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Purification and properties of recombinant β-galactosidase from Bacillus circulans

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Abstract

A gene encoding β-galactosidase from Bacillus circulans which had hydrolysis specificity for the β1-3 linkage was expressed in Escherichia coli. The β-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 β1-3 linked galactose residues. However it did not hydrolyse β1-4 linked galactooligosaccharides. Moreover, Galβ1-3GlcNAc, Galβ1-3GalNAc, and their p-nitrophenyl glycosides were regioselectively synthesized in 10–46% yield by the transglycosylation reaction using this enzyme.

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Authors and Affiliations

  1. Meiji Institute of Health Science, Naruda Odawara, 250, Japan

    Hiroshi Fujimoto, Mariko Miyasato, Yoshiyuki Ito, Takashi Sasaki & Katsumi Ajisaka

Authors
  1. Hiroshi Fujimoto
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  2. Mariko Miyasato
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  3. Yoshiyuki Ito
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  4. Takashi Sasaki
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  5. Katsumi Ajisaka
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Fujimoto, H., Miyasato, M., Ito, Y. et al. Purification and properties of recombinant β-galactosidase from Bacillus circulans. Glycoconj J 15, 155–160 (1998). https://doi.org/10.1023/A:1006916222187

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