Gelation Mechanism of Protein Solution by Transglutaminase
1986 年 50 巻 4 号 p. 851-855
詳細
1986 年 50 巻 4 号 p. 851-855
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.
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