http://scholars.ntou.edu.tw/handle/123456789/17484
標題: | Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs | 作者: | Gurunathan, Revathi Huang, Bin Ponnusamy, Vinoth Kumar Hwang, Jiang-Shiou Dahms, Hans-Uwe |
關鍵字: | PURIFICATION;IDENTIFICATION;EXPRESSION;GENE;PROTEINASE | 公開日期: | 7-六月-2021 | 出版社: | NATURE RESEARCH | 卷: | 11 | 期: | 1 | 來源出版物: | SCI REP-UK | 摘要: | Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus obtained from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7-11) and temperature (40-80 degrees C) ranges, with maximal hydrolytic activities at pH 10 and at 50 degrees C temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non-anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicates that this enzyme is suitable for the degradation of poultry waste without the loss of nutritionally essential amino acids which otherwise are lost in hydrothermal processing. Therefore, the proteinase is efficient in environmental friendly bioconversion of animal waste into fertilizers or value added products such as secondary animal feedstuffs. |
URI: | http://scholars.ntou.edu.tw/handle/123456789/17484 | ISSN: | 2045-2322 | DOI: | 10.1038/s41598-021-90375-4 |
顯示於: | 海洋生物研究所 02 ZERO HUNGER 11 SUSTAINABLE CITIES & COMMUNITIES 14 LIFE BELOW WATER |
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