Characterization and gene cloning of a novel β-mannanase from alkaliphilic Bacillus sp. N16-5
Extremophiles, ISSN: 1431-0651, Vol: 8, Issue: 6, Page: 447-454
2004
- 95Citations
- 35Captures
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Metrics Details
- Citations95
- Citation Indexes94
- 94
- CrossRef82
- Patent Family Citations1
- Patent Families1
- Captures35
- Readers35
- 35
Article Description
An alkaline β-mannanase was purified to homogeneity from a culture broth of alkaliphilic Bacillus sp. N16-5. The enzyme had optimum activity at pH 9.5 and 70°C. It was composed of a single polypeptide chain with a molecular weight of 55 kDa deduced from SDS-PAGE, and its isoelectric point was around pH 4.3. The enzyme efficiently hydrolyzed galactomannan and glucomannan, producing a series of oligosaccharides and monosaccharides. The β-mannanase gene (manA) contained an open reading frame (ORF) of 1,479 bp, encoding a 32-amino acids signal peptide, and a mature protein of 461 amino acids, with a calculated molecular mass of 50,743 Da. Strain N16-5 ManA, deduced from the manA ORF, exhibited relatively high amino acid similarity to the members of the glycosyl hydrolase family 5. The eight conserved active-site amino acids in family 5 glycosyl hydrolase were found in the deduced amino acid sequence of strain N16-5 ManA. © Springer-Verlag 2004.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=12544256289&origin=inward; http://dx.doi.org/10.1007/s00792-004-0405-4; http://www.ncbi.nlm.nih.gov/pubmed/15316858; http://link.springer.com/10.1007/s00792-004-0405-4; http://www.springerlink.com/index/10.1007/s00792-004-0405-4; http://www.springerlink.com/index/pdf/10.1007/s00792-004-0405-4; https://dx.doi.org/10.1007/s00792-004-0405-4; https://link.springer.com/article/10.1007/s00792-004-0405-4
Springer Science and Business Media LLC
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