Influence of milk protein cross‐linking by transglutaminase on the rennet coagulation time and the gel properties

Domagała, Jacek; Najgebauer-Lejko, Dorota; Wieteska-Śliwa, Ilona; Sady, Marek; Wszołek, Monika; Bonczar, Genowefa; Filipczak‐Fiutak, Magda

doi:10.1002/jsfa.7534

Cited by 32 publications

(15 citation statements)

References 33 publications

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“…The simultaneous addition of MTGase and rennet significantly decreased the cheese hardness as well as increased the loss of proteins and fat in the whey [10] [15]. However, other studies recommended this method [21] [22]. The third method [17] [23] and the fourth one [10] [15] [16] have been recommended, as they positively influenced the composition, yield and sensory properties of produced cheese.…”

Section: Introductionmentioning

confidence: 99%

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The Impact of Microbial Transglutaminase on the Quality and Antioxidant Activity of Camel-Milk Soft Cheese

Abou-Soliman¹,

Awad²,

El-Sayed³

2020

FNS

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This study aimed at investigating the impact of adding microbial transglutaminase (MTGase) after rennet addition on some properties of fresh soft cheese made from camel milk. MTGase was added to milk at concentration of 80, 100 and 120 U⁄L after 20 and 30 min of renneting. The chemical composition, yield, hardness, antioxidant activity and sensory properties of cheese were estimated. Enzymatic protein crosslinking was analyzed by SDS-PAGE. Results revealed that MTGase-treated cheeses were higher in moisture and lower in protein content compared to control. In addition, the concentration of MTGase and time of addition significantly (P < 0.05) impacted these parameters. Among treated cheeses, samples with 80 U of MTGase and addition time of 20 min were the highest in total solids and protein content. Adding MTGase significantly (P < 0.05) increased the cheese yield, however, increased MTGase concentration at any time of addition did not improve it. The electrophoretic patterns of MTGase-cheese proteins showed a reduction in the intensity of caseins bands and the appearance of new protein fractions with high molecular weights. However, the changes in the intensity of the whey proteins bands were not sufficiently clear as caseins. The cheese hardness was significantly (P < 0.05) affected by adding MTGase. Cheese containing 80 U of MTGase had the highest hardness value compared to control and other treated samples. The antioxidant activity of cheese was negatively influenced by adding the enzyme. The use of MTGase enhanced the mouthfeel, texture and overall acceptability of cheese. However, the effect of MTGase concentration and addition time was not significant (P > 0.05) on the sensory attributes. In conclusion, adding MTGase to milk at concentration of 80 U after 20 min of renneting is recommended to improve the yield, textural and some sensory properties of fresh soft cheese made from camel milk.

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Section: Introductionmentioning

confidence: 99%

“…due to the high susceptibility of κ-casein to MTGase. The insertion of κ-casein in the crosslinks induced by MTGase may prevent cleavage of κ-casein hence suppress the primary stage of coagulation[22].…”

mentioning

confidence: 99%

The Impact of Microbial Transglutaminase on the Quality and Antioxidant Activity of Camel-Milk Soft Cheese

Abou-Soliman¹,

Awad²,

El-Sayed³

2020

FNS

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“…in TG‐modified yoghurt and by Domagała et al . in TG‐modified milk protein . The differences in curd microstructure lead to differences in textural and rheological properties and gel syneresis.…”

Section: Discussionmentioning

confidence: 99%

“…A similar phenomenon was observed by Tsevdou et al in TG-modified yoghurt and by Domagała et al in TG-modified milk protein. 41,42 The differences in curd microstructure lead to differences in textural and rheological properties and gel syneresis. In general, the propensity of gels to show syneresis increases with increasing pore size.…”

Section: Discussionmentioning

confidence: 99%

Effect of transglutaminase on rennet‐induced gelation of skim milk and soymilk mixtures

Han

Mei

et al. 2018

J Sci Food Agric

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BACKGROUND Protein gels made from cow milk and soymilk can yield products of exceptional value. Transglutaminase (TG) affect rennet‐induced gelation of proteins, and improves the functionality of the final products. In this paper, TG and rennet were added to skim milk and soymilk mixtures simultaneously, and the rennet‐induced coagulation was studied. Diffusing wave spectroscopy and rheology measurements were used to access the structural changes of the mixtures during renneting. Syneresis analysis and microscopy can give more information for understanding the system. RESULTS Soymilk and TG have synergetic effects and inhibit rennet‐induced gelation to a certain degree. With increasing soymilk and TG, elastic index and storage modulus decreased, gelation time was delayed, and curd yield and moisture content increased. At excess soymilk and TG, no curds can be formed. There were significant effects of soymilk and TG on curd microstructure. Soymilk inhibited the aggregation of casein micelles and contributed to more coarse and heterogeneous networks. TG limited reorganization of the proteins, leading to more homogenous networks with small pores. CONCLUSION The use of soymilk and TG simultaneously impair rennet‐induced gelation and curd syneresis, and consequently lead to a higher yield of high‐moisture curd. © 2018 Society of Chemical Industry

