Hostname: page-component-76fb5796d-2lccl Total loading time: 0 Render date: 2024-04-26T20:37:59.716Z Has data issue: false hasContentIssue false
  • English
  • Français

Susceptibility of the individual caseins in reconstituted skim milk to cross-linking by transglutaminase: influence of temperature, pH and mineral equilibria

Published online by Cambridge University Press:  31 July 2012

Katharina Hinz ,
Thom Huppertz  and
Alan L. Kelly
Katharina Hinz
Affiliation:
School of Food and Nutritional Sciences, University College Cork, Cork, Ireland
Thom Huppertz
Affiliation:
NIZO food research, Ede, The Netherlands
Alan L. Kelly*
Affiliation:
School of Food and Nutritional Sciences, University College Cork, Cork, Ireland
*
*For correspondence; e-mail: a.kelly@ucc.ie
Get access Rights & Permissions [Opens in a new window]

Abstract

The susceptibility of total casein and the individual caseins in reconstituted skim milk to transglutaminase (TGase)-induced cross-linking was studied as a function of incubation temperature (5–40 °C), pH (5·0–7·0) and mineral addition. Within the ranges studied, the level of total casein cross-linked increased with increasing temperature, pH and concentration of added trisodium citrate, whereas adding calcium chloride had the opposite effect. These effects can be largely related to the effects of these parameters on TGase activity. In addition, the parameters were also found to influence the susceptibility of κ-casein, and to a lesser extent β-casein, to cross-linking, whereas the susceptibility of αs1-casein was not affected. The susceptibility of κ-casein to cross-linking increased with increasing temperature and calcium chloride addition, but decreased with increasing pH and citrate content, whereas the susceptibility of β-casein to TGase-induced cross-linking decreased with increasing temperature, but was not affected by other parameters. These findings highlight the fact that selection of environmental conditions during cross-linking can be applied to tailor the surface, and hence possibly colloidal stability, of casein micelles in TGase-treated milk.

Keywords

Casein micellestransglutaminasecross-linkingmicelle structure
Type
Research Article
Information
Journal of Dairy Research , Volume 79 , Issue 4 , November 2012 , pp. 414 - 421
Copyright
Copyright © Proprietors of Journal of Dairy Research 2012

