Ecological significance and some biotechnological application of an organic solvent stable alkaline serine protease from Bacillus subtilis strain DM-04
Bioresource Technology, ISSN: 0960-8524, Vol: 100, Issue: 9, Page: 2642-2645
2009
- 56Citations
- 83Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations56
- Citation Indexes56
- 56
- CrossRef41
- Captures83
- Readers83
- 83
Article Description
An organic solvent stable, alkaline serine protease (Bsubap-I) with molecular mass of 33.1 kDa, purified from Bacillus subtilis DM-04 showed optimum activity at temperature and pH range of 37–45 °C and 10.0–10.5, respectively. The enzyme activity of Bsubap-I was significantly enhanced in presence of Fe 2+. The thermal resistance and stability and of Bsubap-I in presence of surfactants, detergents, and organic solvents, and its dehairing activity supported its candidature for application in laundry detergent formulations, ultrafiltration membrane cleaning, peptide synthesis and in leather industry. The broad substrate specificity and differential antibacterial property of Bsubap-I suggested the natural ecological role of this enzyme for the producing bacterium.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0960852408010213; http://dx.doi.org/10.1016/j.biortech.2008.11.042; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=59649121580&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/19136254; https://linkinghub.elsevier.com/retrieve/pii/S0960852408010213; https://dx.doi.org/10.1016/j.biortech.2008.11.042
Elsevier BV
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