Effects of Ca2+ and Sulfhydryl Reductant on the Polymerization of Soybean Glycinin Catalyzed by Mammalian and Microbial Transglutaminases

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• 作者：Guoyan Zhang ; Yasuki Matsumura ; Shinya Matsumoto ; Yukako Hayashi ; and Tomohiko Mori
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2003
• 出版时间：January 1, 2003
• 年：2003
• 卷：51
• 期：1
• 页码：236 - 243
• 全文大小：237K
• 年卷期：v.51,no.1(January 1, 2003)
• ISSN：1520-5118

文摘

Two types of transglutaminases (TGases), Ca²⁺-dependent TGase derived from guinea pig liver(GTGase) and Ca²⁺-independent TGase derived from a variant of Streptoverticillium mobaraense(MTGase), were used to study the cross-linking of soybean 11S globulin (glycinin). The effects ofsulfhydryl reductant (dithiothreitol, DTT) and Ca²⁺ on the conformation and TGase-catalyzedpolymerization of glycinin were investigated. The conformational change of glycinin was probed byspectral methods. The degree of cross-linking and the polymer (aggregate) formation were analyzedby sodium dodecyl sulfate-polyacrylamide gel electrophoresis and dynamic light scattering,respectively. Addition of DTT stimulated the TGase-catalyzed cross-linking reactions without destroyingthe secondary and tertiary structure of glycinin but did not influence the polymer or aggregate formation.It was found that Ca²⁺ caused the formation of larger size polymers at lower concentrations, while itsuppressed the polymerization at higher concentrations. In addition, the cross-linking behaviors ofglycinin were shown to be different between MTGase- and GTGase-catalyzed systems.Keywords: Transglutaminase; polymerization; glycinin