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• W2085260010 abstract "The presence of multiple types of β-galactosidases in a commercial enzyme preparation from Bacillus circulans ATCC 31382 and differences in their transgalactosylation activity were investigated. Four β-galactosidases, β-Gal-A, β-Gal-B, β-Gal-C, and β-Gal-D, which were immunologically homologous, were isolated and characterized. The N-terminal amino acid sequences of all of the enzymes were identical and biochemical characteristics were similar, except for galactooligosaccharide production. β-Gal-B, β-Gal-C, and β-Gal-D produced mainly tri- and tetra saccharides at maximum yields of 20–30 and 9–12%, while β-Gal-A produced trisaccharide with 7% with 5% lactose as substrate. The Lineweaver-Burk plots for all of the enzymes, except for β-Gal-A, showed biphasic behavior. β-Gal-A was truncated to yield multiple β-galactosidases by treatment with protease isolated from the culture broth of B. circulans. Treatment of β-Gal-A with trypsin yielded an active 91-kDa protein composed of 21-kDa and 70-kDa proteins with characteristics similar to those for β-Gal-D." @default.
• W2085260010 created "2016-06-24" @default.
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• W2085260010 date "2011-02-23" @default.
• W2085260010 modified "2023-09-26" @default.
• W2085260010 title "Causes of the Production of Multiple Forms of β-Galactosidase by<i>Bacillus circulans</i>" @default.
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• W2085260010 doi "https://doi.org/10.1271/bbb.100574" @default.
• W2085260010 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21307599" @default.
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