement, reduce the ability of water to bind to soil particles,
and limit the aeration, which adversely affects the ecosystem. The lipase, which is immobilized
with cellulosic particles, was used to degrade the lipids and grease accumulated in wastewater
pipelines [63]. To degrade lipid accumulated oil bodies, TAG (triacylglycerol) lipases are
responsible for the lipid productivity enhancement in microalgae [64].
Due to the esterase solid remediation property, it can degrade the herbicides such as
metsulfuron-methyl, chlorimuron-ethyl, and tribenuron-methyl. The immobilized esterase can
be used in the remediation of soil contaminated with pesticides [65]. The calorimetric method
is used to determine the soil’s esterase activities in which fatty acids esters are linked to p-
nitrophenol as substrates [66]. Novel esterase, which was derived from metagenomics, plays a
major role in diesel-oil degradation [67]. Enzymes are catalytic biosensors that bind to the
analyte & converts into products. By the electrochemical transducer, read out the target
consumption during the conversion. The enzyme will be selected based on the target, such as
acetylcholine esterase for acetylcholine, cholesterol oxidase for cholesterol, glucose oxidase
for glucose, horseradish peroxidase for H2O2, and tyrosinase for bisphenol. Most of the
enzymes act as a biocatalyst as well as a bioreactor for many biological processes, such as H2O2
acts as a signaling molecule for cell death monitoring, immune cell activation, root growth, and
stomatal closure. So, it is important to biosensing in many platforms [68].

5. Clinical usage of enzyme

Currently, enzymes have profound application in the clinical section and an important
role in diagnosis, prevention, therapeutics, and biochemical analysis. Nowadays, in the
therapeutic field, enzymes are used to treat digestive disorders to cancer therapy, also
cardiovascular and lysosomal storage diseases. The recent advanced techniques improve the
production of human-like therapeutic enzymes by DNA recombination [69].
Amylase has the capability of targeted drug delivery and is also used for "Smart
release". Amylase taken from Aspergillus oryzae is used as a digestive aid to treat dyspepsia
[70]. For pancreatic disease diagnostics, primarily amylase is used [71]. The exponential
increase of multidrug-resistant bacteria happened throughout the year and became a severe
threat to human health. These microorganisms form a biofilm which is extracellular polymeric
substances (EPS) that helps to attach to the biotic and abiotic surfaces. On successful
conjugation of silver nanoparticles (AgNPs) with α-amylase, it is used against K.
pneumoniae and methicillin-resistant Staphylococcus aureus (MRSA). It exhibited
antimicrobial activity and reduced the formation of biofilm [72]. The higher levels of α-
amylase in the liver could be used to indicate the earlier stages of obesity [73]. The α-amylase
in the serum can be used as a biomarker for various pancreatic ailments. And α-amylase
concentration can be used as real-time detection for pancreatic disorders. Millions of people
can get benefitted from this affordable procedure [74]. Despite the benefits of kidney
transplantation, complications in the post-transplant period affect the long-term allograft. For
most kidney transplants, "Delayed graft function (DGF)" is a common complication. It is
caused particularly for those who received a kidney transplant from a deceased donor [75]. At

https://biointerfaceresearch.com/ 3452
 https://doi.org/10.33263/BRIAC123.34463471

the earlier stages of DGF, an increase in serum amylase and Resistive index (RI) will occur.
DGF can be detected earlier by the serum amylase and RI>0.7 after the kidney transplant [76].
Cellulase has a vital clinical application. The bezoars are caused by the presence of
partially digested or undigested material in the gastrointestinal tract. It is cured by cellulase,
which prevents reintervention also [77,78]. The cellulase-treated wheat bran used in pasta
production has comparatively high soluble fibers and a lower glycaemic index than untreated
[79]. Keratitis is a serious corneal infection that may cause blindness. The use of contact lenses
is the leading risk factor for microbial keratitis. In combination with anti-amoebic compounds,
cellulase effectively prevents keratitis, which targets the cyst wall [80,81]. In medical textiles,
antibacterial activity was necessary to reduce the bioburden and hospital-acquired infections.
The cellulase-treated fabrics were coated with Zinc Oxide (ZnO) nanoparticles, which provide
better adhesion, and the antibacterial activity remains even after the multiple washing [82]. The
extracts from cellulase-treated microalgae cells show higher toxicity against the benign tumor
than lysozyme and other chemical drugs [83].
Protease (Bromelain, chymotrypsin) from Ananas comosus and serum was used to treat
edema, inflammation, upper respiratory tract, and ophthalmology diseases. Papain protease is
used for the treatment of Thrombotic disorder [84]. Proteolytic activity regulation is a major
factor in the clinical application of protease. Cellular receptors, growth factors, and chemokines
are regulated by protease through inactivation and activation of gene regulation and
intracellular signaling [85]. Protease was also investigated for the nanomedicine approaches to
target and treat the tumor, and some fundamental processes were already implemented to treat
cancer disease [86]. The maintenance of homeostasis is essential in pathogenic organisms and
humans. This can be done by protease enzyme [87].
Lipase enzyme has an excellent pharmaceutical application and diagnostic aids.
Especially, it is used for the digestion of fats in humans also for the treatment of lifestyle
diseases known as obesity [88,89]. The lipase from Candida rugosa synthesizes lovastatin, a
drug that lowers serum cholesterol levels. 4-Methoxyphenyl glycidic acid methyl ester
(MPGM) is a key product synthesis from diltiazem hydrochloride is utilized for the coronary
vasodilator screened from Serratia marcescens [90]. Enantioselective transesterification and
interesterification response by the assistance of lipases have incredible essentialness in the drug
industry for specific diacylation and acylation response [91]. Monoacylglycerol lipase is
responsible for the pro-tumorigenic or pro-inflammatory effects of the metabolism process
[92].
Esterase plays a major role in clinical applications. Cocaine esterase (CocE) is a
favorable strategy for treating addiction and overdose cocaine [93]. Leucocyte esterase enzyme
is widely found in urine and feces. The strip made by leucocyte esterase plays a major role in
periprosthetic joint infection diagnostics [94]. It plays a main role in inflammation reduction,
pain relief from arthritis, menstruation, fever, and sunburn. Esterase extracted from
Trichosporon brassicae has effective pain-relieving results. Pseudomonas sp. producing
esterase enzyme has an ibuprofen-like therapeutic effect [95]. Feruloyl esterase will increase
the antioxidant property when it is added to other compounds like fruit juice, and syrup also
plays a role in flavor and color [96].

https://biointerfaceresearch.com/ 3453
 https://doi.org/10.33263/BRIAC123. 34463471

Table 1. Different sources of enzymes with allied industrially significant details.

Enzyme
Enzyme name Organism name Growth media Specific conditions Source Reference
activity
Streptomyces Starch agar medium which Incubated at 28 ± 2 ℃ Vishakhapatnam coast, Bay of 25.53 ± 0.50 [97]
parvulus strain has the composition of g/L: for 7 days. Bengal (Sediment sample) U/ml.
sankarensis-A10 soluble starch 10.0, seawater
(50% v/v), Meat extract 3.0,
agar 15. Then, the pH
adjusted to 7.0 ± 0.2
Bacillus subtilis Thermus agar added with Incubated at 45 ℃ for Dusun Tua Hot Spring, Hulu 22.14 U/ml. [98]
SUNGB2 agar, Beef extract, peptone, 24-48 hours. Langat, Selangor & Sungai
yeast extract, and NaCl. Klah Hot Spring, Perak,
Malaysia (Water samples)
Streptomyces sp. Al- Actinomycetes isolation agar Incubated at 28 ℃ for 7 Jazan, Saudi Arabia (Soil 241 ± 18.1 [99]
Dhabi-46 days. samples) U/ml.
AMYLASE Bacillus sp. strain SP- Horikoshi medium Incubated at 37 ℃ for Chilika Lake, India (Sediment 202.857 U/ml. [100]
CH7 72 hours. samples)
Bacillus sp. Q-164 Nutrient agar medium Incubated at 37 ℃ for Vishakhapatnam, Andhra 942 U/mg. [14]
48 hours. Pradesh, India (Palm wine)
Saccharopolyspora Glycerol yeast extract agar, Goa, Alibagh, and Mumbai 1640.80 U/mg. [101]
sp. strain A9 Maltose yeast extract agar, coastal region of India
Glucose asparagine agar, (sediment samples)
Starch casein agar medium -
containing Starch
(Prepared in artificial
seawater)
Bacillus tequilensis Starch agar medium Incubated at 37 ℃ for Chandigarh, India (Vegetable 39.736 ± 0.296 [102]
TB5 72 hours. waste) U/ml.
Bacillus subtilis D19 Soluble starch - Food sample 0.670 U/mg. [103]
Bacillus Carboxyl methylcellulose The plates were Rajshahi Sugar Mills Ltd., 7.82 IU/ml. [104]
pseudomycoides Y3 (CMC) Agar medium incubated at 37 ℃ until Bangladesh (Sugarcane
sufficient growth. bagasse)
CELLULASE
Bacillus velezensis Primary screening medium The plates were Lanxi Pig Farm, Suihua City, 20.20 ± 0.74 [105]
(carboxymethylcellulose incubated at 37 ℃ for Heilongjiang Province, China U/ml.
sodium, NaCl, Tryptone, 24 hours. (Manure samples)
yeast powder)

3454
https://biointerfaceresearch.com/
 https://doi.org/10.33263/BRIAC123.34463471

Saccharomyces Media constituents were The pH of the medium Mushroom farm in Yala Local 0.01951 ± 0.32 [106]
cerevisiae SCPW 17 NaNO3, KH2PO4, was 6.0 and plates were Government Area of Cross U/mg
MgSO4.7H2O, KCl, Protease, incubated at 28 ± 2 ℃ River State, Nigeria (Soil
peptone, Agar, aqueous for 3-5 days. samples)
glucose, carboxymethyl
cellulose, and xylan. &
Ligninase basal medium
supplemented with lignin,
agar.
Bacillus Sp. Tryptic soy agar & Modified At 30 ℃ the plates were Gut sample of O. coerulescens 9.0 U/mg. [107]
DNH5437 M-II medium (K2HPO4, incubated and 37 ℃ for collected from North East Iran
KH2PO4, KCl, NaCl, NH4Cl, a month. (Almond gardens).
MgSO4.7H2O, CaCl2.2H2O,
peptone, yeast extract,
glucose, agar)
Bacillus licheniformis Basic Liquid Media Rajapur (Western Coastal area) 42.99 U/ml. [108]
NCIM 5556 (KH2PO4, (NH4) 2SO4, Ratnagiri District, Maharashtra,
-
MgSO4.7H2O, FeSO4, NaCl India. (Soil and water samples)
& yeast extract.)
Aspergillus fumigatus Potato dextrose agar medium Bhubaneswar, India (Soil 1.9 U/ml. [109]
-
(CWSF-7) samples)
Bacillus velezensis Carboxymethyl-cellulose For 48 hours at 37 ℃ Barka, Oman, Animal 2.42 U/ml. [110]
ASN1 (CMC) agar medium the plates were farmhouse. (Soil samples)
incubated.
Bacillus subtilis BY-2 LB agar medium The incubated time is Tibetan pig from Shaanxi 3.56 U/ml. [111]
supplemented with 1 % CMC about 37 ℃ for 24 HuaYi Industrial Co., Ltd.;
hours. Tibetan pig breeding base.
(Intestinal samples)
Cladosporium Potato dextrose agar medium. For 4 to 6 days the Agriculture field of Banaras 0.240 U/mg. [112]
cladosporioides NS2 plates were incubated at Hindu University, Varanasi,
45 ℃. India. (Rotten wood sample)
Aneurinibacillus Nutrient agar medium The medium was Dal lake, Jammu& Kashmir, 83.1092 U/L. [113]
aneurinilyticus BKT- incubated at 37 ℃. India. (Water samples)
9
Vibrio alginolyticus Skim milk media The culture plate Sediments sample collected 228.81 U/ml. [114]
maintained and kept for from Pantai Gading mangroves,
incubation for 21, 24, North Sumatra, Indonesia.
27 hrs at 30°C.
PROTEASE
Citricoccus sp. Alkaline agar media Specific temperature 24- Agriculture soil from Regional 26.87 U/ml. [115]
(KC522120.1) 48hrs was maintained Centre of Soil Salinity Research
for the culture plate at Institute, Lucknow (U.P.), India.
30°C.

