Purification and preliminary characterization of a thermostable lactase from Bacillus coagulans T242

被引：0
|
作者：
Jiang, Shu-juan [1 ]
Mu, Guangqing [1 ]
Liu, Tao [1 ]
Qian, Fang [1 ]
机构：
[1] Dalian Polytech Univ, Sch Food Engn, Dalian 116034, Peoples R China
来源：
MATERIAL DESIGN, PROCESSING AND APPLICATIONS, PARTS 1-4 | 2013年 / 690-693卷
关键词：
Lactase; Bacillus coagulans; Purification; Characterization;
D O I：
10.4028/www.scientific.net/AMR.690-693.1362
中图分类号：
T [工业技术];
学科分类号：
08 ;
摘要：
A thermostable lactase from Bacillus coagulans T242 was subjected to purification on DEAE chromatography followed by gel permeation chromatography, then the homogenous Bacillus coagulans T242-lactase was obtained, and its molecular mass was 55.0 kDa as shown in SDS-PAGE. Analysis indicated its optimum condition was 60 degrees C and pH 6.8 and it was stable at 40 similar to 60 degrees C and pH6.5 similar to 7.8; Mn2+, Mg2+ and Na+ at high concentration all had marked activation on lactase activity. Kinetic constants determination revealed Bacillus coagulans T242-lactase had a strong affinity for lactose.
引用
收藏
页码：1362 / 1365
页数：4
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