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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
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

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.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 2012

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