Crosslinking of casein by microbial transglutaminase and its resulting influence on the stability of micelle structure

Partschefeld, Claudia; Schwarzenbolz, Uwe; Richter, Sven; Henle, Thomas

doi:10.1002/biot.200600232

Cited by 35 publications

(20 citation statements)

References 28 publications

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“…Hydrophobic nutraceuticals, such as curcumin (Sahu et al ., 2008 ), omega-3 fatty acids (Zimet et al ., 2011 ) andvitamin D2 (Semo et al ., 2007 ), can be incorporated into casein micelles. The casein micelle can be further stabilized by cross-linking with transglutaminase (Partschefeld et al ., 2007 ). The enzymatic cross-linking creates nanogel particles that show improved heat stability but lower stability at acidic pH than native casein micelles (Huppertz and de Kruif, 2008 ).…”

Section: Self-assembling Proteins and Peptidesmentioning

confidence: 99%

An overview of the development and applications of nanoscale materials in the food industry

Augustin

Oliver

2012

Nanotechnology in the Food, Beverage and Nutraceutical Industries

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Section: Self-assembling Proteins and Peptidesmentioning

confidence: 99%

An overview of the development and applications of nanoscale materials in the food industry

Augustin

Oliver

2012

Nanotechnology in the Food, Beverage and Nutraceutical Industries

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“…[30] When TGase was used to treat the ultra-high temperature-treated milk, larger hydrodynamic radius and enhanced micellar stability were observed, and formation of intra-micellar iso-peptide bonds in milk proteins was responsible for the enlarged radius. [31] Similarly, both GC-caseinate I and II were crosslinked protein products by TGase with larger hydrodynamic radius and enhanced aggregation than sodium caseinate. GC-caseinate I had slightly larger hydrodynamic radius than GC-caseinate II, because it was much crosslinked during preparation.…”

Section: Other Properties Of Gc-caseinate I and Iimentioning

confidence: 99%

Structure and Property Changes of Transglutaminase-Induced Modification of Sodium Caseinate in the Presence of Oligochitosan of 5 kDa

Zhao

2016

International Journal of Food Properties

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Sodium caseinate was modified by transglutaminase-catalyzed reaction in the presence of oligochitosan of 5 kDa at two different levels, aiming to generate two glycated and crosslinked caseinate products (GC-caseinate I and II) and to clarify their respective structure and property changes. Electrophoretic analysis with aid of protein and saccharide staining confirmed that both GC-caseinate I and II were glycated and crosslinked protein products, while high-performance liquid chromatrography analysis demonstrated that both GC-caseinate I and II contained glucosamine (12.8 and 30.8 g/kg protein, respectively). In comparison with sodium caseinate, GC-caseinate I and II also contained less reactable-NH 2 groups (0.50 and 0.52 versus 0.62 mol/kg protein), more-OH groups in their molecules, but they had more ordered secondary structure than sodium caseinate. In addition, GC-caseinate I and II showed higher water-binding capacity, larger hydrodynamic radius (173.9 and 168.2 versus 145.3 nm), and larger negative zeta-potential (-32.9 and-30.9 versus-27.6 mV) in aqueous dispersions, but they exhibited lower thermal stability (namely, greater mass loss) at temperature higher than 286ºC. Oligochitosan-glycated sodium caseinate at lower and higher extents was observed to be unfavorable and favorable to the in vitro digestibility of GC-caseinate I and II, respectively. It is concluded that application of transglutaminase and the oligochitosan can modify structure and property of sodium caseinate to generate new protein ingredients with good hydration and colloidal stability.

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“…It was observed that caseins cross-linked by TGase have better stability in their micellar structure. 10 When caseinate was crosslinked and glucosamine-conjugated under the action of TGase, its emulsifying, foaming and rheological properties were improved. 11 Moreover, a ternary system comprising the three elements horseradish peroxidase (HRP; EC 1.11.1.7), glucose oxidase (EC 1.1.3.4) and D-glucose was also used to induce the crosslinking of several proteins like SPI, caseinate and gelatin.…”

Section: Introductionmentioning

confidence: 99%

Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

Chang

et al. 2020

J Sci Food Agric

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BACKGROUND: A ternary system containing horseradish peroxidase (HRP), glucose oxidase and D-glucose using one-or twostep treatment was evidently able to cross-link proteins via dityrosine formation and thus was assessed for its possible impact on several properties of a protein ingredient caseinate. RESULTS: HRP, glucose oxidase and D-glucose were used at 200 U, 6 U and 0.05 mmol g −1 protein to treat caseinate by one-and two-step methods, producing two cross-linked caseinates named CLCN-I and CLCN-II, respectively. In response to the conducted cross-linking, both CLCN-I and CLCN-II gained slightly reduced dispersibility at pH 5-10, enlarged hydrodynamic radius (particle size distribution, 266.37 and 258.33 versus 226.67 nm) and negative zeta-potential (−26.60 and −22.27 versus −14.30 mV) in dispersions, increased water-binding (3.70 and 3.09 versus 2.68 kg kg −1 protein), decreased oil-binding (1.75 and 2.74 versus 2.87 kg kg −1 protein) and emulsifying activity (76.2 and 82.3 versus 94.3 m 2 g −1 protein), increased emulsion stability (84.3% and 82.5% versus 78.6%), and enhanced thermal stability with lower mass loss (58.5% and 59.6% versus 64.3%) or higher decomposition temperatures (331.2°C and 328.7°C versus 327.6°C) upon heating at 105-450°C. In addition, CLCN-I and CLCN-II had decreased gelling temperatures and shortened gelling times when forming acid-induced gels, and the gels were endowed with increased values in four textural indices and finer microstructure. Moreover, CLCN-I with a higher cross-linking extent showed greater property changes than CLCN-II. CONCLUSION: This ternary system could be used in caseinate cross-linking to improve properties such as aggregation, emulsification, gelation and thermal stability.

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Crosslinking of casein by microbial transglutaminase and its resulting influence on the stability of micelle structure

Cited by 35 publications

References 28 publications

An overview of the development and applications of nanoscale materials in the food industry

An overview of the development and applications of nanoscale materials in the food industry

Structure and Property Changes of Transglutaminase-Induced Modification of Sodium Caseinate in the Presence of Oligochitosan of 5 kDa

Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

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