3455
https://biointerfaceresearch.com/
 https://doi.org/10.33263/BRIAC123.34463471

Streptomyces sp. Al- Skimmed milk agar media The plates kept at 28°C Soil sample collected from 147.2 ± 3.6 [116]
Dhabi-49 for 5 days up to pH-9. Dammam marine region. U/ml.
Nutrient Agar media The growth of this Agriculture, compost, and 60.41 ± 0.01 [117]
Bacillus cereus TSA5 bacteria is high at 32°C garden soil U/mg.
for 2 days at pH 7-8.
Streptomyces sp. Al- Starch casein agar To reduce the microbial Jazan region of Saudi Arabia 276 U/mg. [118]
Dhabi-82 growth nalidixic acid soil.
and nystatin-like
antibiotics were added
with the starch casein
agar.
Pseudomonas Azocasein with phosphate The specific temperature Raw milk samples from New 1.04±0.02 U/ml. [119]
lundensis DZ845 buffer saline solution and maintained for the Zealand.
sodium azide samples were 37°C for
24 hours.
Pseudomonas Modified Luria- Additionally, 10% of Crude oil contaminated soil 10,876 U/ml. [120]
aeruginosa Bertani(MLB) agar plates toluene and from Jiangsu province, China.
cyclohexane were added
to the medium.
Nesternkonia halobia casein-yeast plate agar (CYP) 48 hrs incubation at Soil or mud from the Lake 41.2 U/mg [121]
37°C recommended. Abjata shore, a soda alkaline
lake, Ethiopian Rift valley.
Chromobacterium Using slaughterhouse effluent From Ramanthpur of 0.1254 U/ml. [122]
violaceum which filtered (500ml) and Telangana, the slaughter house
granulated agar (7.5 g) effluent was collected
-
slaughterhouse effluent agar
was prepared.
Haloferax lucentensi Tryptone Yeast Extract 25% of NaCl was used Agro-food waste. 142.34 U/ml. [123]
(NTYE) agar.
Bacillus sp. SP II-4 Skim milk agar. Saltpan where the strains were 591.04 U/mg. [124]
- collected which is located in
Kanyakumari
Pseudomonas Nutrient agar Soil from mechanic’s shop 528,540 U/ml [125]
aeruginosa - inverse Forestry College,
Jericho, G.R.A, and Ibadan.
Pseudomonas Nutrient broth 20% (v/v) to 40% (v/v) The wastewater produced from 0.76 U/ml. [126]
LIPASE
aeruginosa wastewater added to the oil processing plant located in
broth. Tehran.
Pseudomonas Yeast Extract Peptone This media was From Sikkim, the soil sample 179.3 U/mg. [127]
helmanticensis HS6 Dextrose Agar (YPDA) incubated for 48 hrs at were collected above sea level
30°C to 37°C. ranging 2500 to 4272 m.

3456
https://biointerfaceresearch.com/
 https://doi.org/10.33263/BRIAC123.34463471

Pseudomonas reinekei Inoculated in a medium Incubated at 28°C for Wicklow mountains soil from 3.18I U/mg. [128]
containing olive oil is a 72 hrs. Ireland.
carbon source.
Pria Laot Sabang 80 The solid medium of ½ Kept for 70°C for 18 The water sample was collected 54.2 U/mg. [129]
(PLS 80) Thermus (½ T) hrs. from underwater fumaroles in
Aceh Province, Indonesia.
Cystobasidium YPD medium Incubated at 30°C for Soil collected from Jodhpur is 2.88 ± 0.166 [130]
oligophagum JRC1 120 rpm. rich in cellulosic waste. U/mg.
Staphylococcus Luria Broth (LB) agar Samples from sludge and 2.3 U/mg. [131]
warneri sediment were taken from the
-
Pulp and Paper Mill of
Uttarakhand.
Psychrobacter Nutrient marine medium 2216 Kept for incubation at Seawater collected from Frei 1.78 U/mg. [132]
immobilis 4°C. Montalva Base at King George
Island.
Staphylococcus Nutrient agar with seawater. Plates were incubated at Sediment was collected from 100 ± 0.121 [133]
saprophyticus 37°C for 5 days. the eastern slope of the Arabian U/mg.
Sea.
Aspergillus awamori Malt extract (ME) fungal agar 2% (v/v) of rice bran oil The fungal strain from the 123.7 U/mg. [134]
medium. was added with the Arabian sea of Kerala was
medium. isolated.
Fusarium solani FS1 Potato-dextrose-agar Plates were maintained Federal Rural University, Plant 0.45 U/mg. [135]
4°C. health department, Pernambuco.
Micropolyspora faeni V8 agar Kept incubation at 40°C From London School of 145 U/mg [136]
for 6 days. Hygiene and Tropical Medicine
the soil sample were collected.
Bacillus sp. 4 Castenholz basal salts The plates were kept for Alangȕllȕ thermal spring 137.77 U/ml. [137]
solution 24 h at 65 ◦C on a (Aydin, Turkey)
shaker at 150 rpm.
Rhodococcus sp. Nutrient broth Using 135 rpm at 60°C. Soil sample from Gangotri, 795.1 U/mg. [138]
LKE-021 Uttarakhand, Himalayas.
Rhodococcus sp. Nutrient broth Maintaining in 60°C for Samples of soil from Gangotri, 13.5 U/mg. [25]
ESTERASE
LKE-021 5 days. Uttarakhand Himalayas.
Ophiostoma piceae Malt extract –glucose –agar This culture kept - 79 U/mg. [139]
incubated at 26°C and
160 rpm.
Pseudomonas putida Luria-Bertani Kept at 30 °C for the Soil from National Taiwan 1.00±40 [140]
period of 1 to 2 days. University and the Taoyuan U/ml.
District was collected.
Trichoderma viride Nutrient agar Cultivated area clay in western 0.27 U/mg. [141]
-
Washington was collected.

3457
https://biointerfaceresearch.com/
 https://doi.org/10.33263/BRIAC123. 34463471

6. Diverse sources of enzyme

Microorganisms are extensively used in industries as they afford enormous economic

ease to industries. Enzymes produced by animals and plants are the most favored source
because of their advantages like easy and consistent production. Microbial enzymes are more
stable than plant and animal enzymes. Enzymes extracted from microbes are easier to handle
and cheaper than plant and animal sources. Microbial enzymes can be produced very
effectually by different fermentation techniques in a frugal manner with less time and space
demand.
Production of microbial enzymes on a large scale can be done facilely. The samples are
being selected from different places to know the qualitative or quantitative nature of the
microbes. The growth media of enzymes, conditions, source, and activities are discussed below
(Table 1).

7. Recent process advancements in enzyme technology

Due to its wide range of applications, amylase production needs to be increased. The
important step in the production of enzymes is fermentation technology. For amylase
production, submerged fermentation and flask scale fermentation are suggested because of
their easy handling and control of greater ecology factors such as pH and temperature
[142,143]. In the submerged fermentation, the maximum activity is analyzed under the
optimum condition. Mainly solid-state fermentation is utilized for the production of the
metabolites where the purity requirement is low. But also, the down streaming process involved
in the SSF is more challenging [144]. To obtain the pure polishing amylase enzyme product, a
series of downstream processing is involved. They are ultrafiltration, precipitation, membrane
separations, and chromatography techniques [145].
Owing to its industrial application, cellulase manufacture is essential to increase. After
the isolation process was carried out, the submerged and solid-state fermentation techniques
were utilized to produce cellulase. A study shows that the submerged fermentation was used to
increase cellulase enzyme production [146]. Among the various factors involved in the
submerged fermentation, the incubation time and temperature play a wide role in cellulase
production. But the changes made in submerged fermentation steps and factors can directly
affect the production of the enzyme [147,148]. And the purification steps involved here are
ammonium sulfate precipitation, centrifugation, dialysis, and chromatography techniques like
anion exchange chromatography, gel filtration chromatography [149,150]. After the
downstream process, the purity of the product and activity can be analyzed.
Nearly 60% of the industrial market needs protease enzymes. In order to satisfy, the
production needs to be raised. To raise the production needs, sources from various organisms
were selected, incubated, and characterized; the protease production using the Submerged
fermentation (SmF) or Solid-state fermentation (SSF) step can be carried substrate is liquid,
the shake flask fermentation can carry. The shake flask fermentation used for the production
of protease in a liquid medium gives a high amount of yield, but it undergoes several
purification steps that are difficult to carry out [151,152]. And it also consumes much time.
The production of protease can be influenced by pH, temperature, incubation period, and
nitrogen concentration. In these above methods, the widely explored process is wheat bran

https://biointerfaceresearch.com/ 3458
 https://doi.org/10.33263/BRIAC123.34463471

mediated SSF because of its easy purification steps and high yield production of protease [153].
Down streaming represents obtaining pure products and product polishing. A wide range of
techniques is available to recover the product from the fermented substrate. Protease
purification involves several steps and procedures like precipitation, liquid-liquid extraction,
chromatography, etc. [154]. To purify protease Diethylaminoethyl cellulose (DEAE-C)
column chromatography, gel filtration technique, sodium dodecyl sulfate-polyacrylamide gel
electrophoresis (SDS-PAGE) is used. Among these techniques, DEAE-C column
chromatography is used tremendously in the past few years to reduce the number of steps
involved in purification [155,156].
Lipase versatility makes this a preferable choice for potential application in the
pharmaceutical and cosmetics industries. After the strain selection, improvement, and media
optimization, fermentation technology was carried out. SmF is mostly used to produce lipase,
SSF can also be used rarely. Both SMF and SSF are utilized for the production of largescale
bioactive compounds [157]. The nitrogen and carbon concentration, temperature, pH, and
dissolved oxygen concentration may influence lipase production [158].
In some cases, immobilized cell culture is also used, but the submerged fermentation is
a technique that is employed for the controlled microorganism cultivation in the liquid substrate
and target for high yield formation. Recent studies show that the preferred choice for lipase
fermentation is SSF because it is cost-effective, simple, easy purification, and eco-friendly
[159]. Purification is used to evaluate the enzyme's stability, activity, and commercial value.
There are so many techniques for purifying the enzyme-like chromatography, precipitation,
flocculation [160]. In this technique, pre-purification steps like ultra-purification and so forth
are needed. To overcome the above issues, numerous research works are carried out
continuously by industrial researchers. Recent technologies applied for lipase purification are
immuno-purification, column chromatography, and hydrophobic interaction chromatography.
Hydrophobic interaction chromatography is considered preferable among these techniques
because the lipase enzyme is hydrophobic, so lipase purification is achieved by hydrophobic
interaction chromatography [161].
Esterase can degrade industrial pollutants, so the enzyme needs to be produced
immensely. Fermentation was carried after the preparation of the sample. There are three
techniques involved in esterase fermentation. They are submerged, solid-state, and slurry state
[162]. Among the above-mentioned three methods, SmF supplement with olive oil and maltose
gives high production of esterase enzyme [163]. These crude enzymes are purified using
several techniques to obtain the maximum amount of purified esterase enzyme [164]. This
purification step includes various processes like ammonium sulfate precipitation, dialysis, acid
hydrolysis, and chromatography like gel filtration chromatography, column chromatography
[165].

