Gelation Mechanism of Protein Solution by Transglutaminase
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概要
- 論文の詳細を見る
Transglutaminase catalyzes the formation of ε-(γ-glutamyl)lysyl cross-links within and between protein molecules. Therefore, transglutaminase polymerizes proteins through the formation of isopeptide bonds. We have reported that several high-concentration protein solutions formed firm gels when they were incubated with transglutaminase. This paper presents unambiguous evidence that αs1-casein solution is gelled by the formation of ε-(γ-glutamyl)lysyl cross-links. Gelation of αs1-casein was effected by the amount of transglutaminase and pH value, and αs1-casein gel was not dissolved by various denaturants. Succinylated αs1-casein, in which E-amino groups of lysine residues are blocked, was not gelled by transglutaminase. Therefore, it is confirmed that αs1-casein is formed by the action of transglutaminase.
- 社団法人 日本農芸化学会の論文
著者
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Nio Noriki
Central Research Laboratories, Ajinomoto Co., Inc.
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Motoki Masao
Central Research Laboratories Ajinomoto Co. Inc.
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Takinami Koichi
Central Research Laboratories Ajinomoto Co. Inc.
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TAKINAMI Koichi
Central Research Laboratories, Ajinomoto Co., Inc.
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