Biblid: 1450-5029 (2009) 13; 2; p.

124-127 Original scientific paper

UDK: 664.653.4 Originalni naučni rad

HIGH QUALITY NOODLE PRODUCTS AND THEIR TRADITIONAL AND

NON-TRADITIONAL PROCESSING
VISOKOKVALITETNI TESTIČARSKI PROIZVODI I NJIHOVA
TRADICIONALNA I NETRADICIONALNA PROIZVODNJA
Dr. Elisabeth T. KOVACS
University of Szeged, Faculty of Engineering, Institute of Food Engineer
H-6724 Szeged, Mars tér 7, Hungary, e-mail: [email protected].

SUMMARY
Traditional pasta is produced only from different qualities of wheat flour (T. durum, T. aestivum) and water, but the use of legu-
minous flour (like yellow pea flour), pseodecereals (like amaranth ) or maize starch as well etc. for producing noodle products is un-
conventional. There are several possibilities for improving the quality of the products: to change the technology (drying on low or
high temperature) or to use additives such as emulsifiers and/or enzymes. For developing an improved pasta structure the enzyme
transglutaminase can be used as well.
In the presence of emulsifier an emulsifier-carbohydrate-protein-lipid complex can be expected. The rate of the individual interac-
tions depends on the components of the sample and on the type of applied emulsifiers. Transglutaminase enzyme, a protein-glutamine
γ-glutamyl- transferase (EC.2.3.2.13), catalysis acyl-transfer reactions, and introduces covalent cross-links between proteins. The
application of transglutaminase has great importance for the development of pasta products: from pseudocereals, or wheat flours (T.
durum, T. aestivum). Pasta products with good quality like T. durum-based pastas can be produced from T. aestivum flour. By using
transglutaminase the quality of T. durum flour can also be improved, so the pastas will show higher cooking quality. The enzyme in-
sures cholesterol free products. Pasta and noodle products were produced according a modelling system. The effect of the enzyme
treatment on cooking properties, sensory assessment and protein distribution was analyzed. The change of the protein structure de-
pends on the type of systems, the amount and the type of additives.
Key words: emulsifiers, transglutaminase enzyme, pasta properties, SDS-PAGE.

INRODUCTION The protein-emulsifier interactions help to develop a better

According to nutritionists and consumers, pasta from wheat structure in food systems. We can see these interactions in the
flour is a valuable nutritional and long-lasting energy source, change of molecular weight distribution of the protein fraction
which made this product increasingly popular in the human diet. (salt soluble, gliadin and glutelin fractions).
The popularity of dried pasta may be also attributed to its sen- Emulsifier-carbohydrate interactions. Starch consists of
sory appearance, quality, low cost, easy preparation and excel- two types of carbohydrate, amylose and amylopectin, both built
lent storage stability. In addition, fresh (non-dried) pasta prod- up from glucose units. From the two fractions of carbohydrate
ucts appear on the market as a new type of "fresh product" with the amylose is in the position to form a starch inclusion com-
high consumer acceptance, therefore a growth of pasta consump- pounds, so called complex with suitable ligands. The other pos-
tion is expected. In Hungary pasta is very popular, one of the sibility of interaction with the ligands is to form a hydrogen-
most preferably eaten product. So far the production of pastas bridge with the amylopectin.
was mainly made with egg. There are several possibilities for
improving the quality of the products: to change the technology
(drying on low or high temperature) or to use additives such as
emulsifiers, enzymes.
Use of emulsifiers. Emulsifiers activity is based on its mo-
lecular structure, namely the hydrophilic ("head") and the hy-
drophobic ("tail") part. The foods are very complex hydrocol-
loidical systems. If we use emulsifiers in this system, different
kind of interactions should occur between the components of
food and emulsifiers. The most important interactions can be the a) b)
following: protein-emulsifier, carbohydrate-emulsifier and lipid-
emulsifier [1]. Fig. 1. Emulsifier-carbohydrate interactions [2]
Protein-emulsifier interactions can be: hydrophobic bonds, a) Glycerol-monostearete and amylose complex
hydrogen bridges and electrostatic interactions. The interactions b) Hydrogen bridge interaction between emulsifier and amy-
depend on the amino acid components of the protein. The possi- lopectin
ble interactions are listed in Table 1.
Table 1 The possible interactions between protein and emul- From the point of complex forming ability the emulsifiers
sifiers are ideal ligands. In the case of the emulsifier-amylose inclusion
Type of interaction Amino acid components Energy of bond kJ/mol compounds only the hydrophibic residues of the molecules will
Ala, Val, Leu, I-Leu Pro, be built into the helical configuration and the hydrophilic head is
Hydrophobic bonds 3-19
Phe-Ala, Tryp, Met outside of the helical structure. The emulsifiers glycerol-
Electrostatic bonds Lys, Arg, His, Asp, Glu 21 monostearate, lysolecithin are good complex forming agents,
Hydrogen bridge Gly, Ser, Cys, Tyr, Asp, Glu 12-16 where as lecithin is not able to form a complex.