8. High throughput enzyme assay

Metagenomics is a technique that studies most of the microbes and the enzyme related
to the microbes isolated from an environment. It is a powerful technique for novel gene
discovery and provides an opportunity for innovative biotechnological process development.
Recently, it was used in the discovery of novel biocatalysts. Up to 99% of the uncultured
bacteria were explored using this technique. Industries depend highly on enzymes for the
catalytic process because of the increased reaction rate to several folds. In addition to this, it
https://biointerfaceresearch.com/ 3459
 https://doi.org/10.33263/BRIAC123.34463471

helps in finding superior catalysts for numerous industrial applications [166]. Metagenomics
is involved with two ways of approaches for screening the biomolecules. They are sequence-
based and functional-based screening of metagenomic libraries. It surpasses the technique that
needed the bacteria to be isolated and cultivated. The genomic DNA was isolated directly from
samples. It was found to be effective in tapping the metabolic and genetic diversity of complex
ecosystems. It helps in the identification of bioactive molecules and novel enzymes [167].
The new approach for efficient amylase activity detection was studied. Glucose oxidase
was commonly used in glucose monitoring systems because it is highly specific to glucose. It
works based on the principle that the glucose oxidase and the products of amylase interact in
the presence of O2, which results in the formation of gluconic acid and H2O2. Later, the
produced H2O2 can be detected using a kit (Phenol, 4-aminoantipyrine, and peroxidase) and
results in red color formation. Further, the absorbance will be measured. Due to the reliability
& applicability of this method, the α-amylase activity can successfully determine [168].
The transcriptional regulator-based biosensors can specifically interact with their
effectors and produce measurable signals by using the specific products from enzymatic
reactions. The Genetic enzyme screening system, massive libraries were utilized by a biosensor
to find novel enzymes. The Cellobiose detectible genetic enzyme screening system, a whole-
cell biosensor, can detect cellulolytic activity and reported that it was a powerful tool because
of the high sensitivity in the presence of Cellulosic substrates. The biosensor consists of the
regulator and reporter fluorescent protein for detecting the cellulase activity in live cells [169].
The energy transfer-based biosensors were most commonly used to detect proteolytic
activity detection in real-time, and they are highly sensitive & wash-free. As a result of long-
range dipole-dipole interactions, energy transfer will occur. So, it can be used in in-vivo
conditions. They are used in the early diagnosis of severe diseases [170].
Various studies on lipase enzyme activity prediction were made in recent years. Among
those, the lipase activity determined by the aggregation-induced emission-based fluorescence
turn-on assay is very notable. The tertraphenylethylene (TPE) derivative with -COOC6H13 can
be hydrolyzed into TPE-COOH, which aggregates easily and has low solubility. A novel
fluorescence turns on the probe, which has the ability to detect aggregation-induced emission
to visualize the lipase activities. It has high sensitivity and has the application for real-time
detection of lipase activity [171].
The enzyme works more in the activities of all organisms, from cell division & growth
to aging & death. Abnormal activity of enzymes leads to dysfunction and disease. So, it has
great significance in the diagnosis and also in the disease treatment. An ultrasensitive technique
for detecting T4 polynucleotide kinase (T4 PNK) and telomerase has significant importance. It
works based on the primers continuously extending to produce more activation regions,
resulting in the initiation of DNase activity of the CRISPR/Cas12a. Then, fluorescent assay
ultra-sensitively or visually detects the T4 PNK and telomerase activity. When compared to
other methods of detection of these enzymes, it was ultrasensitive, fast, and visual detection of
enzyme activity is feasible [172].
The enzyme activity analysis is needed for understanding the pathways associated with
disease at the molecular biology level. The construction and implementation of nano kits were
helpful in the cost-effective analysis of enzyme activity within the living cells. A nanometer-
sized capillary tube containing the working electrode and the kit components has to be inserted

https://biointerfaceresearch.com/ 3460
 https://doi.org/10.33263/BRIAC123.34463471

into it for protein analysis. For enzyme activity analysis, reversed electrochemical pumping
can be used to confine the targeted organelle in the nanocapillary tip [173].
Recent advancements in chemical proteomic methods facilitate enzyme activity
detection and quantification. The activity-based proximity ligation (ADPL) method was used
to detect and quantify the enzyme activity in single cells. The ADPL platform uses direct
conjugation formats, which enables amplification and quantification of active enzymes, even
in subcellular resolution [174].
Matrix metalloproteinases-9 (MMP 9) play a vital role in tumor metastasis & cancer
cell invasion. It is commonly used as a potential biomarker for different cancers such as breast
cancer, cervical cancer, bone tumor, hepatocellular carcinoma, pancreatic cancer, lung cancer,
ovarian cancer, and Osteosarcoma. For the detection of MMP 9, researchers developed an
electrode-free electrochemical biosensor. Methylene Blue (MB) was conjugated to the N-
terminal of this specific substrate peptide and was immobilized on the Au electrodes. In the
presence of MMP 9, it will cleave this peptide. This cleavage results in the release of
electroactive MB peptide and changes the electrical tunneling current. It can be used in the
detection of MMP 9 [175].

9. Conclusions

There is a perpetual hunt for enzymes as it is widely used, particularly in industries.

Enzymes are widely used in key fields, such as pharmaceuticals, food processing, and even as
substitutes for chemical additives. This review strives to overview amylase, cellulase, protease,
lipase, and esterase and their industrial and clinical application. For this review, fonts are
collected from various supreme journals and publications. Sources used and the method of
production is also described in this review. The reason for using enzymes is that it is a
biocatalyst without any side effects and reduces time consumption. Industrial consumers use it
every day to create marketable products. Industries are in need of enzymes because of their low
processing time. But the industries are facing difficulties in enzyme production and its
purification. The recent advanced methods for enzyme production and purification discussed
in this review may help researchers and industrialists choose the best, most effective, and
suitable techniques for their specific approaches. Nowadays, there is a necessity for new and
more versatile enzymes. For the research purpose, this review will give full thought about
enzyme production from the microorganism. This allows us to understand the future
perspective of enzymes and their importance in the industrials sectors. The further year should
see a lot of trends in enzyme and its application.

Funding

This review received no external funding.

Acknowledgments

The author gratefully acknowledges the Bioprospecting Research Laboratory, Bannari Amman
Institute of technology, for providing an enormous resource and peaceful environment to
successfully complete this review.

https://biointerfaceresearch.com/ 3461
 https://doi.org/10.33263/BRIAC123.34463471

Conflicts of Interest

The authors declare no conflict of interest.

Reference

1. Kermasha, S.; Michael N. A. E. Enzyme. In Enzyme, Novel Biotechnological Approaches for the Food
Industry, 3rd Edition, Editors: Selim Kermasha, Michael N.A. Eskin, Academic press, New York 2021, 5, 15-
44, https://doi.org/10.1016/B978-0-12-800217-9.00002-2.
2. Matamá, T.; Cavaco-Paulo, A. Enzymatic modification of polyacrylonitrile and cellulose acetate fibres for
textile and other applications. Adv. Text. Biotechnol. 2010, 5, 98–131,
https://doi.org/10.1533/9780857090232.2.98.
3. Roy, C.; Asim, K. Introduction to enzymes. Sustainable Technologies for Fashion and Textiles, 4th ed.;
Elsevier Ltd: West Bengal, India 2019, 75-90, https://doi.org/10.1016/B978-0-08-102867-4.00004-9.
4. Rigoldi, F.; Donini, S.; Redaelli, A.; Parisini, E.; Gautieri, A. Review: Engineering of thermostable enzymes
for industrial applications. APL Bioeng. 2018, 2, 011501-17, https://doi.org/10.1063/1.4997367.
5. Silva, C.; Cavaco-Paulo, A.; Nierstrasz, V. A. Enzymatic hydrolysis and modification of core polymer fibres
for textile and other applications. Adv. Text. Biotechnol. 2010, 4, 77–97,
https://doi.org/10.1533/9780857090232.2.77.
6. Robinson, P. K. Enzymes: principles and biotechnological applications. Essays Biochem. 2015, 59, 1–41,
https://doi.org/10.1042/BSE0590001.
7. Petrovic, D.; Risso, V. A.; Kamerlin, S. C. L.; Sanchez-Ruiz, J. M. Conformational dynamics and enzyme
evolution, J. R. Soc. Interface 2018, 15, 1-18, https://doi.org/10.1098/rsif.2018.0330.
8. Kumar, J.; Pandey, A.; Singh, S. P. An introduction to enzyme structure dynamics and enzyme catalysis.
Biomass, Biofuels, Biochem. 2020, 1, 3–10, https://doi.org/10.1016/b978-0-12-819820-9.00001-6.
9. Bhatia, S. Introduction to enzymes and their applications. Introd. to Pharm. Biotechnol. 2018, 2, 1-29,
https://doi.org/10.1088/978-0-7503-1302-5ch1.
10. Kani, P.; Hashemi, T.; Amir Jouya, K.; Abdulkarim Yasin, N.; Nadir, M. Q. S.; Abbas, A. F.; Mohammad
Y.; Bing, K.; Rizwan, H. S.; Ali, A. Enzyme immobilization onto the nanomaterials: Application in enzyme
stability and prodrug-activated cancer therapy. Int. J. Biol. Macromol. 2020, 143, 665-676,
https://doi.org/10.1016/j.ijbiomac.2019.12.064.
11. Vlieghe, P.; Lisowski, V.; Martinez, J.; Khrestchatisky, M. Synthetic therapeutic peptides: science and
market. Drug Discov. Today 2010, 15, 40–56, https://doi.org/10.1016/j.drudis.2009.10.009.
12. Aldridge, S. Industry backs biocatalysis for greener manufacturing. Nat. Biotechnol. 2013, 31, 95–96,
https://doi.org/10.1038/nbt0213-95.
13. Araújo, R.; Casal, M.; Cavaco-Paulo, A. Application of enzymes for textile fibres processing. Biocatal.
Biotransformation 2008, 26, 332–349, https://doi.org/10.1080/10242420802390457.
14. Lakshmi, S. S.; Mahesh, C. H.; Gayatri, K.; Manisha, P.; Aishwarya, K. Statistical optimization of amylase
production and its purification from a palm wine isolate Bacillus sp., Q-164. Biocatal. Agric. Biotechnol.
2020, 29, 101-820, https://doi.org/10.1016/j.bcab.2020.101820.
15. Bhatt, K.; Lal, S. R.; Joshi, B. Bioconversion of agriculture wastes to produce α- amylase from Bacillus
velezensis KB 2216: Purification and characterization. Biocatal. Agric. Biotechnol. 2020, 28, 101-703,
https://doi.org/10.1016/j.bcab.2020.101703.
16. Božić, N.; Rozeboom, H. J.; Lončar, N.; Slavić, M. S.; Janssen, D. B.; Vujčić, Z. Characterization of the
starch surface binding site on Bacillus paralicheniformis α-amylase. Int. J. Biol. Macromol. 2020, 165, 1529–
1539, https://doi.org/10.1016/j.ijbiomac.2020.10.025.
17. Prasad, S.; Roy, I. Converting Enzymes into Tools of Industrial Importance. Recent Pat. Biotechnol. 2017,
12, 33–56, https://doi.org/10.2174/1872208311666170612113303.
18. Li, Y.; Dandan, T.; Shi, Z.; Yaning, W.; Xu, Y.; Enbo, C.; Bo, H. Preparation of porous starch by α-amylase-
catalyzed hydrolysis under a moderate electric field. Lwt 2020, 137, 1104-49,
https://doi.org/10.1016/j.lwt.2020.110449.
19. Okal, E. J.; Aslam, M. M.; Karanja, J. K.; Nyimbo, W. J. Mini review: Advances in understanding regulation
of cellulase enzyme in white-rot basidiomycetes. Microb. Pathog. 2020, 147, 104-410,
https://doi.org/10.1016/j.micpath.2020.104410.