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“…amino acid compositions, molecular weights, hydrophobicity, etc.) and extrinsic (protein concentrations, pH value, temperature, metal ions, and ionic strengths) factors all show impacts on gelation and physiochemical properties of protein gels.During the last years, transglutaminase (TGase, EC 2.3.2.13) has been used to modify proteins via inducing protein cross-linking (between glutamine and lysine residues of the proteins) (Anema & Kruif 2012;Domagała et al 2015). TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al 2013), and thus improve water retention (Schorsch et al 2000;Ercili-Cura et al 2013) and texture (Ercili-Cura et al 2010) of protein gels.…”

mentioning

confidence: 99%

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

Song¹,

Zhao²

2016

Czech J. Food Sci.

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Milk gels have both traditional and high commercial value within the dairy industry (Schorsch et al. 2000;Siamand et al. 2014). Besides renneting, acidification of milk is the most routine way to form milk protein gels. Acidifying milk using glucono-δ-lactone (GDL) can slowly form structured gel products (Lucey 2004). Two major steps are involved in the formation of the acidified milk gels. In the first step, a collapse of the hairy brush of the casein micelles occurs, and the colloidal calcium and phosphate are then dissolved out of the casein micelle as a result of the protonation of ionised phosphate groups (Gaygadzhiev et al. 2009). Micellar structure is thus profoundly altered but without dissociation. In the second step, at a pH value about 5.0, casein precipitates isoelectrically, or under quiescent conditions it forms rather fragile gels (Lucey 2004). The balance between attractive and repulsive forces within protein molecules results in gel formation (Havea 2006;Rocha et al. 2009). Both intrinsic (e.g. amino acid compositions, molecular weights, hydrophobicity, etc.) and extrinsic (protein concentrations, pH value, temperature, metal ions, and ionic strengths) factors all show impacts on gelation and physiochemical properties of protein gels.During the last years, transglutaminase (TGase, EC 2.3.2.13) has been used to modify proteins via inducing protein cross-linking (between glutamine and lysine residues of the proteins) (Anema & Kruif 2012;Domagała et al. 2015). TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al. 2013), and thus improve water retention (Schorsch et al. 2000;Ercili-Cura et al. 2013) and texture (Ercili-Cura et al. 2010) of protein gels. 564Food Technology and Economy, Engineering and Physical Properties Czech J. Food Sci., 34, 2016 (6) Caseinate, transglutaminase (TGase), and an oligochitosan of 1 kDa were used to prepare a glycated and cross-linked caseinate (GC-caseinate), aiming to assess potential changes in both the structure and gelling properties of such caseinate. The results of Fourier transform infrared analysis revealed that only GC-caseinate contained saccharide portions in its molecules, evidencing TGase-induced caseinate glycation. Circular dichroism results showed that GC-caseinate possessed a more ordered secondary structure than caseinate. Other results also demonstrated that TGase-induced modification resulted in a lower gelation temperature of GC-caseinate (59°C vs. 68°C) and increased the final tan δ value (0.30 vs. 0.15) compared to caseinate during the development of acidified gels. In addition, the acidified gels from GC-caseinate were detected to have lower water holding capacity (0.720 vs. 0.781 g/g gels), expanded gel network, and larger pore sizes than those from caseinate. It is thus evidenced that the used TGase-induced modification could confer caseinate with ordered secondary structure, expanded gel network but lower water holding capacity.

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Influence of milk protein cross‐linking by transglutaminase on the rennet coagulation time and the gel properties

Abstract: Rennet cheese with modified textural and nutritional properties and improved yield can be obtained upon TGase modification but simultaneous addition of rennet and TGase is recommended. © 2015 Society of Chemical Industry.

Cited by 32 publications

References 33 publications

The Impact of Microbial Transglutaminase on the Quality and Antioxidant Activity of Camel-Milk Soft Cheese

The Impact of Microbial Transglutaminase on the Quality and Antioxidant Activity of Camel-Milk Soft Cheese

Effect of transglutaminase on rennet‐induced gelation of skim milk and soymilk mixtures

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

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