124 PTEP 13(2009) 2

 Emulsifiers-lipids interactions. This interaction can be METHODS
mainly hydrophobic.
Use of enzyme transglutaminase (TG). For developing a Compositional analysis.
pasta structure the enzyme transglutaminase can also be used. The composition (dry matter-, protein- and fat contents of
Transglutaminase is a protein-glutamine γ-glutamyl-transferase, raw materials was determined according to Karácsonyi [6] in
(EC.2.3.2.13) catalyses acyl-transfer reactions, introducing cova- triplicate. Sensory assessment and the calculation of the total
lent crosslinks in proteins. Crosslinks are formed between lysine score were carried out according to the Hungarian Standard [7].
residues and glutamine residues producing an ε-(γ-Glu)-Lys Method of cooking test (amount of water uptake, cooking
bond, without reducing the nutritional value of the lysine resi- loss) was made according to Karácsonyi [6] (water: pasta =
due. 25:1, tap-water, pH of cooking water = 6.80, cooking time 5
H2N – (CH2)4 – CH – COOH + O═C – CH2 ─ CH2 ─ CH ─COOH min, electric cooker). All determination were performed in trip-
| | | licate and were statistically evaluated by ANOVA ANALYSIS
NH2 NH2 NH2 [8] with a probability level based on P =0.05.
Lysine Glutamine Protein fractionation procedures.
Transglutaminase is getting used in a wide variety of foods, Water, salt, alcohol and alkali-soluble protein fractions were
particularly since large quantities of microbial transglutaminase obtained by extraction from the pasta products according to
became commercially available. It is generally assumed that the methods of to Feillet [9]. At pea noodle products were isolated
effects of transglutaminase in foods are due to its crosslinking only salt-soluble protein fraction. The amount of soluble frac-
activity. The 3 reactions catalysed by microbial transglutami- tions was determined by Micro-Kjeldahl Method. The molecular
nase: protein cross linking, incorporation of a free amine and weight distributions of the fraction were established by SDS-
hydrolysis of a glutamine residue [3]. The use of transglutami- PAGE-electrophoresis according Laemmli [10] for 110 min at
nase improved the functional property and structure of the prod- 140 V (32 mA). Proteins were separated in a 12.5% acrylamide
ucts. The modification with transglutaminase enzyme induced gel. Mini-gels (100x100x1 mm) were used. The gels were fixed
drastic changes in the physicochemical properties as well as in and stained in one step in a mixture of 12.5 %TCA and 0.25%
the rheological behaviour of the products. Coomassie Brillant Blue R-250.
I would like to give same new results about the use of trans-
glutaminase enzymes and emulsifiers in different pasta systems DISCUSSION
made from T. aestivum and pea flours.
The compositions of raw materials are listed in Table 2.
RAW MATERIALS
Table 2. Composition of raw materials
In my tests, commercially available wheat flours (T. aesti-
vum, T. durum) with an ash content of 0.55 % and yellow pea Fraction Dry matter (%) Protein (d.m.%) Fat (d.m %)
flour were used, in particle sizes of 250-500µm. Water-soluble T. aestivum 88.35±0.78 11.83±0.32 1.78±0.32
transglutaminase enzyme ACTIVA®STG-M having an enzyme T. durum 89.42±0.50 15.23±0.46 2.45±0.82
activity of 20-30 Ug-1, was obtained from Ajinomoto Co. Ham- Yellow pea flour 89.40±0.50 18.51±0.46 1.75±0.32
burg, Germany. Emulsifiers were used: lecithin (L) Lucas
Meyer, Germany and diacylglycerols, Dimodan PM (DPM) Figure 2 shows the molecular weight distribution of the
originated from Grindsted, Denmark. soluble protein fractions in T. aestivum wheat flour systems, the
Pasta models: wheat flour and water was mixed to dough pasta properties are presented in Figure 3.
with 40% moisture content. The amount of TG enzyme was var- We could not find great differences in the amount and
ied between 10-200 mgkg-1, using distilled water, based on the change of molecular weight distribution of salt soluble fraction
amount of flour. Pasta products from T. aestivum flour were pre- of the wheat flour fractions, but we could detect a difference in
pared by German pasta maker, NUDELMEISTER 8495 [4]. In the amount and molecular weight distribution of gluten proteins.
case of pea noodle model systems the amount of yellow pea Pasta on wheat basis produced with the TG-Enzyme has shown
flour and water was counted to obtain 40% moisture content in excellent quality parameters. Pasta without additives has shown
the dough with the addition of 1.2% (w/w) emulsifier related to a lower quality level. Pasta with supplement of 40 mgkg-1 en-
the flour too. A suspension was made from the emulsifiers and zyme TG has shown excellent sensory results. The TG-Enzyme
water. The temperature of suspension was raised up to 97°C. has influenced and changed the molecular weight distribution of
The mixture was stirred for 15 min in a mixer. The amount of the soluble protein fractions. The TG-Enzyme could integrate
TG Enzyme in pea systems was varied between 50-200 mgkg -1, LMW fractions into the developed protein structure. The cook-
based on the amount of flour. After mixing the enzymatic treat- ing time of pasta products produced with TG-Enzymes is longer
ment followed for 60 min at room temperature. A dough- than that of products without this enzyme (22 -26 min). For im-
processing machine produced macaroni and by pressing them proving the quality of pasta products from T. durum 10-40
through a teflon matrix. Pasta produced with wheat flour were mgkg-1 TG-Enzyme is enough.
dried at 39°C and at 87% relative humidity for 24 hours and the Pea seeds contain only salt soluble albumin and globulin, so
pea noodles were dried at 39°C and at 110°C for 1 hour, at without additives it is impossible to form a pasta structure, but
70°C for 2 hour as well as at room temperature. After drying the the use of TG-Enzyme ACTIVA®STGM we could produce
samples were stored at room temperature for another 48 hours pasta products. The gel slab can be seen on Figure 4. On the ba-
[5]. (All the pasta models were made in duplicate). The dried sis of electrophoreses great differences were observed in the mo-
pastas were ground in a LABMILL ‘QC-114-type grinder to a lecular weight distribution as TG enzyme developed direct cova-
particle size 200 - 450 µm. The pastas were investigated only in lent bindings, while emulsifiers developed only secondary inter-
powder form. The regular pasta was used only for the determina- action. This resulted better structure and noodle products with
tion of the cooking quality and - properties. higher quality (Figure 5).