https://biointerfaceresearch.com/ 3462
 https://doi.org/10.33263/BRIAC123.34463471

20. Yang, L.; Wei, F.; Huan, Z.; Min, Z.; Zheng, Y.; Lishi, J.; Xin, L. Synergistic effect of ionic liquid and
surfactant for enzymatic hydrolysis of lignocellulose by Paenibacillus sp. LLZ1 cellulase. Biomass and
Bioenergy 2020, 142, 1057-60, https://doi.org/10.1016/j.biombioe.2020.105760.
21. Zou, G. B.; Dapeng, W.; Ying, Z.; Sichi, X.; Meili, Y.; Zhanshan, W.; Yinmei, Z. Z. Alleviating product
inhibition of Trichoderma reesei cellulase complex with a product-activated mushroom endoglucanase.
Bioresour. Technol. 2021, 319, 1241-19, https://doi.org/10.1016/j.biortech.2020.124119.
22. Gupta, R.; Beg, Q.; Lorenz, P. Bacterial alkaline proteases: Molecular approaches and industrial applications.
Appl. Microbiol. Biotechnol. 2002, 59, 15–32, https://doi.org/10.1007/s00253-002-0975-y.
23. Antonia, M.; Colabone, P.; Baldo, C. Lipase: properties,functions,and Food Applications. In Microbial
Enzyme Technology in Food Applications, 1st edition, Editor:1 Ramesh C Ray, Editor 2: Cristina M Rosell,
Taylor & Francis, Boca Raton, United States 2015, 12, 216–242, https://doi.org/10.1201/9781315368405.
24. Treichel, H.; de Oliveira, D.; Mazutti, M.A.; Marco, D. L.; Vladimir Oliveira, J. A Review on Microbial
Lipases Production. Food Bioprocess Technol 2010, 3, 182–196, https://doi.org/10.1007/s11947-009-0202-
2.
25. Singh, L.; Sharma, G.; Awasthi, G.; Kumar, L.; Ali, M. I.; Moin, S. Screening, isolation and identification of
thermophilic esterase enzyme isolated from Rhodococcus sp: LKE-021. J. Pure Appl. Microbiol. 2019, 13,
1855–1861, https://doi.org/10.22207/JPAM.13.3.63.
26. Bornscheuer, U. T. Microbial carboxyl esterases: Classification, properties and application in biocatalysis.
FEMS Microbiol. Rev. 2002, 26, 73–81, https://doi.org/10.1016/S0168-6445(01)00075-4.
27. De Luca, V.; Mandrich, L. Lipases/esterases from extremophiles: main features and potential
biotechnological applications. In Physiological and Biotechnological Aspects of Extremophiles, Edition:1,
Editors: Sharma, Richa Salwan, Vivek, Elsiver INC, India 2020, 169-181, https://doi.org/10.1016/b978-0-
12-818322-9.00013-7.
28. Lagarde, D. N.; Hong, K. R.; Gilles, W.; Denis, R.; Jean, L.; Hills, G. V.; Thomas, L. F. High-throughput
screening of thermostable esterases for industrial bioconversions. Org. Process Res. Dev. 2002, 6, 441–445,
https://doi.org/10.1021/op020019h.
29. Boyce, S.; Tipton, K. F. Enzyme Classification and Nomenclature. Food Biochem. Food Process. 2007, 1,
135–154, https://doi.org/10.1002/9780470277577.ch6.
30. Angel, T.; Martíneza, F.; Ruiz-Dueñas, J.; Susana, C.; Ana, S.; Dolores, L.; Henrik, L.; Jesper, V.; Morten,
T.; Owik, M. H.; Martin, H. Oxidoreductases on their way to industrial biotransformations. Biotechnol. Adv.
2017, 35, 815-831, https://doi.org/10.1016/j.biotechadv.2017.06.003.
31. Yadav, P.; Sangeeta, K.; Yadav, K.; Dinesh, D.; Yadav, S. Pectin lyase: A review. Process Biochem.
Biochem. 2009, 44, 1–10, https://doi.org/10.1016/j.procbio.2008.09.012.
32. Cuesta, S. M.; Rahman, S. A.; Thornton, J. M. Exploring the chemistry and evolution of the isomerases. Proc.
Natl. Acad. Sci. U. S. A. 2016, 113, 1796–1801, https://doi.org/10.1073/pnas.1509494113.
33. Martinez Cuesta, S.; Furnham, N.; Rahman, S. A.; Sillitoe, I.; Thornton, J. M. The evolution of enzyme
function in the isomerases. Current Opinion in Structural Biology 2014, 26, 121-130,
http://dx.doi.org/10.1016/j.sbi.2014.06.002.
34. Samanta, S. T.; Shuzo, D.; Louis, M. F.; Paulette, M.; Yohei, K.; Hisamori, L.; Rich, B.; Ronald J. L.; Vonne,
G.Y.; Neamati, N. Expression of protein disulfide isomerase family members correlates with tumor
progression and patient survival in ovarian cancer. Oncotarget 2017, 8, 103543–103556,
https://doi.org/10.18632/oncotarget.21569.
35. Neifar, S. H.; Hajer, B. M.; Sonia, M.; Monia, B.; Khelifa, I.; Adel, H. J.; Bassem, B. D.; Amel, B. S. A novel
thermostable and efficient Class II glucose isomerase from the thermophilic Caldicoprobacter algeriensis:
Biochemical characterization, molecular investigation, and application in High Fructose Syrup production.
Int. J. Biol. Macromol. 2019, 129, 31–40, https://doi.org/10.1016/j.ijbiomac.2019.01.150.
36. Cornish B. A. Current IUBMB recommendations on enzyme nomenclature and kinetics. Perspect. Sci. 2014,
1, 74–87, https://doi.org/10.1016/j.pisc.2014.02.006.
37. Holliday, G. L.; Rahman, S. A.; Furnham, N.; Thornton, J. M. Exploring the biological and chemical
complexity of the ligases. J. Mol. Biol. 2014, 426, 2098–2111, https://doi.org/10.1016/j.jmb.2014.03.008.
38. Manubolu, M.; Goodla, L.; Pathakoti, K.; Malml, K. Enzymes as direct decontaminating agents-mycotoxins.
Enzym. Hum. Anim. Nutr. Princ. Perspect. 2018, 16, 313–330, https://doi.org/10.1016/B978-0-12-805419-
2.00016-2.
39. Porto, S. V.; Luciana, K.; Susan, G. B. P.; Maria, G.; Linsingen, V. T.; Matheus, L. J.; Nelson, V. D.; Kim,

https://biointerfaceresearch.com/ 3463
 https://doi.org/10.33263/BRIAC123.34463471

