Abstract
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 C and pH 6.8 and it was stable at 40~60 C and pH6.5~7.8; 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.
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