Characterisation of a thermostable family 42 β-galactosidase (BgalC) family from Thermotoga maritima showing efficient lactose hydrolysis
作者： Priti Katrolia , Min Zhang , Qiaojuan Yan , Zhengqiang Jiang , Chunlei Song
DOI: 10.1016/J.FOODCHEM.2010.08.075
关键词:
摘要: Abstract A β-galactosidase gene (TM_1195) of Thermotoga maritima was cloned and expressed in Escherichia coli . The recombinant (BgalC), belonging to glycosyl hydrolase (GH) family 42, purified homogeneity with 23.4-fold purification a recovery 36.6%. Its molecular mass estimated be 78 kDa by SDS–PAGE. BgalC exhibited maximum activity at an optimal pH 5.5 optimum temperature 80 °C. enzyme displayed important properties, such as stability over broad range 5.0–9.0 thermostability up 75 °C. K m values for p -nitrophenyl-β-galactopyranoside ( NPGal), o NPGal) lactose were 1.21, 7.31 6.5 mM, respectively. efficient complete removal from milk. is significantly one the few β-galactosidases 42 displaying significant hydrolysis lactose. These properties make ideal candidate commercial use, production lactose-free
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