A novel alkaline serine protease from bacillus amyloliquefaciens strain S1-13

Q3 Agricultural and Biological Sciences
Y. Yingchutrakul, S. Roytrakul, E. Chukeatirote, Teerawit Waratrujiwong
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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.
解淀粉芽孢杆菌S1-13的一种新型碱性丝氨酸蛋白酶
菌株S1-13经鉴定为含有16s rRNA基因的解淀粉芽孢杆菌(Bacillus olimyquefaciens),编码:JX441363。菌株S1-13在含1%脱脂牛奶的营养液中生长时,表达并分泌碱性丝氨酸蛋白酶(称为ASP1-13)。部分纯化得到ASP1-13,比活性为1324 U/mg,产率为2%。测定了ASP1-13的分子量约为40 kDa,等电点约为8。结果表明,它是碱性丝氨酸蛋白酶,在碱性条件下(pH 7-12)具有广泛的活性,被丝氨酸蛋白酶抑制剂完全抑制。ASP1-13在高温(50-60℃)条件下也有活性,在pH(5-12)、表面活性剂、氧化剂、还原剂和有机溶剂等较宽范围内均具有稳定性。最后,LC/MS-MS鉴定的部分氨基酸序列与枯草芽孢杆菌中性蛋白酶前体序列相似。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Asia-Pacific Journal of Science and Technology
Asia-Pacific Journal of Science and Technology Agricultural and Biological Sciences-Agricultural and Biological Sciences (all)
CiteScore
0.90
自引率
0.00%
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0
审稿时长
8 weeks
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