V.; Jéssica, A. S.; Carlos, R. Classification of enzymes and catalytic properties. Biomass, Biofuels, Biochem.
2020, 2, 11–30, https://doi.org/10.1016/b978-0-12-819820-9.00002-8.
40. Patricia, J.; Khushbu, P.; Dinesh, R. Disorder : Carnitine-acylcarnitine translocase deficiency. In A Quick
Guide to Metabolic Disease Testing Interpretation, 2nd Edition, Editors: Patricia Jones, Khushbu Patel,
Dinesh Rakheja, Elsevier, British Library Cataloguing-in-Publication Data, United Kingdom 2020, 133–136,
https://doi.org/10.1016/B978-0-12-816926-1.00025-0.
41. Hammami, A.; Fakhfakh, N.; Abdelhedi, O.; Nasri, M.; Bayoudh, A. Proteolytic and amylolytic enzymes
from a newly isolated Bacillus mojavensis SA: Characterization and applications as laundry detergent
additive and in leather processing. Int. J. Biol. Macromol. 2018, 108, 56–68,
https://doi.org/10.1016/j.ijbiomac.2017.11.148.
42. Sen, S. K.; Jana, A.; Bandyopadhyay, P.; Das Mohapatra, P.K.; Raut, S. Thermostable amylase production
from hot spring isolate Exiguobacterium sp: A promising agent for natural detergents. Sustain. Chem. Pharm.
2016, 3, 59–68, https://doi.org/10.1016/j.scp.2016.04.002.
43. Wang, G.; Xiaofei, K.; Ren, C.; Xiulian, Y.; Geng, S.; Xie, M.; Qiuju, W.; Hua, B. Molecular cloning and
characterization of a novel -Amylase from antarctic sea ice bacterium pseudoalteromonas sp. M175 and its
primary application in detergent. Biomed Res. Int. 2018, 2018, 1-16, https://doi.org/10.1155/2018/3258383.
44. Al-Ghanayem, A. A.; Joseph, B. Current prospective in using cold-active enzymes as eco-friendly detergent
additive. Appl. Microbiol. Biotechnol. 2020, 104, 2871–2882, https://doi.org/10.1007/s00253-020-10429-x.
45. Qiang, W. Z.; Yu, C. H.; Hui, F. M.; Jun, W. Y.; Qiao, J. L.; Hai, J. J. A novel high maltose-forming α-
amylase from Rhizomucor miehei and its application in the food industry. Food Chem. 2020, 305, 125-447,
https://doi.org/10.1016/j.foodchem.2019.125447.
46. Khemakhem, B.; El Abed, H.; Chakroun, M.; Fendri, I.; Smaoui, S. Functional effects of ice plant amylases
on cake and bun quality. Food Biosci. 2019, 29, 142–149, https://doi.org/10.1016/j.fbio.2019.04.008.
47. Roth, E.; Christian, M.; Olga, V. T.; Johan, P. B.; Waterman, S.; Jitka, A.; Antonio, M.; Li-Tianqi, C.;
Andersen, G.; Davies, J.; Wilson, K. S. Structural and functional characterization of three novel fungal
amylases with enhanced stability and ph tolerance. Int. J. Mol. Sci. 2019, 20, 1–15,
https://doi.org/10.3390/ijms20194902.
48. Cripwell, R. A.; Van Zyl W. H.; Viljoen-Bloom, M. Fungal Biotechnology: Fungal Amylases and Their
Applications. In Reference Module in Life Sciences, 1st edition, Editor: Shi Pengjun, Elsevier Ltd.,
Stellenbosch, South Africa 2020, 1-13, https://doi.org/10.1016/b978-0-12-809633-8.21082-0.
49. Kumar D.; Singh, V. Dry ‑ grind processing using amylase corn and superior yeast to reduce the exogenous
enzyme requirements in bioethanol production. Biotechnol. Biofuels 2016, 9, 1–12,
https://doi.org/10.1186/s13068-016-0648-1.
50. Wood, N. M.; Ian, P. C.; Wilson, P.; David, R. R.; Robertson, K. W.; James, A. W. Ethanol from a biorefinery
waste stream : Saccharification of amylase, protease and xylanase treated wheat bran. FOOD Chem. 2015,
198, 125-131, https://doi.org/10.1016/j.foodchem.2015.09.108.
51. Vinod Kumar, N.; Rani, M. E.; Gunaseeli, R.; Kannan, N. D. Paper pulp modification and deinking efficiency
of cellulase-xylanase complex from Escherichia coli SD5. Int. J. Biol. Macromol. 2018, 111, 289–295,
https://doi.org/10.1016/j.ijbiomac.2017.12.126.
52. Bajaj, M.; Priyanka, R. Cellulase and xylanase synergism in industrial biotechnology. Appl. Microbiol.
Biotechnol. 2019, 1, 1-14, https://doi.org/10.1007/s00253-019-10146-0.
53. Wang, X.; Qiang, L.; Shanshan, Y.; Guihua, C.; Jiachuan, J.; Ni, Y. Recycling cellulase towards industrial
application of enzyme treatment on hardwood kraft-based dissolving pulp. Bioresour. Technol. 2016, 212,
160–163, https://doi.org/10.1016/j.biortech.2016.04.048
54. Gu, M.; Fang, H.; Gao, Y.; Su, T.; Niu, Y.; Yu, L. Characterization of enzymatic modified soluble dietary
fiber from tomato peels with high release of lycopene. Food Hydrocoll. 2020, 99, 105-321,
https://doi.org/10.1016/j.foodhyd.2019.105321.
55. Ademakinwa A. N.; Agboola, F. K. Kinetic and thermodynamic investigations of cell-wall degrading
enzymes produced by Aureobasidium pullulans via induction with orange peels : application in lycopene
extraction. Prep. Biochem. Biotechnol. 2019, 1–12, https://doi.org/10.1080/10826068.2019.1650375.
56. Cheng, Y.; Li, Z.; Xianmei, H.; Li, C.; Zhaofeng, L.; Gu, Z. Title: Characterisation of Physicochemical and
Functional Properties of Soluble Dietary Fibrefrom Potato Pulp Obtained by Enzyme-assisted Extraction. Int.
J. Biol. Macromol. 2017, 101, 1-42, https://doi.org/10.1016/j.ijbiomac.2017.03.156.
57. Barzkar, N. Marine microbial alkaline protease: recent developments in biofilm n ideal choice for industrial

https://biointerfaceresearch.com/ 3464
 https://doi.org/10.33263/BRIAC123.34463471

application. Int. J. Biol. Macromol. 2020, 161, 1216–1229, https://doi.org/10.1016/j.ijbiomac.2020.06.072.

58. Fang, J.; Zhen, Y.; Yang, C. Z.; Juan, D. G. C. Keratinolytic protease : a green biocatalyst for leather industry.
Appl. Microbiol. Biotechnol. 2017, 101, 7771–7779, https://doi.org/10.1007/s00253-017-8484-1.
59. Cao, H.; Shan, S.; Jinzhi, L. F.; Wang, K. L.; Yanchun, L.; Yu, L.; Liu, B. Improving characteristics of
biochar produced from collagen-containing solid wastes based on protease application in leather production.
Waste Manag. 2020, 105, 531–539, https://doi.org/10.1016/j.wasman.2020.02.043.
60. Gurumallesh, P.; Alagu, B.; Kamalini, R.; Muthusamy, S. International Journal of Biological
Macromolecules A systematic reconsideration on proteases. Int. J. Biol. Macromol. 2019, 128, 254–267,
https://doi.org/10.1016/j.ijbiomac.2019.01.081.
61. Philipps, W. P. Proteases-human food. In Enzyme in Human and Animal Nutrition, 1st Edition, Kumar, Carlos
Simões Nunes and Vikas, Elsevier Inc., United States 2018, 267-277, https://doi.org/10.1016/B978-0-12-
805419-2.00013-7.
62. Guo, H.; Yujie, T.; Tao, Y.; Peng, W.; Yaru, R.; Yaxin, Y.; Bin, L. High-level expression and characterization
of a novel aspartic protease from Talaromyces leycettanus JCM12802 and its potential application in juice
clarification. Food Chem. 2019, 281, 197–203, https://doi.org/10.1016/j.foodchem.2018.12.096.
63. Ismail, A. R.; Baek, K. H. Lipase immobilization with support materials, preparation techniques, and
applications: Present and future aspects. Int. J. Biol. Macromol. 2020, 163, 1624–1639,
https://doi.org/10.1016/j.ijbiomac.2020.09.021.
64. Nomaguchi, Y.; Tatsuhiro, M.; Liang, T.; Yue, Y.; Tomoko, A.; Tanaka, T. Comprehensive analysis of
triacylglycerol lipases in the oleaginous diatom Fistulifera solaris JPCC DA0580 with transcriptomics under
lipid degradation. J. Biosci. Bioeng. 2018, 1-8, https://doi.org/10.1016/j.jbiosc.2018.03.003.
65. Yu, Z. Z.; Huiwen, F.; Xuanhe, L.; Xu, G.; Qiucui, Y.; Tingting, L. X. Immobilization of esterase SulE in
cross-linked gelatin/chitosan and its application in remediating soils polluted with tribenuron-methyl and
metsulfuron-methyl. Process Biochem. 2020, 98, 217–223, https://doi.org/10.1016/j.procbio.2020.08.014.
66. Tsuboi, K.; Shun, T.; Takumi, Y. T.; Kitamoto, H. High-throughput method for the evaluation of esterase
activity in soils. J. Microbiol. Methods 2018, 146, 22–24, https://doi.org/10.1016/j.mimet.2018.01.009.
67. Maester, D. M.; Thaís, C. P.; Mariana, R. S.; Machado, E. G.; Balan, A. G.; Eliana, L. Characterization of
EST3 : a metagenome-derived esterase with suitable properties for biotechnological applications. Appl.
Microbiol. Biotechnol. 2016, 100, 5815–5827, https://doi.org/10.1007/s00253-016-7385-z.
68. Sanati, A. J.; Mahsa, R.; Keyvan, K.; Fathallah, K.; Mashid, S. S. M. A review on recent advancements in
electrochemical biosensing using carbonaceous nanomaterials. Microchim. Acta 2019, 186, 186-773,
https://doi.org/10.1007/s00604-019-3854-2.
69. Kumar, S. S.; Sabu, A. Fibrinolytic enzymes for thrombolytic therapy. Advances in Experimental Medicine
and Biology 2019, 1148, 345-381, https://doi.org/10.1007/978-981-13-7709-9_15.
70. Vachher, M.; Sen, A.; Kapila, R.; Nigam, A. Microbial therapeutic enzymes: A promising area of
biopharmaceuticals. Current Research in Biotechnology 2021, 3, 195-208,
https://doi.org/10.1016/j.crbiot.2021.05.006.
71. Logie, J. J.; Cox, M.; Sharkey, J.; Williams, A. A multidisciplinary approach to an unusual cause of
hyperamylasaemia. BMJ Case Reports 2015, 2015, 1-3, https://doi.org/10.1136/bcr-2015-209780.
72. Abeleda, H. E. P.; Javier, A. P.; Murillo, A. Q. M.; Baculi, R. Q. Alpha-amylase conjugated biogenic silver
nanoparticles as innovative strategy against biofilm-forming multidrug resistant bacteria. Biocatal. Agric.
Biotechnol. 2020, 29, 1017-84, https://doi.org/10.1016/j.bcab.2020.101784.
73. Mojbafan, M. A.; Zohreh, A.; Mahsa, M. M.; Mahdi, Y. P. L.; Bagher, E. H.; Azadehkbar, F.; Mojtaba, F.
Liver alpha-amylase gene expression as an early obesity biomarker. Pharmacol. Reports 2017, 69, 229–234,
https://doi.org/10.1016/j.pharep.2016.11.001.
74. Bhattacharjee, M.; Middya, S.; Escobedo, P.; Chaudhuri, J.; Bandyopadhyay, D.; Dahiya, R. Microdroplet
based disposable sensor patch for detection of α-amylase in human blood serum. Biosens. Bioelectron. 2020,
165, 1123-33, https://doi.org/10.1016/j.bios.2020.112333.
75. Wu, W. K.; Famure, O.; Li, Y.; Kim, S. J. Delayed graft function and the risk of acute rejection in the modern
era of kidney transplantation. International society of Nephrolog, 2015, 1, 1–8.,
https://doi.org/10.1038/ki.2015.190.
76. Comai, G. B.; Olga, C.; Vania, C.; Valeria, A.; Andrea, B.; Seidju, C.; Irene, C.; Maria, M.; Gaetano, L. A.
Increase in Serum Amylase and Resistive Index After Kidney Transplant Are Biomarkers of Delayed Graft
Function. In-vivo 2018, 402, 397–402, https://doi.org/10.21873/invivo.11252.

https://biointerfaceresearch.com/ 3465
 https://doi.org/10.33263/BRIAC123.34463471

