Role of the Phosphoryl Group of β-Casein in Milk Curdling
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概要
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β-Casein was modified by trypsin, chymosin or phosphoprotein phosphatase. Each modified β-casein was fortified to the test-milk which was pretreated at 10°C by immobilized thermolysin to curdle non-enzymatically at 35°C. Fortification with chymosin-modified β-casein, devoid of the hydrophobic moiety near the C-terminus, increased the curd tension as did native β-casein. The test-milk fortified with trypsin-modified β-casein, which has been deleted some part of the hydrophilic region near the N-terminus, had similar curd tension to unfortified test-milk. The test-milk fortified with dephosphorylated β-casein, formed a softer curd than that with native β-casein. Trypsin-modified β-casein or dephosphorylated β-casein retained its associative ability, but chymosin-modified β-casein revealed negligible ability to associate. These results led to the conclusion that the phosphoryl group on the hydrophilic moiety of β-casein contributes to the increase in curd tension, while the hydrophobic moiety is responsible for the association of β-casein.
- 社団法人 日本農芸化学会の論文
著者
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Ohmiya Kunio
Department Of Bioresources School Of Bioresources Mie University
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SHIMIZU Shoichi
Department of Applied Chemistry, Shibaura Institute of Technology
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YUN Se-Eok
Department of Food Science and Technology, Faculty of Agriculture, Nagoya University
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