Protease Enzyme Definition
“Protease is an enzyme that catalyses the hydrolysis of peptide bonds
present in proteins.”
In most of the living organisms, protease enzymes are essential for digestion and
absorption of proteins.
Proteases are found in all the living organisms, e.g. bacteria, algae, plants and animals
and in some of the viruses too. They are involved in the catabolism and digestion of
proteins and also in cell signalling.
Protease Enzyme Types
There are many different types of proteases, that take part in various biochemical
processes.
On the basis of the site of the peptide bond cleavage, proteolytic enzymes are
divided into two broad groups:
Exopeptidase: They catalyse the cleavage on terminal peptide bond, e.g.
aminopeptidases, carboxypeptidases, etc.
Endopeptidase: They facilitate the cleavage of internal peptide bonds of proteins,
e.g. pepsin, trypsin, chymotrypsin, elastase, etc.
Oligopeptidase refers to enzymes, that act on a specific peptide bond.
Different types of protease enzymes remain active in the different pH range,
e.g. acid proteases, alkaline or basic proteases and neutral proteases.
Protease Enzyme Functions
Protease enzymes are essential for many biological processes. They are required for regulation
of various metabolic and cellular processes.
They are proteolytic, they help in digestion and catabolism of proteins. They catalyse the
hydrolysis of peptide bonds and convert them to amino acids, which is then absorbed and
utilised by cells.
They are required for the blood coagulation process.
Protease enzymes are involved in the cell division, growth and apoptosis.
Proteases provide immune support and regulate the process of tumour growth, metastasis,
inflammation, etc.
They may help in wound healing.
Plant proteases such as bromelain, ficin and papain are widely used in food industry for
various applications such as brewing, tenderization of meat, coagulation of milk and as a
digestive aid.
Proteases are widely used in baking industry for the production of bread, baked foods,
crackers and waffles. These enzymes are used to reduce the mixing time, decrease dough
consistency and uniformity, regulate the gluten strength in bread and to improve the texture
and flavour
The addition of protease could release sufficient peptides and amino acid
levels in the wort to get a proper fermentation. Acidic fungal proteases are
used in improving fermentation of beer as they are efficient even at low pH by
balancing the amino acid profile of beer.
Naturally occurring proteases contribute significantly to the flavour
characteristics of cheese. They are used for the acceleration of cheese
ripening, to modify the functional properties and reduce the allergenic
properties of milk products
Protease Enzyme Examples
Here is the list of some of the important protease enzymes and their functions:
Protease Enzyme Name Function
Trypsin Found in pancreatic juice and breaks proteins and
peptones
Carboxypeptidase Found in pancreatic juice and breaks proteins and
peptones and proteoses to dipeptides
Nuclease (ribonuclease and deoxyribonuclease) Present in pancreatic juice. They split nucleic acid to
nucleotides
Collagenase It digests collagen
Dipeptidase Found in intestinal secretion. Breaks dipeptides to
amino acids
Pepsin Present in stomach and converts proteins to smaller
peptides – proteoses and peptones
Rennin Secreted by chief cells of the stomach and milk
protein
Thrombin Involved in blood coagulation
Plasmin Involved in blood coagulation
Chymases, tryptases They are present in mast cells and involved in
allergic reactions and inflammation
How does Protease work?
Protease enzymes catalyse the hydrolysis of peptide bonds. Catalysis
facilitates the nucleophilic attack of an activated water molecule on the
peptide bond.
Serine, cysteine and threonine proteases function by forming an acyl-enzyme
intermediate, which then gets hydrolysed by water to get the product and
enzyme is set free.
Protease enzyme range from general to specific, e.g. digestive protease
enzyme, trypsin can cleave many proteins into smaller fragments, whereas
enzymes like thrombin, which takes part in blood clotting are highly specific.
Many protease enzymes are present in an inactive form. Being protein
themselves, these precursors get converted to an active form by another
protease enzymes. It helps in the regulation and control of the activity. E.g.
trypsinogen, chymotrypsinogen, proelastase, etc.
Where can protease enzymes be found?