77. Pinos, N.; Moreno-Merino, S.; Congregado, M. Phytobezoar by aloe vera as long term complication after
oesophagectomy resolved using cellulase. Int. J. Surg. Case Rep. 2015, 13, 37–39,
https://doi.org/10.1016/j.ijscr.2015.05.008.
78. Reyes-Mondragón, A. L.; Canel-Paredes, A.; Martìnez-Granados, R. J.; Salazar-Mejía, C. E.; Hernández-
Barajas, D.; Vidal-Gutiérrez, O. Bezoar as a cause of intestinal obstruction as the first manifestation of
duodenal adenocarcinoma. Med. Clin. Pract., 2020, 3, 1001-44,
https://doi.org/10.1016/j.mcpsp.2020.100144.
79. Nguyen, S. N.; Ngo, T. C.; Tran, T. T.; Nguyet, N. M.; Man Le, V. V. Pasta from cellulase-treated wheat
bran and durum semolina: Effects of vital gluten addition and/or transglutaminase treatment. Food Biosci.
2020, 38, 1007-82, https://doi.org/10.1016/j.fbio.2020.100782.
80. Brown, L.; Leck, K. A.; Gichangi, M.; Burton, M. J.; Denning, D. W. The global incidence and diagnosis of
fungal keratitis. Lancet Infect. Dis. 2020, 3099, 1–9, https://doi.org/10.1016/S1473-3099(20)30448-5.
81. Abjani, F.; Khan, N. A.; Jung, S. Y.; Siddiqui, R. Status of the effectiveness of contact lens disinfectants in
Malaysia against keratitis-causing pathogens. Exp. Parasitol. 2017, 183, 187–193,
https://doi.org/10.1016/j.exppara.2017.09.007.
82. Petkova, P.; Francesko, A.; Perelshtein, I.; Gedanken, A.; Tzanov, T. Simultaneous sonochemical-enzymatic
coating of medical textiles with antibacterial ZnO nanoparticles. Ultrason. Sonochem. 2016, 29, 244–250,
https://doi.org/10.1016/j.ultsonch.2015.09.021.
83. Jabeen, A. R.; Brandon, H.; Soleiman, A.; Salman, D.; Naeema, A. B.; Sinan, A. Z. S.; Effect of Enzymatic
pre-treatment of microalgae extracts on their anti-tumor activity. Biomed. J. 2017, 40, 339–346,
https://doi.org/10.1016/j.bj.2017.10.003.
84. Kunamneni, A.; Ogaugwu, C.; Goli, D. Enzymes as therapeutic agents. Enzym. Hum. Anim. Nutr. Princ.
Perspect. 2018, 15, 301–312, https://doi.org/10.1016/B978-0-12-805419-2.00015-0.
85. Craik, C. S.; Page, M. J.; Madison, E. L. Proteases as therapeutics. Biochemical journal 2011, 16, 1-16,
https://doi.org/10.1042/BJ20100965.
86. Cogo, F.; Williams, R.; Burden, R. E.; Scott, C. J. Application of nanotechnology to target and exploit tumour
associated proteases. Biochimie 2019, 166, 112–131, https://doi.org/10.1016/j.biochi.2019.04.021.
87. Tyndall, J. D. A.; Huston, W. M.; Gamble, A. B. Proteases and protease inhibitors in infectious diseases.
Medicina Clinica Practica 2017, 38, 1295-1331, https://doi.org/10.1002/med.21475.
88. Jawed, A. S.; Kohli, G.; Sumera, S.; Haque, A.; Prasad, S.; Paul, R. D. Therapeutic role of lipases and lipase
inhibitors derived from natural resources for remedies against metabolic disorders and lifestyle diseases.
South African J. Bot. 2018, 01999, 1–8, https://doi.org/10.1016/j.sajb.2018.04.004.
89. Rajan, L.; Palaniswamy, D.; Mohankumar, S. K. Targeting Obesity with plant-derived pancreatic lipase
inhibitors: A comprehensive review. Pharmacol. Res. 2020, 155, 104–681,
https://doi.org/10.1016/j.phrs.2020.104681.
90. Matsumae, H.; Furui, M.; Shibatani, T. Lipase-catalyzed asymmetric hydrolysis of 3-phenylglycidic acid
ester, the key intermediate in the synthesis of diltiazem hydrochloride. Journal of Fermentation and
Bioengineering 1993, 75, 93-98, https://doi.org/10.1016/0922-338X(93)90216-U.
91. Vishnoi, N.; Dixit, S.; Mishra, J. Microbial Lipases and Their Versatile Applications. Microb. Enzym. Roles
Appl. Ind. 2020, 8, 207–230, https://doi.org/10.1007/978-981-15-1710-5_8.
92. Gil-ordóñez, A.; Martín-fontecha, M.; Ortega-gutiérrez, S.; López-rodríguez, M. L. Monoacylglycerol lipase
(MAGL) as a promising therapeutic target. Biochem. Pharmacol. 2018, 1, 1-66,
https://doi.org/10.1016/j.bcp.2018.07.036.
93. Narasimhan, D. L.; Macdonald, J.; Brim, R.; Ko, M.; Landry, D. W.; Woods, J. H.; Sunahara, R. K.; Zhan,
C. Thermostable Variants of Cocaine Esterase for Long-Time Protection against Cocaine Toxicity. Molecular
Pharmacology 2009, 75, 318-323, https://doi.org/10.1124/mol.108.049486.
94. Zheng, Q.; Zhang, G. Application of leukocyte esterase strip test in the screening of periprosthetic joint
infections and prospects of high-precision strips. Arthroplasty 2020, 2, 34-70, http://doi.org/10.1186/s42836-
020-00053-5.
95. Lai, O. M.; Lee, Y. Y.; Phuah, E. T.; Akoh, C. C. Lipase/Esterase: Properties and industrial applications. In
Encyclopedia of Food Chemistry, 1st edition, Editors: Beddows, Caitlin, Elsevier, United States 2018, 158-
167, https://doi.org/10.1016/B978-0-08-100596-5.21640-5.
96. Swamy, P.; Govindaswamy, V. Therapeutical properties of ferulic acid and bioavailability enhancement
through feruloyl esterase. J. Funct. Foods 2015, 17, 657–666, https://doi.org/10.1016/j.jff.2015.06.013.

https://biointerfaceresearch.com/ 3466
 https://doi.org/10.33263/BRIAC123.34463471

97. Shaik, M.; Girija, S. G.; Iswarya, M.; Rajitha, P. Isolation and characterization of bioactive metabolites
producing marine Streptomyces parvulus strain sankarensis-A10. J. Genet. Eng. Biotechnol. 2017, 15, 87–
94, https://doi.org/10.1016/j.jgeb.2017.02.004.
98. Msarah, M. J.; Ibrahim, I.; Hamid, W. S.; Aidil, A. A. Optimisation and production of alpha amylase from
thermophilic Bacillus spp. and its application in food waste biodegradation. Heliyon 2020 6, e041-83,
https://doi.org/10.1016/j.heliyon.2020.e04183.
99. Al-Dhabi, N. A.; Esmail, G. A.; Ghilan, A. K. M.; Arasu, M. V.; Duraipandiyan, V.; Ponmurugan, K. Isolation
and purification of starch hydrolysing amylase from Streptomyces sp. Al-Dhabi-46 obtained from the Jazan
region of Saudi Arabia with industrial applications. J. King Saud Univ. - Sci. 2020, 32, 1226–1232,
https://doi.org/10.1016/j.jksus.2019.11.018.
100. Priyadarshini, S.; Ray, P. Exploration of detergent-stable alkaline α-amylase AA7 from Bacillus sp strain SP-
CH7 isolated from Chilika Lake. Int. J. Biol. Macromol., 2019, 140, 825–832,
https://doi.org/10.1016/j.ijbiomac.2019.08.006.
101. Chakraborty, L. S.; Khopade, A.; Biao, R.; Jian, W.; Liu, X. Y.; Mahadik, K.; Chopade B. Z. Characterization
and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic
Saccharopolyspora sp. A9. J. Mol. Catal. B Enzym., 2011, 68, 52–58,
https://doi.org/10.1016/j.molcatb.2010.09.009.
102. Paul, J. S.; Beliya, E.; Tiwari, S.; Patel, K.; Gupta, N.; Jadhav, S. K. Production of biocatalyst α-amylase
from agro-waste 'rice bran' by using Bacillus tequilensis TB5 and standardizing its production process.
Biocatal. Agric. Biotechnol. 2020, 26, 101-648, https://doi.org/10.1016/j.bcab.2020.101648.
103. Almanaa, T. N.; Vijayaraghavan, P.; Alharbi, N. S.; Kadaikunnan, S.; Khaled, J .M.; Alyahya, S. A. Solid
state fermentation of amylase production from Bacillus subtilis D19 using agro-residues. J. King Saud Univ.
- Sci. 2020, 32, 1555–1561, https://doi.org/10.1016/j.jksus.2019.12.011.
104. Jabin, T.; Naher, K.; Uddin, S. Fermentation optimization of cellulase production from sugarcane bagasse by
Bacillus pseudomycoides and molecular modeling study of cellulase. Curr. Res. Microb. Sci. 2020, 2, 1000-
13, https://doi.org/10.1016/j.crmicr.2020.100013.
105. Li, F. X.; Yingjie, G.; Xiang, S.; Mingxu, S.; Changchao, N.; Yan, D. S.; Anshan, S. Screening of cellulose
degradation bacteria from Min pigs and optimization of its cellulase production. Electron. J. Biotechnol.
2020, 48, 29–35, https://doi.org/10.1016/j.ejbt.2020.09.001.
106. Amadi, O.; Egong, C.; Egong, J.; Nwagu, T.; Okpala, N.; Gloria, O.; Chukwudi, O.; Chukwu, G.; Okolo, C.;
Bartholomew, N.; Agu, R.; Moneke, C.; Anene, N. Process optimization for simultaneous production of
cellulase, xylanase and ligninase by Saccharomyces cerevisiae SCPW 17 under solid state fermentation using
Box-Behnken experimental design. Heliyon 2020, 6, e045-66, https://doi.org/10.1016/j.heliyon.2020.e04566.
107. Hatefi, A.; Makhdoumi, A.; Asoodeh, A.; Mirshamsi, O. Characterization of a bi-functional cellulase
produced by a gut bacterial resident of Rosaceae branch borer beetle, Osphranteria coerulescens (Coleoptera:
Cerambycidae). Int. J. Biol. Macromol. 2017, 103, 158–164, https://doi.org/10.1016/j.ijbiomac.2017.05.042.
108. Shajahan, S.; Moorthy, I. G.; Sivakumar, N.; Selvakumar, G. Statistical modeling and optimization of
cellulase production by Bacillus licheniformis NCIM 5556 isolated from the hot spring, Maharashtra, India,
J. King Saud Univ. - Sci. 2017, 29, 302–310, https://doi.org/10.1016/j.jksus.2016.08.001.
109. Mohapatra, S.; Padhy, S.; Das Mohapatra, P. K.; Thatoi, H. N. Enhanced reducing sugar production by
saccharification of lignocellulosic biomass, Pennisetum species through cellulase from a newly isolated
Aspergillus fumigatus. Bioresour. Technol. 2018, 1, 1-34, https://doi.org/10.1016/j.biortech.2018.01.023.
110. Sadasivan, A.; Al-battashi, H.; Al-akzawi, A.; Annamalai, N.; Gujarathi, A. Waste office paper : A potential
feedstock for cellulase production by a novel strain Bacillus velezensis ASN1. Waste Manag. 2018, 79, 491–
500, https://doi.org/10.1016/j.wasman.2018.08.014.
111. Yang, W. M.; Fanxu, P.; Jiayin, H.; Peng, F.; Fang, M.; Li, C. B. Electronic Journal of Biotechnology
Isolation and identification of a cellulolytic bacterium from the Tibetan pig's intestine and investigation of its
cellulase production. Electronic Journal of Biotechnology 2014, 17, 262–267,
https://doi.org/10.1016/j.ejbt.2014.08.002.
112. Srivastava, N.; Elgorban, A. M.; Mishra, P. K.; Marraiki, N. Environmental Technology & Innovation
Enhance production of fungal cellulase cocktail using cellulosic waste. Environ. Technol. Innov. 2020, 19,
1009-49, https://doi.org/10.1016/j.eti.2020.100949.
113. Ahmad, T. S.; Anshula, G.; Gaganjot, M.; Sheikhan, S. Kaur.; Baljinder, P.; Bilal, A. A. Response surface
optimization of cellulase production from Aneurinibacillus aneurinilyticus BKT-9: An isolate of urban

https://biointerfaceresearch.com/ 3467
 https://doi.org/10.33263/BRIAC123.34463471

Himalayan freshwater. Saudi J. Biol. Sci. 2020, 1-11, https://doi.org/10.1016/j.sjbs.2020.04.036.

