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。
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.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2007年第2期209-214,共6页
Food Science