PTEP 13(2009) 2 125

 Gliadin Glutenin

94 94

67 67
43 43
30 30

20 20

14 14

kDa 1 2 3 4 5 6 7 8 9 10 kDa 1 2 3 4 5 6 7 8 9 10
Fig. 2 Molecular weight distribution of gluten protein fractions (Gliadin and Glutenin) of T. aestivum based pasta products made
with 10-80 mgkg-1 TG Enzyme
Lines: 1 Standard (Pharmacia Sweden), 2: flour, 3: pasta10 mgkg-1TG, 4: pasta 20 mgkg-1TG, 5: pasta 30 mgkg-1TG, 6: pasta 40
mgkg-1 TG, 7: pasta 50 mgkg-1TG, 8: pasta 60 mgkg-1TG, 9: pasta 70 mgkg-1TG, 10 : pasta 80 mgkg-1TG

300

250

200

150

100

50

0
flour 0 mg 10 mg 20 mg 30 mg 40 mg 50 mg 60 mg 70 mg 80 mg
TG enzyme
Salt soluble,%* Cooking loss,% Sensory assessm

Gliadin,%* Glutenin,%* Water uptake, %

Fig. 3. Pasta properties based on T.aestivum flour with 10-80 mgkg-1 transglutaminase enzyme
94

67

43

30

20
kDa
14
kD

1 2 3 4 5 6 7 8 9 10 11 12 13
Fig. 4. Molecular weight distribution of salt soluble fraction of yellow pea noodle products (YPNP) made with 160 mgkg-1 TG en-
zyme or 1.2% w/w% Lecithin(L) or 1.2% w/w% Dimodan PM(DPM) with different drying temperature and time.
Lines : 1: Standard(Pharmacia Sweden), 2:YPNP flour, 3: YPNP TG 110°C,1h, 4: YPNP TG 70°C, 2 h, 5: YPNP TG 39°C, 24 h, 6:
YPNP TG room temperature, 7: YPNP L 110°C, 1 h, 8: YPNP DPM room temperature, 9: YPNP L 70°C, 2 h, 10: YPNP L 39°C 24
h , 11: YPNP DPM 110°C, 1h, 12: YPNP DPM 70°C, 2 h, 13: YPNP DPM 39°C, 24 h

126 PTEP 13(2009) 2

 300

200

100
Cooking loss,%

0 Complex,%

ur
0°
C C C g C C C g C C C
0° 39° ryin 10° 70° 39° ryin 10° 70° 39° ryin
g
flo11 -1 7 d 1 d 1 d
YP
160 mgkg TG air L ai DPM
r
ai
r

Complex,% Soluble protein,% Total scores Cooking loss,% Water uptake,%

Fig. 5. Pasta properties made with 160 mgkg-1 transglutaminase enzyme, 1,2 w/w% lecithin and 1,2 w/w% Dimodan PM from yel-
low pea flour

Pea noodle products have shown different quality level de- REFERENCES
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Primljeno:13.03.2009. Prihvaćeno:10.04.2009.

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