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Effects of the thermal denaturation degree of a whey protein isolate on the strength of acid milk gels and the dissociation of κ-casein

Published online by Cambridge University Press:  03 March 2022

Daiki Oka ,
Wataru Ono ,
Shojiro Tamaki ,
Tomohiro Noguchi  and
Katsumi Takano
Daiki Oka*
Affiliation:
Department of Agricultural Chemistry, Tokyo University of Agriculture, Tokyo 156-8502, Japan
Wataru Ono
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan
Shojiro Tamaki
Affiliation:
Milk Science Research Institute, Megmilk Snow Brand Co., Ltd., Saitama 350-1165, Japan
Tomohiro Noguchi
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan
Katsumi Takano
Affiliation:
Department of Agricultural Chemistry, Tokyo University of Agriculture, Tokyo 156-8502, Japan
*
Author for correspondence: Daiki Oka, Email: d3oka@nodai.ac.jp
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Abstract

In this study, the effects of the degree of thermal denaturation of whey protein (WP) added to milk on the dissociation of κ-casein from casein micelles were investigated, since they are related to the strength of acid milk gel and its factors. Acid milk gels were prepared by heating thermally denatured WP isolate (WPI) and undenatured milk mixtures and treating them with glucono-δ-lactone as a coagulant. The strength of these gels was negatively correlated with the WPI denaturation degree and strongly positively correlated with the extent of κ-casein dissociation from casein micelles. This behavior was ascribed to the fact that α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) contained in WPI denatured after heating and engaged in disulfide bond formation with each other. With an increase in the degree of denaturation and disulfide bond formation, the bonding between β-lactoglobulin and κ-casein was suppressed to decrease the amount of κ-casein–WPI complexes. When β-Lg forms SS bonds with α-La, the number of highly reactive, free SH groups decreases, which complicates the formation of SS bridges between β-Lg and κ-casein. Thus, the denaturation degree of WPI largely determined the degree of κ-casein dissociation from casein micelles and, consequently, the strength of acid milk gels. Adding WP to milk increases the strength of acid milk gel, and it can be controlled by changing the degree of thermal denaturation of the WP. Furthermore, it was clarified for the first time that the dissociation of κ-casein from casein micelles influences this effect. Further studies are needed to elucidate the structural features of κ-casein-dissociated micelles.

Keywords

Casein micellewhey protein isolateβ-lactoglobulinκ-casein
Type
Research Article
Information
Journal of Dairy Research , Volume 89 , Issue 1 , February 2022 , pp. 104 - 108
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press on behalf of Hannah Dairy Research Foundation

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