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A novel alkaline serine protease from Bacillus amyloliquefaciens strain S1-13 |
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| รหัสดีโอไอ | |
| Creator | 1. Yodying Yingchutrakul 2. Sitiruk Roytrakul 3. Ekachai Chukeatirote 4. Teerawit Waratrujiwong |
| Title | A novel alkaline serine protease from Bacillus amyloliquefaciens strain S1-13 |
| Publisher | Research and Technology Transfer Affairs Division |
| Publication Year | 2559 |
| Journal Title | KKU Research Journal |
| Journal Vol. | 21 |
| Journal No. | 13 (Supplement) |
| Page no. | 127-139 |
| Keyword | Bacillus amyloliquefaciens,16 rRNA gene,alkaline serine protease,metal-dependent enzyme,and LC/MS-MS |
| ISSN | 0859-3957 |
| Abstract | Bacillus sp. strain S1-13 was identified as Bacillus amyloliquefaciens with 16s rRNA gene (Accession number: JX441363). The strain S1-13 was expressed and secreted alkaline serine protease (called ASP1-13) when growth in nutrient broth containing with 1% skim milk. ASP1-13 was partial purified with a specific activity of 1,324 U/mg and 2% yield. The molecular weight and isoelectric point of ASP1-13 was determined about 40 kDa and 8, respectively. It was indicated as alkaline serine protease with a broad range of activity at alkaline condition (pH 7-12) and completely inhibited with serine protease inhibitor. ASP1-13 was also active in high temperature (50-60?C) and stabilizes with broad range of pH (5-12), surfactant, oxidant, reducing agent and organic solvent. Finally, the partial amino acid sequence from LC/MS-MS was confirmed similarity with sequence of neutral protease precursor from Bacillus subtilis. |
