摘要
对自行从土壤中筛选分离出的一株能合成海糖藻的菌株T007的酶学特性进行了研究。该酶最适反应温度为38～40℃,最适反应pH为pH6.6～7.2,Mg2+、K+对该酶有一定的激活作用,Ca2+、Ba2+、Mn2+对该酶有抑制作用,而Zn2+、Cu2+、Hg2+则可强烈地抑制该酶活力。试验证实,该菌株是在海藻糖合酶(trehalosesynthase)作用下特异性地以麦芽糖为底物转化为海藻糖的。该细胞酶在4℃保存14d酶活力仍保持稳定,-18℃保存期可延长到30d。
The enzymatical properties of strain T007 producing trehalose were studied. The enzyme had high substrate speciality. It could transfer maltose into trehalose specificly and was named as trehalose synthase. The optimal temperature ranged from 38℃ to 40℃. The optimal pH from 6.6 to 7.2. Mg^2＋, K^＋ could activate the enzyme and Ca^2＋, Ba^2＋, Mn^2＋ had the inhibition capability of its activity, while Zn^2＋, Cu^2＋, Hg^2＋ could strongly inhibit its activity. The enzyme had a good stability when kept at 4℃ for two weeks.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2006年第8期60-63,共4页
Food Science
基金
山东省中青年科学家奖励基金项目(03BS084)
关键词
海藻糖
合酶
麦芽糖
酶学特性
trehalose
synthase
maltose
enzymatical property
作者简介
刘建龙（1961-），男，高级工程师，在读博士，主要从事生物发酵技术方面的研究。
