食品科学 ›› 2007, Vol. 28 ›› Issue (2): 209-214.

• 生物工程 • 上一篇    下一篇

源于不同菌种的谷氨酰胺转胺酶的特性研究

 马微, 李春, 付丽, 王海波, 张兰威   

  1. 东宁出入境检验检疫局; 东北农业大学; 郑州牧业工程高等学校; 哈尔滨工业大学 黑龙江东宁157200; 黑龙江哈尔滨150030; 河南郑州450011; 黑龙江东宁157200;
  • 出版日期:2007-02-15 发布日期:2011-12-31

Study on Tansglutaminase Characteristics of Different Bacillus Strains

 MA  Wei, LI  Chun, FU  Li, WANG  Hai-Bo, ZHANG  Lan-Wei   

  1. 1.Dongning Entry-Exit inspection and Quarantine Bureau, Dongning 157200, China;2.Northeast Agricultural University, Harbin 150030, China;3.Zhengzhou College of Animal Husbandry Engineering, Zhengzhou 450011, China; 4.Harbin Institute of Technology, Haerbin 150030, China
  • Online:2007-02-15 Published:2011-12-31

摘要: 本文对TG-K和TG-N的特性进行对比研究发现:TG-K和TG-N粗酶酶活分别为11.32、9.41U/ml;对酶进行分离纯化的步骤越多,酶活力和蛋白含量就损失的越多,但是TG-K降低的幅度比TG-N小;经SDS-PAGE凝胶电泳可知TG-K的分子量为41.5kDa,而TG-N的分子量为39.6kDa,不同离子对TG-K和TG-N交联酪蛋白的影响不尽相同;经扫描电镜对酸奶凝块的超微结构进行观察,证实TG-K比TG-N更适合催化交联酪蛋白。

关键词: 谷氨酰胺转胺酶, 不同菌种, SDS-PAGE, 酶活力, 超微结构

Abstract: This paper mainly studied the characteritics of TG-K and TG-N apparently. The crude enzyme activity of TG-K and TG-N were 11.32U/ml and 9.41U/ml respectively. The results showed that the more separated and purification steps, the less of enzyme activity and protein contents, but the loweling level of TG-N was less than TG-K. The molecular weight of TG- K is 41.5 kDa and while that of TG-N 39.6kDa by SDS-PAGE. The different ionics have different effects on cross-linking casein of TG-K or TG-N. It has proved that TG-K is better to cross-linked casein observing the ultra structure of yoghourt by EM.

Key words: transglutaminase, different strains, SDS-PAGE, enzyme activity, ultra structure