Purification and properties of recombinant β-galactosidase from Bacillus circulans

被引:75
作者
Fujimoto, H [1 ]
Miyasato, M
Ito, Y
Sasaki, T
Ajisaka, K
机构
[1] Meiji Inst Hlth Sci, Naruda Odawara 250, Japan
[2] Meiji Cent Res Inst, Naruda Odawara 250, Japan
关键词
beta-galactosidase; Bacillus circulans;
D O I
10.1023/A:1006916222187
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A gene encoding beta-galactosidase from Bacillus circulans which had hydrolysis specificity for the beta 1-3 linkage was expressed in Escherichia coli. The beta-galactosidase was purified from crude cell lysates of E. coli by column chromatographies on Resource Q and Sephacryl S-200 HR. The enzyme released galactose with high selectivity from oligosaccharides which had terminal beta 1-3 linked galactose residues. However it did not hydrolyse beta 1-4 linked galactooligosaccharides. Moreover, Gal beta 1-3GlcNAc, Gal beta 1-3GalNAc, and their p-nitrophenyl glycosides were regioselectively synthesized in 10-46% yield by the transglycosylation reaction using this enzyme.
引用
收藏
页码:155 / 160
页数:6
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