Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

Abstract 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....

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Autores principales:	Revathi Gurunathan, Bin Huang, Vinoth Kumar Ponnusamy, Jiang-Shiou Hwang, Hans-Uwe Dahms
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/59ae56c00e7b448fa4ec31b9bfffc0a4
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spelling	oai:doaj.org-article:59ae56c00e7b448fa4ec31b9bfffc0a42021-12-02T14:58:19ZNovel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs10.1038/s41598-021-90375-42045-2322https://doaj.org/article/59ae56c00e7b448fa4ec31b9bfffc0a42021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90375-4https://doaj.org/toc/2045-2322Abstract 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 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °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.Revathi GurunathanBin HuangVinoth Kumar PonnusamyJiang-Shiou HwangHans-Uwe DahmsNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Revathi Gurunathan Bin Huang Vinoth Kumar Ponnusamy Jiang-Shiou Hwang Hans-Uwe Dahms Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs
description	Abstract 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 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °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.
format	article
author	Revathi Gurunathan Bin Huang Vinoth Kumar Ponnusamy Jiang-Shiou Hwang Hans-Uwe Dahms
author_facet	Revathi Gurunathan Bin Huang Vinoth Kumar Ponnusamy Jiang-Shiou Hwang Hans-Uwe Dahms
author_sort	Revathi Gurunathan
title	Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs
title_short	Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs
title_full	Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs
title_fullStr	Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs
title_full_unstemmed	Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs
title_sort	novel recombinant keratin degrading subtilisin like serine alkaline protease from bacillus cereus isolated from marine hydrothermal vent crabs
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/59ae56c00e7b448fa4ec31b9bfffc0a4
work_keys_str_mv	AT revathigurunathan novelrecombinantkeratindegradingsubtilisinlikeserinealkalineproteasefrombacilluscereusisolatedfrommarinehydrothermalventcrabs AT binhuang novelrecombinantkeratindegradingsubtilisinlikeserinealkalineproteasefrombacilluscereusisolatedfrommarinehydrothermalventcrabs AT vinothkumarponnusamy novelrecombinantkeratindegradingsubtilisinlikeserinealkalineproteasefrombacilluscereusisolatedfrommarinehydrothermalventcrabs AT jiangshiouhwang novelrecombinantkeratindegradingsubtilisinlikeserinealkalineproteasefrombacilluscereusisolatedfrommarinehydrothermalventcrabs AT hansuwedahms novelrecombinantkeratindegradingsubtilisinlikeserinealkalineproteasefrombacilluscereusisolatedfrommarinehydrothermalventcrabs
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Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

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