Proteases are found in both animals and plants. In humans, proteases are
mainly present in pancreatic juice and gastric secretions to break down
dietary proteins. Trypsin and chymotrypsin are secreted by the pancreas and
pepsin is secreted by the chief cells in the stomach. Protease enzymes are
naturally found in various food sources such as roots, leaves and fruits of
papaya contain papain, a protease enzyme. Pineapple fruits contain a protease
enzyme known as bromelain.
What fruit contains protease enzymes?
Fruits like papaya, fig, pineapple, kiwi, etc. contain proteases. Proteases help
in the digestion of proteins. Proteases from fruits are used as dietary
supplements, treating wounds and also in food processing industries.
What is an example of a protease?
An example of a protease enzyme is pepsin. It is secreted by peptic of chief cells
of gastric mucosa as a proenzyme called pepsinogen. Pepsinogen gets
converted into pepsin by the action of HCl secreted by gastric glands. It
converts proteins to short-chain polypeptides known as peptones.
The glucose oxidase enzyme also known as notatin is an oxidoreductase that
catalyses the oxidation of glucose to hydrogen peroxide and gluconic acid
C6H12O7
Glucose oxidase enzymes are used to remove small amounts of oxygen from
food products or glucose from diabetic drinks. Glucose oxidase is playing an
important role in color development, flavor, texture, and increasing the shelf
life of food products
Oxidases are enzymes that catalyze the oxidation of C–N and C–O bonds at
the expense of molecular oxygen, which is reduced to hydrogen peroxide.
Other uses of glucose oxidase include the removal of oxygen from food
packaging and removal of D-glucose from egg white to prevent browning.
How does glucose oxidase detect glucose?
The enzyme glucose oxidase catalyzes the oxidation of glucose to gluconic acid
C6H12O7 and hydrogen peroxide (H2O2): Addition of the enzyme peroxidase
and a chromogenic oxygen acceptor, such aso-dianisidine, results in the
formation of a colored compound that is measured: Glucose oxidase is highly
specific for β-D-glucose.
Principle. Oxidase Test is based on the principle that certain bacteria produce
indophenol blue from the oxidation of dimethyl-p-phenylenediamine and α-
naphthol. In presence of the enzyme cytochrome oxidase (gram-negative
bacteria), the N,N-dimethyl-p-phenylenediamine oxalate and α-naphthol react
to indophenol blue.
Catalase is a common enzyme that is found in nearly all living organisms that
are exposed to oxygen such as bacteria, plants, and animals. The catalase
location in mammals is found in the liver. This catalyzes the decomposition
of the substance hydrogen peroxide to form water and oxygen. It is a very
important enzyme in protecting the cell from oxidative damage by reactive
oxygen species. Catalase has one of the highest turnover numbers of all
enzymes whereas one catalase molecule can convert millions of hydrogen
peroxide molecules each second to water and oxygen.
Catalase is a tetramer molecule consisting of four polypeptide chains, each
of these chains are over 500 amino acids long. It contains four iron-
containing heme groups that allow the enzyme to react with hydrogen
peroxide. The optimum pH for human catalase is approximately seven is
neutral and the rate of reaction does not change in between the pH range of
6.8 and 7.5.
Catalase Function
The presence of catalase in a microbial or tissue sample can be demonstrated
by adding hydrogen peroxide and observing the reaction. The production of
oxygen can be seen by the formation of bubbles.
This easy test, which can be viewed with the naked eye, without the aid of
instruments.
Cellular Role:
Hydrogen peroxide is a harmful byproduct that is formed from many of the
normal metabolic processes. It is done in order to prevent damage that occurs
to cells and tissues, these byproducts must be quickly converted into other
forms or to less dangerous substances.
By the end, catalase is frequently used by cells to catalyze rapidly the
decomposition of hydrogen peroxide into less-reactive gaseous oxygen and
water molecules.
Hydrogen peroxide is used as a potent antimicrobial agent when the cells in
the organisms are infected with a pathogen. Catalase-positive pathogens, such
as Mycobacterium tuberculosis and Campylobacter jejuni.
Catalase Uses
Catalase enzyme is used mostly in the food industry for removing the hydrogen
peroxide content from the milk prior to cheese production.
It is widely used in the production of food wrappers which helps to prevent the
food from oxidizing. Catalase is also used in the textile industry, in order to
remove the hydrogen peroxide content from the fabrics to make sure the
material is peroxide-free.
