PURIFICATION AND CHARACTERIZATION OF THE NEWLY THERMOSTABLE PROTEASE PRODUCED BY Brevibacillus thermoruber LII ISOLATED FROM PADANG CERMIN HOTSPRING, INDONESIA
Thermostability is among of the vital enzyme characteristics for industrial application. Brevibacillus thermoruber LII was obtained as a potential isolate from the previous research which screened the potential thermostable protease producing bacteria from Indonesian hotspring. The newly thermostable protease produced by thermophilic Brevibacillus thermoruber LII had been purified and characterized. It was predicted that the pure enzyme obtained from Brevibacillus thermoruber LII was homo hexameric, having molecular weight of 36 kDa unit protein and its native was 215 kDa. In addition, it was also a neutral metalo serine protease according to biochemical tests that it was totaly inhibited by PMSF (Phenylmethanesulfonyl fluoride) and EDTA (Ethylenediaminetetraacetic acid). It showed optimum activity at pH of 8 and active in acidic buffer (up to pH of 4). All of metal ion in the form of chloride salt (2.5 mM) which were tested on the enzyme enhanced the enzyme activity but Li 2+. Ca 2+ ion increased the activity and the stability of enzyme against thermal. The enzyme also showed the stability against solvent. The protease LII had optimum temperature at 60 oC without CaCl 2 and 80–85 oC with addition of 2.5 mM CaCl 2. The KM and V max values for the purified protease LII were 27.2 mg/ml or 0.362 – 0.272 M for substrate HammersteinCasein (MM 75–100 kDa) and 261.1 μg/minute/ml, respectively.
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| B1801821 | Koleksi Digital | Archivelago Indonesia Marine Library - Perpustakaan Kementerian Kelautan dan Perikanan | Available |
Detail Information
- Series Title
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Koleksi Digital
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- 2014 : KKP-Badan Penelitian dan Pengembangan Kelautan dan Perikanan., Jakarta
- Collation
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1-10 hlm.
- Language
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English
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NONE
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- Edition
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9 (1), 2014
- Subject(s)
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- Statement of Responsibility
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Squalen Bulletin of Marine & Fisheries Postharvest & Biotechnology
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