114. Mamangkey, J.; Suryanto, D.; Munir, E.; Mustopa, A. Z.; Sibero, M. T.; Mendes, L. W.; Hartanto, A.;
Taniwan, S.; Ek-Ramos, M. J.; Harahap, A.; Verma, A.; Trihatmoko, E.; Putranto, W. S.; Pardosi, L.; Rudia,
La O. A. P. Isolation and enzyme bioprospection of bacteria associated to Bruguiera cylindrica, a mangrove
plant of North Sumatra, Indonesia. Biotechnology Reports 2021, 30, e006-17,
https://doi.org/10.1016/j.btre.2021.e00617.
115. Verma, J.; Pandey, S. Characterization of partially purified alkaline protease secreted by halophilic bacterium
Citricoccus sp. isolated from agricultural soil of northern India. Biocatalysis and Agricultural Biotechnology
2019, 17, 605-612, https://doi.org/10.1016/j.bcab.2019.01.020.
116. Al-Dhabi, N.; Esmail, Galal A.; Ghilan, A. K.; M.; Arasu, M. V. Isolation and screening of Streptomyces sp.
Al-Dhabi-49 from the environment of Saudi Arabia with concomitant production of lipase and protease in
submerged fermentation. Saudi Journal of Biological Sciences 2020, 27, 474-479,
https://doi.org/10.1016/j.sjbs.2019.11.011.
117. Thomas, N. N.; Archana,V.; Shibina, S.; B. T. Edwin. Isolation and characterization of a protease from
Bacillus sps. Mater. Today Proc. 2020, 41, 685-691, https://doi.org/10.1016/j.matpr.2020.05.435.
118. Abdullah, A. N.; Ali Esmail, G.; Mohammed Ghilan, A. K.; Valan Arasu, M.; Duraipandiyan, V.;
Ponmurugan, K. Characterization and fermentation optimization of novel thermo stable alkaline protease
from Streptomyces sp. Al-Dhabi-82 from the Saudi Arabian environment for eco-friendly and industrial
applications. J. King Saud Univ. - Sci. 2020, 32, 1258–1264, https://doi.org/10.1016/j.jksus.2019.11.011.
119. Zhang, D.; Palmer, J.; Teh, K. H.; Calinisan, M. M. A.; Flint, S. Milk fat influences proteolytic enzyme
activity of dairy Pseudomonas species. Int. J. Food Microbiol. 2020, 320, 108-543,
https://doi.org/10.1016/j.ijfoodmicro.2020.108543.
120. Tang, X. Y.; Pan, Y.; Li, S.; He, B. F. Screening and isolation of an organic solvent-tolerant bacterium for
high-yield production of organic solvent-stable protease. Bioresour. Technol. 2008, 99, 7388–7392,
https://doi.org/10.1016/j.biortech.2008.01.030.
121. Gessesse, A.; Hatti-Kaul, R.; Gashe, B. A.; Mattiasson, B. Novel alkaline proteases from alkaliphilic bacteria
grown on chicken feather. Enzyme Microb. Technol. 2003, 32, 519–524, https://doi.org/10.1016/S0141-
0229(02)00324-1.
122. Ramakodi, M P.; Santhosh, N.; Pragadeesh, T.; Mohan, S. V.; Basha, S. Production of protease enzyme from
slaughterhouse effluent: An approach to generate value-added products from waste. Bioresour. Technol.
Reports 2020, 12, 1005-52, https://doi.org/10.1016/j.biteb.2020.100552.
123. Gaonkar, S. K.; Furtado, I. J. Valorization of low-cost agro-wastes residues for the maximum production of
protease and lipase haloextremozymes by Haloferax lucentensis GUBF-2 MG076078. Process Biochem.
2020, 1, 1-41, https://doi.org/10.1016/j.procbio.2020.10.019.
124. Rejisha, R. P.; Murugan, M. Materials Today : Proceedings Alkaline protease production by halophilic
Bacillus sp . strain SP II-4 and characterization with special reference to contact lens cleansing. Mater. Today
Proc. 2020, 45, 1757-1760, https://doi.org/10.1016/j.matpr.2020.08.624.
125. Ilesanmi, O. I.; Adekunle, A. E.; Omolaiye, J. A.; Olorode, E. M.; Ogunkanmi, A. L. Isolation, optimization
and molecular characterization of lipase producing bacteria from contaminated soil. Sci. African 2020, 8,
e002-79, https://doi.org/10.1016/j.sciaf.2020.e00279.
126. Mobarak-Qamsari, E.; Kasra-Kermanshahi, R.; Moosavi-Nejad, Z. Isolation and identification of a novel,
lipase-producing bacterium, pseudomnas aeruginosa KM110. Iran. J. Microbiol. 2011, 3, 92–98,
https://doi.org/10.5281/zenodo.3249860.
127. Chiring, L.; Chourasia, R.; Kumari, M.; Krishnan, T.; Sahoo, D.; Parameswaran, B. Bioresource Technology
Production and characterisation of lipase for application in detergent industry from a novel Pseudomonas
helmanticensis HS6. Bioresource Technology 2020, 309, 123-352,
https://doi.org/10.1016/j.biortech.2020.123352.
128. Priyanka, P.; Kinsella, G.; Henehan, G. T.; Ryan, B. J. Isolation, purification and characterization of a novel
solvent stable lipase from Pseudomonas reinekei. Protein Expr. Purif. 2019, 153, 121–130,
https://doi.org/10.1016/j.pep.2018.08.007.
129. Febriani, N.; Aura, P.; Kemala, N.; Saidi, T.; Iqbalsyah, M. Novel thermostable lipase produced by a thermo-
halophilic bacterium that catalyses hydrolytic and transesterification reactions. Heliyon 2020, 6, e04-520,
https://doi.org/10.1016/j.heliyon.2020.e04520.
130. Vyas, S.; Chhabra, M. Isolation, identification and characterization of Cystobasidium oligophagum JRC1: A

https://biointerfaceresearch.com/ 3468
 https://doi.org/10.33263/BRIAC123.34463471

cellulase and lipase producing oleaginous yeast. Bioresour. Technol. 2017, 223, 250–258,
https://doi.org/10.1016/j.biortech.2016.10.039.
131. Tripathi, R.; Singh, J.; Bharti, R. K.; Thakur, I. S. Isolation, purification and characterization of lipase from
microbacterium sp. and its application in biodiesel production. Energy Procedia 2014, 54, 518–529,
https://doi.org/10.1016/j.egypro.2014.07.293.
132. Parra, L. P.; Reyes, F.; Acevedo, J. P.; Salazar, O.; Andrews, B. A.; Asenjo, J. A. Cloning and fusion
expression of a cold-active lipase from marine Antarctic origin. Enzyme Microb. Technol. 2008, 42, 371–
377, https://doi.org/10.1016/j.enzmictec.2007.11.003.
133. Farha, A. K.; TR, T.; Purushothaman, A.; Salam, J. A.; Hatha, A. M. Phylogenetic diversity and
biotechnological potentials of marine bacteria from continental slope of eastern Arabian Sea. J. Genet. Eng.
Biotechnol. 2018, 16, 253–258, https://doi.org/10.1016/j.jgeb.2018.06.002.
134. Basheer, S. M.; Chellappan, S.; Beena, P. S.; Sukumaran, R. K.; Elyas, K. K.; Chandrasekaran, M. Lipase
from marine Aspergillus awamori BTMFW032: Production, partial purification and application in oil effluent
treatment. N. Biotechnol. 2011, 28, 627–638, https://doi.org/10.1016/j.nbt.2011.04.007.
135. Maia, M. M. D.; Heasley, A.; Morais, M. M. C.; Melo, E. H. M.; Jr, M. A. M.; Ledingham, W. M.; Filho, J.
L. L. Effect of culture conditions on lipase production by Fusarium solani in batch fermentation. Bioresource
Technology 2001, 76, 23-27, https://doi.org/10.1016/S0960-8524(00)00079-1.
136. Bannerman, E. N.; Nicolet, J. Isolation and characterization of an enzyme with esterase activity from
Micropolyspora faeni. Appl. Environ. Microbiol. 1976, 32, 138–144, https://doi.org/10.1128/aem.32.1.138-
144.1976.
137. Ateşlier, Z. B. B.; Metin, K. Production and partial characterization of a novel thermostable esterase from a
thermophilic Bacillus sp. Enzyme and Microbial Technology 2006, 38, 628-635,
https://doi.org/10.1016/j.enzmictec.2005.07.015.
138. Singh, S.; Lekha, S.; Gaurav, S.; Asha, A.; Gyanendra, K.; Lokendra, A.; Mohammad, I.; Moin, S.
Purification, Isolation, and Characterization of Esterase from Rhodococcus sp. lKe-021. J. Pure Appl.
Microbiol. 2020, 14, 1387–1395, https://doi.org/10.22207/JPAM.14.2.36.
139. Calero-Rueda, O.; Plou, F. J.; Ballesteros, A.; Martínez, A. T.; Martínez, M. J. Production, isolation and
characterization of a sterol esterase from Ophiostoma piceae. Biochim. Biophys. Acta - Proteins Proteomics
2002, 1599, 28–35, https://doi.org/10.1016/S1570-9639(02)00378-3.
140. Peng, Y.H.; Hsin Shih, Y.; Lai, Y. C.; Liu, Y. Z.; Liu, Y. T.; Lin, N. C. Degradation of polyurethane by
bacterium isolated from soil and assessment of polyurethanolytic activity of a Pseudomonas putida strain.
Environ. Sci. Pollut. Res. 2014, 21, 9529–9537, https://doi.org/10.1007/s11356-014-2647-8.
141. Satyanarayana, T.; Getzin, L. W. Properties of a Stable Cell-Free Esterase from Soil. Biochemistry 1973, 12,
1566–1572, https://doi.org/10.1021/bi00732a016.
142. Rengasamy, S. Isolation, Screening And Determination Of Α -Amylase Activity From Marine Streptomyces
Species. Int. J. Pharm. Pharm. Sci. 2018, 10, 122-127, https://doi.org/10.22159/ijpps.2018v10i4.24447.
143. Singh, R.; Sharma, D. C.; Gupta, M. K. Optimization of critical process parameters for amylase production
by Bacillus sp. using statistical approach (RSM). Journal of Microbiology and Biotechnology Research 2017,
7, 7-15, https://doi.org/10.24896/jmbr.2017732.
144. Kumar, J.; Vinod, A.; Vivek, S.; Saurabh, K.; Kumar, A.; Rani, R. Recent developments on solid-state
fermentation for production of microbial secondary metabolites : Challenges and solutions. Bioresour.
Technol. 2021, 323, 1245-66, https://doi.org/10.1016/j.biortech.2020.124566.
145. John, J. Amylases- Bioprocess and Potential Applications : A Review. Int. J. Bioinfomatica Biol. Sci. 2019,
5, 41–50, https://doi.org/10.5958/2321-7111.2017.00006.3.
146. Banerjee, S.; Maiti, T. K.; Roy, R. N. Production, purification, and characterization of cellulase from
Acinetobacter junii GAC 16 . 2, a novel cellulolytic gut isolate of Gryllotalpa africana , and its effects on
cotton fiber and sawdust. Ann. Microbiol. 2020, 70, 1–16, https://doi.org/10.1186/s13213-020-01569-6.
147. Sreedharan, S.; Sreedevi, S.; Prakasan, P. Production and Partial Purification of Cellulase from a New Isolate,
Penicillium verruculosum BS3. Br. Microibology Res. J. 2015, 9, 1–12,
https://doi.org/10.9734/BMRJ/2015/17865.
148. Sigh, N. P.; Dayal, A.; Sharan, A. K. Production of cellulase enzyme by Aspergillus niger, Aspergillus terreus
and Pencillium sp. isolated from soil. Ann. Plant Sci., 2020, 9, 3991–3998,
http://dx.doi.org/10.5281/aps.2020.9.9.1.
149. Islam, F.; Roy, N. Screening, purification and characterization of cellulase from cellulase producing bacteria