A minor use is in the hygiene of contact lens, few of the lens-cleaning products
can disinfect the lens using a hydrogen peroxide solution.
A solution that contains catalase is then used to decompose the hydrogen
peroxide from the solution before the lens is used again.
It is used a glucose oxidase/catalase cocktail for elimination of oxygen from wine
before bottling and evaluated the formation of acetaldehydes. Results showed
that colour and amount of acetaldehyde were stable if treated properly with
enzymes.
Catalase test:
The catalase test is one of the three main tests that are used by
microbiologists to identify the presence of species of bacteria. If the
bacteria possess the enzyme catalase, then bubbles of oxygen are
observed when a small amount of bacterial isolate is added to the
hydrogen peroxide. This catalase test is done by adding a drop of hydrogen
peroxide to a microscope slide. An applicator stick is touched to the
colony, and the tip is then smeared onto the hydrogen peroxide drop.
Lactase is a protein that acts as an enzyme. Lactase is sometimes created by cells in
your body, however, some people that suffer from genetic abnormality may have to
require pills or capsules that contain the accelerator.
The organic chemistry reaction that involves disaccharides breaks down disaccharide,
a sugar in milk. Some people’s bodies don’t build enough disaccharides so that
they aren’t able to digest milk well. These individuals are “lactase deficiency”
and known as “lactose intolerant.” they’ll take supplemental disaccharides to
assist them to break down disaccharide and tolerate milk.
Lactose, a disaccharide, is a sugar composed of galactose and glucose subunits and
has the molecular formula C₁₂H₂₂O₁₁. Lactose makes up around 2–8% of milk.
In these individual’s disaccharides will forestall symptoms of genetic
abnormality together with cramps, diarrhoea, and gas. Many
health consultants assume it’s vital to treat a genetic abnormality, therefore,
individuals will consume milk and milk merchandise. Milk could be
a major supply of Ca, that is required for sturdy bones. People who don’t get enough
milk develop weak bones (osteoporosis).
Uses
Food Use
Lactase enzyme is an enzyme that some people are unable to produce in their
small intestine. Without it they cannot break down the natural disaccharide in
milk, leaving them with diarrhoea, gas and bloating when drinking regular milk.
Technology to supply lactose-free milk and yogurt were developed by the
Agricultural Analysis Service in 1985. This technology is used to add lactase to milk,
thereby hydrolysing the lactose naturally found in milk, leaving it slightly sweet
but digestible by everyone. Without disaccharides, lactose intolerant people pass
the lactose undigested to the colon where bacteria break it down, creating carbon
dioxide and that leads to bloating and flatulence.
Lactase is added to ice cream to breakdown lactose (primary sugar found in dairy
products) as the lactose molecule is too large to be carried through the small
intestine. Lactose is broken down by converting itself into the two sugars that
form the lactose molecule.
Medical Use
Lactase supplements square measure generally treat genetic abnormality.
Industrial Use
Lactase created commercially are often extracted each from
yeasts like Kluyveromyces fragilis and Kluyveromyces lactis and from molds, such
as Aspergillus niger and Aspergillus oryzae. Its primary business use, in
supplements such as Lacteeze and Lactaid, is to break down lactose in milk to
make it suitable for people with lactose intolerance.
Lactase Deficiency
Some individuals square measure unable to provide enough disaccharidase to
fulfill their bodies’ requirements. These patients square measure aforesaid to
be laid low with congenital disease, or lactose intolerance. According to
MedlinePlus, a service of the National Institutes of Health, symptoms of the
congenital disease begin half-hour to two hours once ingesting milk or the
same food product. Symptoms include bloating of the stomach, abdominal
cramps, flatulence, nausea, and diarrhoea. Larger doses
of farm product typically cause additional severe symptoms. Premature births,
bowel surgery, intestinal diseases, and intestinal infections are all possible risk
factors for developing lactose intolerance.
Lactase Supplements
Lactase supplements are is obtainable to patients who are suffering from an
intolerable genetic disorder. Typically, these capsules are consumed just before
you ingest dairy products. The Lactaid within the capsule dissolves the sugar
contained within the food and this allows your body to soak up the sugar.
