作　　者： ; ; ; ;

机构地区： 华南理工大学食品与生物工程学院

出　　处： 《食品科学》 2003年第6期23-27,共5页

摘　　要： 首次提出微生物转谷氨酰胺酶(MTGase)催化球状蛋白质的催化机理,同时显示MTGase聚合球蛋白存在一个“诱导期”,在该阶段底物蛋白的构象发生一定的变化,后者提高了MTGase对它们的催化活性。以β-乳球蛋白为例,采用紫外光谱(UVspectrum)和红外光谱(FT-IRspectrum)证实了MTGase催化球状蛋白,确实致使后者的空间结构发生了明显的变化。该论文所提出的MTGase催化球蛋白的聚合机理在一定程度上解释了MTGase改性蛋白质的机制,也为MTGase的进一步应用研究提供了理论指导。 The catalytic mechanism of microbial transglutaminase (MTGase) towards globular proteins was proposed for the firsttime.It was shown that there was an “induction phase”during the polymerization of globular proteins by MTGase,and thespatial structures of substrate proteins distinctly changed. The changes of structure improved the catalytic activity of MTGaseagainst globular proteins.β-lactoglubolin (β-LG) was chosen as the example. It was proved that catalysis of MTGase againtβ-LG did make the spatial structure ofβ-LG change remarkably.This catalytic mechanism of MTGase against globular proteinsproposed in this paper to a certein extent could explain the mechanism of modification of proteins by MTGase,and also providedirection for the more application of MTGase in different fields.

关 键 词： 微生物转谷氨酰胺酶 催化机理 球状蛋白质 聚合机理 乳球蛋白 底物

领　　域： [轻工技术与工程] [轻工技术与工程]