| Literature DB >> 9557875 |
H Fujimoto1, M Miyasato, Y Ito, T Sasaki, K Ajisaka.
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.Entities:
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Year: 1998 PMID: 9557875 DOI: 10.1023/a:1006916222187
Source DB: PubMed Journal: Glycoconj J ISSN: 0282-0080 Impact factor: 2.916