Y. Yingchutrakul, S. Roytrakul, E. Chukeatirote, Teerawit Waratrujiwong
{"title":"A novel alkaline serine protease from bacillus amyloliquefaciens strain S1-13","authors":"Y. Yingchutrakul, S. Roytrakul, E. Chukeatirote, Teerawit Waratrujiwong","doi":"10.14456/KKURJ.2016.18","DOIUrl":null,"url":null,"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.","PeriodicalId":8597,"journal":{"name":"Asia-Pacific Journal of Science and Technology","volume":"21 1","pages":"127-139"},"PeriodicalIF":0.0000,"publicationDate":"2016-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Asia-Pacific Journal of Science and Technology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.14456/KKURJ.2016.18","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Agricultural and Biological Sciences","Score":null,"Total":0}
引用次数: 0
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.