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Glycoconj J. 1998 Feb;15(2):155-60.

Purification and properties of recombinant beta-galactosidase from Bacillus circulans.

Author information

1
Meiji Institute of Health Science, Naruda Odawara, Japan. RXG01204@niftyserve.or.jp

Abstract

A gene encoding beta-galactosidase from Bacillus circulans which had hydrolysis specificity for the beta1-3 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 beta1-3 linked galactose residues. However it did not hydrolyse beta1-4 linked galactooligosaccharides. Moreover, Galbeta1-3GlcNAc, Galbeta1-3GalNAc, and their p-nitrophenyl glycosides were regioselectively synthesized in 10-46% yield by the transglycosylation reaction using this enzyme.

PMID:
9557875
DOI:
10.1023/a:1006916222187
[Indexed for MEDLINE]

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