Microwave-assisted cross-linking of milk proteins induced by microbial transglutaminase

Chen, Chun‐Chi; Hsieh, Jung-Feng

doi:10.1038/srep39040

Cited by 14 publications

(14 citation statements)

References 37 publications

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“…Both casein and whey α-lactalbumin and β-lactoglobulin are excellent acyl donors and/or acceptors substrates for transglutaminase, although some differences between them apply in relation to the crosslinking reaction (Faergemand and Qvist 1997;Oner et al 2008;Rodriguez-Nogales 2006;Rossa et al 2011). According to a study by Chen and Hsieh (2016), in a cascade reaction, mTGase catalyzes the cross-linking of κ-casein (κ-CN) and β-casein (β-CN) before it proceeds to crosslink the serum albumin (AS), α-lactalbumin (α-LA), α s1casein (α s1 -CN), α s2 -casein (α s2 -CN), and β-lactoglobulin (β-LG) moieties, as shown in Fig. 2.…”

Section: Dairy Productsmentioning

confidence: 99%

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Duarte

Matte

Bizarro

et al. 2019

World J Microbiol Biotechnol

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Because of their protein cross-linking properties, transglutaminases are widely used in several industrial processes, including the food and pharmaceutical industries. Transglutaminases obtained from animal tissues and organs, the first sources of this enzyme, are being replaced by microbial sources, which are cheaper and easier to produce and purify. Since the discovery of microbial transglutaminase (mTGase), the enzyme has been produced for industrial applications by traditional fermentation process using the bacterium Streptomyces mobaraensis. Several studies have been carried out in this field to increase the enzyme industrial productivity. Researches on gene expression encoding transglutaminase biosynthesis were performed in Streptomyces lividans, Escherichia coli, Corynebacterium glutamicum, Yarrowia lipolytica, and Pichia pastoris. In the first part of this review, we presented an overview of the literature on the origins, types, mediated reactions, and general characterizations of these important enzymes, as well as the studies on recombinant microbial transglutaminases. In this second part, we focus on the application versatility of mTGase in three broad areas: food, pharmacological, and biotechnological industries. The use of mTGase is presented for several food groups, showing possibilities of applications and challenges to further improve the quality of the end-products. Some applications in the textile and leather industries are also reviewed, as well as special applications in the PEGylation reaction, in the production of antibody drug conjugates, and in regenerative medicine.

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Section: Dairy Productsmentioning

confidence: 99%

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Duarte

Matte

Bizarro

et al. 2019

World J Microbiol Biotechnol

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“…Cross-linking of milk proteins by TGase was analysed via two-dimensional gel electrophoresis by Hsieh & Pan [126] and Chen & Hsieh [127]. In contrast to the aforementioned studies on non-enzymatic cross-linking, almost no polymeric components were visible on the gels.…”

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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Abstract:Casein is the major protein fraction in milk, and its cross-linking has been a topic of scientific interest for many years. Enzymatic cross-linking has huge potential to modify relevant techno-functional properties of casein, whereas non-enzymatic cross-linking occurs naturally during the storage and processing of milk and dairy products. Two size separation techniques were applied for characterisation of these reactions: gel electrophoresis and size exclusion chromatography. This review summarises their separation principles and discusses the outcome of studies on cross-linked casein from the last~20 years. Both methods, however, show limitations concerning separation range and are applied mainly under denaturing and reducing conditions. In contrast, field flow fractionation has a broad separation range and can be easily applied under native conditions. Although this method has become a powerful tool in polymer and nanoparticle analysis and was used in few studies on casein micelles, it has not yet been applied to investigate cross-linked casein. Finally, the principles and requirements for absolute molar mass determination are reviewed, which will be of increased interest in the future since suitable calibration substances for casein polymers are scarce.

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“…Crosslinking the proteins with transglutaminase (TGase, EC 2.3.2.13) is one method to modify the functionality and structural properties of proteins such as caseins and WP. Transglutaminase catalyzes the acyl transfer reaction between the protein-bound glutaminyl residues and the primary amines (Folk and Finlayson, 1977;Chen and Hsieh, 2016;Raak et al, 2018). Transglutaminase has the potential to modify the physical properties of caseins by covalently crosslinking the caseins and thereby reducing the steric stability of κ-CN.…”

Section: Introductionmentioning

confidence: 99%

Use of micellar casein concentrate and milk protein concentrate treated with transglutaminase in imitation cheese products—Unmelted texture

Salunke

Marella

Amamcharla

et al. 2022

Journal of Dairy Science

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The amount of intact casein provided by dairy ingredients is a critical parameter in dairy-based imitation mozzarella cheese (IMC) formulation because it has a significant effect on unmelted textural parameters such as hardness. From a functionality perspective, rennet casein (RCN) is the preferred ingredient. Milk protein concentrate (MPC) and micellar casein concentrate (MCC) cannot provide the required functionality due to the higher steric stability of casein micelle. However, the use of transglutaminase (TGase) has the potential to modify the surface properties of MPC and MCC and may improve their functionality in IMC. The objective of this study was to determine the effect of TGasetreated MPC and MCC powders on the unmelted textural properties of IMC and compare them with IMC made using commercially available RCN. Additionally, we studied the degree of crosslinking by TGase in MPC and MCC retentates using capillary gel electrophoresis. Three lots of MCC and MPC retentate were produced from pasteurized skim milk via microfiltration and ultrafiltration, respectively, and randomly assigned to 1 of 3 treatments: no TGase (control); low TGase: 0.3 units/g of protein; and high TGase: 3.0 units/g of protein, followed by inactivation of enzyme (72°C for 10 min), and spray drying. Each MCC, MPC, and RCN was then used to formulate IMC that was standardized to 21% fat, 1% salt, 48% moisture, and 20% protein.The IMC were manufactured by blending, mixing, and heating ingredients (4.0 kg) in a twin-screw cooker. The capillary gel electrophoresis analysis showed extensive inter-and intramolecular crosslinking. The IMC formulation using the highest TGase level in MCC or MPC did not form an emulsion because of extensive crosslinking. In MPC with a high level of TGase, whey protein and casein crosslinking were observed. In contrast, crosslinking and hydrolysis of proteins were observed in MCC. The IMC made from MCC powder had significantly higher texture profile analysis hardness compared with the corresponding MPC powder. Further, many-to-one (multiple) comparisons using the Dunnett test showed no significant differences between IMC made using RCN and treatment powders in hardness. Our results demonstrated that TGase treatment causes crosslinking hydrolysis of MCC and MPC at higher TGase levels, and MPC and MCC have the potential to be used as ingredients in IMC applications.

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Microwave-assisted cross-linking of milk proteins induced by microbial transglutaminase

Cited by 14 publications

References 37 publications

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Use of micellar casein concentrate and milk protein concentrate treated with transglutaminase in imitation cheese products—Unmelted texture

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