Serine alkaline protease from a newly isolated Bacillus sp. SSR1
Process Biochemistry, ISSN: 1359-5113, Vol: 36, Issue: 8, Page: 781-785
2001
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- 57Captures
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Article Description
An extracellular serine alkaline protease produced by Bacillus sp. SSR1 was purified to homogeneity by Sephadex A-50 and Sepharose 6B column chromatography. The enzyme is a monomeric protein with a molecular weight of 29 and 35 kDa as estimated by SDS–PAGE and native PAGE respectively. The purified enzyme is stable in the alkaline pH range (8.0–11.0) and retains 100% activity at its optimum temperature of 40°C even after 300 min of incubation. The presence of CaCl 2 shifts the optimum temperature to 45°C and produces a 1.3-fold increase in its activity. The enzyme remains active and stable in various detergents and is strongly activated by metal ions (Fe 3+, Ca 2+, Na + )
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0032959200002752; http://dx.doi.org/10.1016/s0032-9592(00)00275-2; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035069423&origin=inward; http://linkinghub.elsevier.com/retrieve/pii/S0032959200002752; http://api.elsevier.com/content/article/PII:S0032959200002752?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0032959200002752?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0032959200002752; https://api.elsevier.com/content/article/PII:S0032959200002752?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:S0032959200002752?httpAccept=text/plain; http://dx.doi.org/10.1016/s0032-9592%2800%2900275-2; https://dx.doi.org/10.1016/s0032-9592%2800%2900275-2
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