| Literature DB >> 8481013 |
S Paavilainen1, J Hellman, T Korpela.
Abstract
An intracellular beta-glucosidase was purified from cell extracts of Bacillus circulans subsp. alkalophilus by NAD affinity and high-performance anion-exchange chromatographies. The enzyme was active against a wide range of aryl-beta-glucosides and beta-linked disaccharides. The structural gene for beta-glucosidase was cloned in Escherichia coli. The beta-glucosidase gene consisted of an open reading frame of 1,350 bp encoding a protein of 450 amino acids with a calculated M(r) of 51,303. The enzyme exhibited from 45 to 66% identity with five bacterial beta-glucosidases.Entities:
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Year: 1993 PMID: 8481013 PMCID: PMC202212 DOI: 10.1128/aem.59.3.927-932.1993
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792