https://biointerfaceresearch.com/ 3469
 https://doi.org/10.33263/BRIAC123.34463471

in molasses. BMC Res. Notes, 2018, 11, 1–6. https://doi.org/10.1186/s13104-018-3558-4.

150. Shahriarinour, M.; Ramanan, R. N. Purification and Characterisation of Extracellular Cellulase Main
Components from Aspergillus terreus. Bioresour. Technol. 2015, 10, 4886–4902,
http://dx.doi.org/10.15376/biores.10.3.4886-4902.
151. Brammacharry, U. Production and characterization of protease enzyme from Bacillus laterosporus. African
J. Microbiol. Res. 2018, 4, 1057–1063, https://doi.org/10.5897/AJMR.9000592.
152. Pant, G. V. N. S.; Gaurav, P.; Anil, P.; Bera, J. V. P.; Sayantan, D.; Kumar, A.; Panchpuri, M.; Gyana, R.
Production, optimization and partial purification of protease from Bacillus subtilis. Integr. Med. Res. 2015,
9, 50–55, https://doi.org/10.1016/j.jtusci.2014.04.010.
153. Ishaku, K.; Inuwa, M.; Moses, O. Purification, characterization and optimization conditions of protease
produced by Aspergillus brasiliensis strain BCW2. Sci. African 2020, 8, e003-98,
https://doi.org/10.1016/j.sciaf.2020.e00398.
154. Gimenes, N.; Silveira, E.; Tambourgi, E. An Overview of Proteases: Production, Downstream Processes and
Industrial Applications. Separation and Purification Reviews 2021, 50, 223-243,
https://doi.org/10.1080/15422119.2019.1677249.
155. Ahmed, M. E. Extraction and purification of protease from Aspergillus niger isolation. Pharm. Pharmacol.
Int. J. 2018, 6, 96–99, https://doi.org/10.15406/ppij.2018.06.00162.
156. Lakshmi, B. K. M.; Muni Kumar, D.; Hemalatha, K. P. J. Purification and characterization of alkaline
protease with novel properties from Bacillus cereus strain S8. Journal of Genetic Engineering and
Biotechnology 2018, 16, 295-304, https://doi.org/10.1016/j.jgeb.2018.05.009.
157. Manan M. A.; Webb, C. Design aspects of solid state fermentation as applied to microbial bioprocessing. J.
Appl. Biotechnol. Bioeng. 2017, 4, 511–532, https://doi.org/10.15406/jabb.2017.04.00094.
158. Fasim, A.; More, V. S.; More, S. S. Large-scale production of enzymes for biotechnology uses. Curr. Opin.
Biotechnol. 2021, 69, 68–76, https://doi.org/10.1016/j.copbio.2020.12.002.
159. Herna'ndez, A. L.; Martı´nez, J. R. Solid state fermentation ( SSF ): diversity of applications to valorize waste
and biomass. Biotechnology 2017, 7, 1-9, https://doi.org/10.1007/s13205-017-0692-y.
160. Mukherjee, S. Isolation and Purification of Industrial Enzymes: Advancement in enzyme technology. In
Advances in Enzyme Technology, 1st edition, Ram Sarup Singh, Reeta Rani Singhania, Christian Larroche,
Elsevier B.V, Amsterdam, Netherlands 2019, 41-70, https://doi.org/10.1016/B978-0-444-64114-4.00002-9.
161. Patel, S.; Naveen, R.; Dhananjai, S.; Shivam, S. Lipases : Sources, Production, Purification, and Applications,
Recent Pat. Biotechnol. 2019, 12, 1–12, https://doi.org/10.2174/1872208312666181029093333.
162. Toke, E. R.; Nagy, V.; Recseg, K.; Szakács, G.; Poppe, L. Production and application of novel sterol esterases
from aspergillus strains by solid state fermentation. JAOCS Journal of the American Oil Chemists' Society
2007, 84, 907-915, https://doi.org/10.1007/s11746-007-1127-4.
163. Torres, G. R.; Sebastián, B.; Mario, D. P.; Ashok, C. Production and Purification of a Solvent-Resistant
Esterase from Bacillus licheniformis S-86. Appl. Biochem. Biotechnol. 2018, 151, 221–232,
https://doi.org/10.1007/s12010-008-8181-8.
164. Chen, Z.; Cheng-cheng, C.; Zhe, L.; Guang-lei, J.; Hong, H.; Chi, Z. Production, purification, characterization
and gene cloning of an esterase produced by Aureobasidium. In Process Biochemistry, 1st edition, J-J. Zhong
E.J. Vandamme Boudrant, J, Elsevier Ltd, Singapore 2018, 1-41,
https://doi.org/10.1016/j.procbio.2016.12.006.
165. Bhardwaj, A.; Kamal, K. D.; Kapoor, A.; Smita, M.; Gupta, R. Purification and Properties of an Esterase
from Bacillus licheniformis and it' s Application in Synthesis of Octyl Acetate. Open Microbiol. J. 2020, 15,
113–121, https://doi.org/10.2174/1874285802014010113.
166. Ahmad, T.; Singh, R. S.; Gupta, G.; Sharma, A.; Kaur, B. Metagenomics in the search for industrial enzymes,
Biomass, Biofuels, Biochemicals. In Advances in Enzyme Technology,1st edition, Ram Sarup Singh, Reeta
Rani Singhania, Christian Larroche, Elsevier B.V, India 2019, 419-451, https://doi.org/10.1016/B978-0-444-
64114-4.00015-7.
167. Madhavan, A .; Sindhu, R.; Parameswaran, B.; Sukumaran, R. K.; Pandey, A. Metagenome Analysis: a
Powerful Tool for Enzyme Bioprospecting. Appl. Biochem. Biotechnol., 2017, 183, 636–651,
https://doi.org/10.1007/s12010-017-2568-3.
168. Visvanathan, R.; Jayathilake, C.; Liyanage, R.; Sivakanesan, R. Applicability and reliability of the glucose
oxidase method in assessing α-amylase activity. Food Chem. 2019, 275, 265–272,
https://doi.org/10.1016/j.foodchem.2018.09.114.

https://biointerfaceresearch.com/ 3470
 https://doi.org/10.33263/BRIAC123.34463471

169. Kwon, K. K.; Yeom, S. J.; Lee, D. H.; Jeong, K. J.; Lee, S. G. Development of a novel cellulase biosensor
that detects crystalline cellulose hydrolysis using a transcriptional regulator. Biochem. Biophys. Res.
Commun. 2018, 495, 1328–1334, https://doi.org/10.1016/j.bbrc.2017.11.157.
170. Oliveira-Silva, R.; Sousa-Jerónimo, M.; Botequim, D.; Silva, N. J. O.; Paulo, P. M. R.; Prazeres, D. M. F.
Monitoring Proteolytic Activity in Real Time: A New World of Opportunities for Biosensors. Trends
Biochem. Sci. 2020, 45, 604–618, https://doi.org/10.1016/j.tibs.2020.03.011.
171. Shi, F. H. J.; Zhang, S.; Zheng, M.; Deng, Q.; Zheng, C.; Li, J. A novel fluorometric turn-on assay for lipase
activity based on an aggregation-induced emission (AIE) luminogen. Sensors Actuators B Chem. 2017, 238,
765–771, https://doi.org/10.1016/j.snb.2016.07.116.
172. Xiaolong, C. C.; Gaihua, Z.; Jiajin, D.; Yuanyi, L.; Xiaogang, Y.; Mei, H.; Danqun, H. C. An ultrasensitive
and point-of-care strategy for enzymes activity detection based on enzyme extends activators to unlock the
ssDNase activity of CRISPR/Cas12a (EdU-CRISPR/Cas12a). Sensors Actuators B Chem. 2021, 333, 129553,
https://doi.org/10.1016/j.snb.2021.129553.
173. Pan, R.; Jiang, D. Nanokits for the electrochemical quantification of enzyme activity in single living cells, In
Methods in Enzymology, 1st ed., Nancy L. Allbritton, Michelle L. Kovarik, Elsevier Inc., Jiangsu, China
2019, 628, 173-189, https://doi.org/10.1016/bs.mie.2019.06.015.
174. Gang, M. L.; Raymond, E. Chemical probes for spatially resolved measurement of active enzymes in single
cells. In Methods in Enzymology, 1st ed., Nancy L. Allbritton, Michelle L. Kovarik, Elsevier Inc., United
States 2019, 628, 243-262, https://doi.org/10.1016/bs.mie.2019.06.017.
175. Huang, H. Matrix metalloproteinase-9 (MMP-9) as a cancer biomarker and MMP-9 biosensors: Recent
advances. Sensors (Switzerland) 2018, 18, 5–7, https://doi.org/10.3390/s18103249.

https://biointerfaceresearch.com/ 3471

View publication stats