Purification and Characterization of Two Novel Halotolerant Extracellular Proteases from Bacillus subtilis Strain FP-133
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- SETYORINI Endang
- Division of Life Science, Graduate School of Science and Technology, Kobe University
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- TAKENAKA Shinji
- Laboratory of Applied Microbiology, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University
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- MURAKAMI Shuichiro
- Laboratory of Applied Microbiology, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University
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- AOKI Kenji
- Laboratory of Applied Microbiology, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University
Bibliographic Information
- Other Title
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- Purification and Characterization of Two Novel Halotolerant Extracellular Proteases from<i>Bacillus subtilis</i>Strain FP-133
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Abstract
Bacillus subtilis strain FP-133, isolated from a fermented fish paste, synthesized two novel halotolerant extracellular proteases (expro-I and expro-II), showing activity and stability at concentrations of 0–20% (w/v) NaCl. Each protease was purified to homogeneity and characterized. The purified expro-I was a non-alkaline serine protease with an optimum pH of 7.5, although most serine proteases from Bacillus strains act at the alkaline side. The molecular mass of expro-I was 29 kDa. The purified expro-II was a metalloprotease with a molecular mass of 34 kDa. It was activated by Fe2+, which has never been reported as a bacterial protease activator. At a concentration of 7.5% (w/v) NaCl, both proteases preferred animal proteins to vegetable proteins as natural substrates. In addition, under saline conditions, expro-I and II showed high catalytic activity toward gelatin and casein respectively.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (2), 433-440, 2006
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390001206475807104
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- NII Article ID
- 10018534281
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 7833483
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed