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Effect of heat-induced κ-casein dissociation on acid coagulation of milk

Published online by Cambridge University Press:  22 February 2018

Daiki Oka ,
Wataru Ono ,
Shintarou Ohara ,
Tomohiro Noguchi  and
Katsumi Takano
Daiki Oka*
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Wataru Ono
Affiliation:
Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Shintarou Ohara
Affiliation:
Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Tomohiro Noguchi
Affiliation:
Food Processing Technology Center, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
Katsumi Takano
Affiliation:
Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1, Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
*
*For correspondence; e-mail: d3oka@nodai.ac.jp
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Abstract

In this study, the relationship between the dissociation of κ-casein from casein micelles due to heat-induced denaturation and the strength of acid milk gel was investigated. The κ-casein-dissociated micelles were fractionated by gel filtration chromatography and two-dimensional polyacrylamide gel electrophoresis, and their zeta potential and surface hydrophobicity were measured. The negative charge of the κ-casein-dissociated micelles was lower than that of native micelles, and micellar surface hydrophobicity was higher. For confirmation, the isoelectric point of the casein micelles was measured. The κ-casein-dissociated micelles were found to cohere at an earlier stage of acidification than the native micelles. These results demonstrated that the heat-induced increase in the strength of acid milk gel was partly due to the decrease in micellar surface charge and partly to the increase in surface hydrophobicity caused by the dissociation of κ-casein.

Keywords

κ-caseinYogurtheat-denaturationcasein micellesnegative charge

Information

Type
Research Article
Information
Journal of Dairy Research , Volume 85 , Issue 1 , February 2018 , pp. 104 - 109
Copyright
Copyright © Hannah Dairy Research Foundation 2018 

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