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Anema, SG, Lauber, S, Lee, SK, Henle, T & Klostermeyer, H 2005 Rheological properties of acid gels prepared from pressure- or transglutaminase-treated skim milk. Food Hydrocolloids 19 879–887Google Scholar
Dalgleish, DG 2011 On the structural models of bovine casein micelles—review and possible improvements. Soft Matter 7 2265–2272Google Scholar
Dalgleish, DG & Law, AJR 1988 pH-induced dissociation of bovine casein micelles. I. Analysis of liberated caseins. Journal of Dairy Research 55 529–538Google Scholar
Davies, DT & Law, AJR 1983 Variation on the protein composition of bovine casein micelles and serum casein in relation to micellar size and temperature. Journal of Dairy Research 50 67–75Google Scholar
De Kruif, CG 1999 Casein micelle interactions. International Dairy Journal 9 183–188Google Scholar
De Kruif, CG & Holt, C 2003 Casein micelle structure, functions and interactions. In Advanced Dairy Chemistry Volume 1: Proteins, pp. 233–276 (Eds Fox, PF & McSweeney, PLH). New York: Kluwer Academic/Plenum PublishersGoogle Scholar
De Kruif, CG & Roefs, SPFM 1996 Skim milk acidification at low temperatures: a model for the stability of casein micelles. Netherlands Milk and Dairy Journal 50 113–120Google Scholar
De Kruif, CG & Zhulina, EB 1996 κ-Casein as a polyelectrolyte brush on the surface of casein micelles. Colloids and Surfaces A 117 151–159Google Scholar
Hinz, K, Huppertz, T, Kulozik, U & Kelly, AL 2007 Influence of enzymatic cross-linking on milk fat globules and emulsifying properties of milk proteins. International Dairy Journal 17 289–293Google Scholar
Holt, C & Horne, DS 1996 The hairy casein micelle: evolution of the concept and its implications for dairy technology. Netherlands Milk and Dairy Journal 50 85–111Google Scholar
Huppertz, T 2009 Novel applications of enzymes in the dairy sector: optimizing functional properties of milk proteins by enzymatic cross-linking. In Dairy-Derived Ingredients, pp. 395–416 (Ed. Corredig, M). Oxford: Woodhead PublishingGoogle Scholar
Huppertz, T 2011 Restoring the rennetability of transglutaminase-treated casein micelles. Milchwissenschaft 66 175–177Google Scholar
Huppertz, T & De Kruif, CG 2007a Rennet-induced coagulation of enzymatically cross-linked casein micelles. International Dairy Journal 17 442–447CrossRefGoogle Scholar
Huppertz, T & De Kruif, CG 2007b Ethanol stability of casein micelles cross-linked by transglutaminase. International Dairy Journal 17 436–441Google Scholar
Huppertz, T & De Kruif, CG 2008 Structure and stability of nanogel particles prepared by internal cross-linking of casein micelles. International Dairy Journal 18 556–565Google Scholar
Huppertz, T & Smiddy, MA 2008 Behaviour of partially cross-linked casein micelles under high pressure. International Journal of Dairy Technology 61 51–55CrossRefGoogle Scholar
Huppertz, T, Smiddy, MA & De Kruif, CG 2007 Biocompatible protein micro-gel particles from cross-linked casein micelles. Biomacromolecules 8 1300–1305CrossRefGoogle ScholarPubMed
Ikura, K, Kometani, T, Yoshikawa, M, Sasaki, R & Chiba, H 1980 Cross-linking of casein components by transglutaminase. Agricultural and Biological Chemistry 44 1567–1573Google Scholar
Jaros, D, Jacob, M, Otto, C & Rohm, H 2010 Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels. International Dairy Journal 20 321–327Google Scholar
Jaros, D, Partschefeld, C, Henle, T & Rohm, H 2006 Transglutaminase in dairy products: chemistry, physics and applications. Journal Texture Studies 37 113–155Google Scholar
Kütemeyer, C, Froeck, M, Werlein, HD & Watkinson, BM 2005 The influence of salts and temperature on enzymatic activity of microbial transglutaminase. Food Control 16 735–737Google Scholar
Lorenzen, PC 2000a Renneting properties of transglutaminase-treated milk. Milchwissenschaft 55 433–437Google Scholar
Lorenzen, PC 2000b Techno-functional properties of transglutaminase-treated milk proteins. Milchwissenschaft 55 667–670Google Scholar
Moon, JH, Yogh, YH, Huppertz, T, Fox, PF & Kelly, AL 2009 Properties of casein micelles cross-linked by transglutaminase. International Journal of Dairy Technology 62 27–32Google Scholar
O'Sullivan, MM, Lorenzen, PC, O'Connell, JE, Kelly, AL, Schlimme, E & Fox, PF 2001 Influence of transglutaminase on the heat stability of milk. Journal of Dairy Science 84 1331–1334Google Scholar
O'Sullivan, MM, Kelly, AL & Fox, PF 2002a Influence of transglutaminase treatment on some physico-chemical properties of milk. Journal of Dairy Research 69 433–442Google Scholar
O'Sullivan, MM, Kelly, AL & Fox, PF 2002b Effect of transglutaminase on the heat stability of milk: a possible mechanism. Journal of Dairy Science 85 1–7Google Scholar
Rollema, HS & Brinkhuis, HJ 1989 A 1H-NMR study of bovine casein micelles; influence of pH, temperature and calcium ions on micellar structure. Journal of Dairy Research 56 417–425Google Scholar
Seguro, K, Nio, N & Motoki, M 1996 Some characteristics of a microbial protein cross-linking enzyme: transglutaminase. ACS Symposium Series 650 271–280Google Scholar
Sharma, R, Lorenzen, PC & Qvist, KB 2001 Influence of transglutaminase treatment of skim milk on the formulation of ε-(γ-glutamyl)lysine and susceptibility of individual proteins towards crosslinking. International Dairy Journal 11 785–793Google Scholar
Smiddy, MA, Martin, JEGH, Kelly, AL, de Kruif, CG & Huppertz, T 2006 Stability of casein micelles cross-linked by transglutaminase. Journal Dairy Science 89 1906–1914CrossRefGoogle ScholarPubMed
Tang, C, Yang, XQ, Chen, Z, Wu, H & Peng, ZY 2005 Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 29 402–421Google Scholar
Udabage, P, McKinnon, IR & Augustin, MA 2000 Mineral and casein equilibria in milk: effects of added salts and calcium-chelating agents. Journal of Dairy Research 67 361–370Google Scholar
Visser, S, Slangen, CJ & Rollema, HS 1991 Phenotyping of bovine milk proteins by reversed-phase high performance liquid chromatography. Journal of Chromatography 548 361–370Google Scholar