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- Title
An Oxidant- and Organic Solvent-Resistant Alkaline Metalloprotease from Streptomyces olivochromogenes.
- Authors
Simkhada, Jaya; Cho, Seung; Park, Seong; Mander, Poonam; Choi, Yun; Lee, Hyo; Yoo, Jin
- Abstract
Organic solvent- and detergent-resistant proteases are important from an industrial viewpoint. However, they have been less frequently reported and only few of them are from actinomycetes. A metalloprotease from Streptomyces olivochromogenes (SOMP) was purified by ion exchange with Poros HQ and gel filtration with Sepharose CL-6B. Apparent molecular mass of the enzyme was estimated to be 51 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and gelatin zymography. The activity was optimum at pH 7.5 and 50 °C and stable between pH 7.0 and 10.0. SOMP was stable below 45 °C and Ca2 increased its thermostability. Ca2 enhanced while Co2 , Cu2 , Zn2 , Mn2 , and Fe2 inhibited the activity. Ethylenediaminetetraacetic acid and ethylene glycol-bis (β-aminoethyl ether)- N, N, N′, N′-tetraacetic acid, but not phenylmethylsulfonyl fluoride, aprotinin, and pefabloc SC, significantly suppressed the activity, suggesting that it might be a metalloprotease. Importantly, it is highly resistant against various detergents, organic solvents, and oxidizing agents, and the activity is enhanced by H2O2. The enzyme could be a novel protease based on its origin and peculiar biochemical properties. It may be useful in biotechnological applications especially for organic solvent-based enzymatic synthesis.
- Subjects
OXIDIZING agents; ORGANIC solvents; METALLOPROTEINASES; STREPTOMYCES; DETERGENTS; PROTEOLYTIC enzymes; ACTINOMYCETALES
- Publication
Applied Biochemistry & Biotechnology, 2010, Vol 162, Issue 5, p1457
- ISSN
0273-2289
- Publication type
Academic Journal
- DOI
10.1007/s12010-010-8925-0