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作 者:张若愚[1] 侯东丽[1] 师俊玲[1] 杨保伟[1]
机构地区:[1]西北农林科技大学食品科学与工程系,陕西杨凌712100
出 处:《食品工业科技》2010年第10期206-209,共4页Science and Technology of Food Industry
基 金:国家大学生创新性实验计划项目(071071238);西北农林科技大学基金(07ZR03)
摘 要:在分离获得清蛋白、球蛋白、醇溶蛋白单一组分的基础上,研究了微生物源谷氨酰胺转胺酶(MTG)对这些蛋白组分在单蛋白、双蛋白及三蛋白水平上,分子内及分子间结合的催化作用;通过可溶性蛋白含量和电泳图谱中蛋白条带的变化,从反应速度和分子量的变化探究了MTG对除麦谷蛋白以外的其它蛋白组分的作用效果及机制。结果发现,MTG可以催化小麦中清蛋白、球蛋白和醇溶蛋白组分的分子内和分子间的作用;对球蛋白的催化作用大于清蛋白,但两者均小于醇溶蛋白;清蛋白对MTG催化其它蛋白组分的分子内结合,球蛋白对MTG催化醇溶蛋白分子内结合都有一定的抑制作用。The effects of transglutaminase on the reaction within wheat albumin, globulin and gliadin when one,two, and three of them appeared were studied, respectively.All the above proteins were isolated from wheat flour and reconstructed again for different experimental designs. Decrease of soluble protein content in the system was tested to ex^ress the reaction speed.Compositions before and after the reaction were analyzed by using SDS- PAGE.The results showed that MTG could catalyze the interactions within a same, or between different proteins, including albumin,globulin,and gliadin.The catalyzing speed was faster on globulin than albumin and fastest on giiadin at single protein level.Albumin could reduce the catalyzing effect of MTG on the interaction of globulin and gliadin,while globulin increased the effect on gliadin.
分 类 号:TS201.2[轻工技术与工程—食品科学]
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