A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

Abstract Alkaline proteases have a myriad of potential applications in many industrial processes such as detergent, food and feed production, waste management and the leather industry. In this study, we isolated several alkaline protease producing bacteria from soda lake soil samples. A novel serine...

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Autores principales:	Cheng Zhou, Hongliang Qin, Xiujuan Chen, Yan Zhang, Yanfen Xue, Yanhe Ma
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Alkaline Protease Enzymatic Dehairing Cattle Hides Secretory Expression Soda Lakes Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5707edf1dae549229779efd7d12dceb1
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spelling	oai:doaj.org-article:5707edf1dae549229779efd7d12dceb12021-12-02T15:08:27ZA novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry10.1038/s41598-018-34416-52045-2322https://doaj.org/article/5707edf1dae549229779efd7d12dceb12018-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-34416-5https://doaj.org/toc/2045-2322Abstract Alkaline proteases have a myriad of potential applications in many industrial processes such as detergent, food and feed production, waste management and the leather industry. In this study, we isolated several alkaline protease producing bacteria from soda lake soil samples. A novel serine alkaline protease (AprA) gene from alkaliphilic Idiomarina sp. C9-1 was cloned and expressed in Escherichia coli. The purified AprA and its pre-peptidase C-terminal (PPC) domain-truncated enzyme (AprA-PPC) showed maximum activity at pH 10.5 and 60 °C, and were active and stable in a wide range of pH and temperature. Ca2+ significantly improved the thermostability and increased the optimal temperature to 70 °C. Furthermore, both AprA and AprA-PPC showed good tolerance to surfactants and oxidizing and reducing agents. We found that the PPC domain contributed to AprA activity, thermostability and surfactant tolerance. With casein as substrate, AprA and AprA-PPC showed the highest specific activity of 42567.1 U mg−1 and 99511.9 U mg−1, the K m values of 3.76 mg ml−1 and 3.98 mg ml−1, and the V max values of 57538.5 U mg−1 and 108722.1 U mg−1, respectively. Secreted expression of AprA-PPC in Bacillus subtilis after 48 h cultivation resulted in yield of 4935.5 U ml−1 with productivity of 102.8 U ml−1 h−1, which is the highest reported in literature to date. Without adding any lime or sodium sulfide, both of which are harmful pollutants, AprA-PPC was effective in dehairing cattle hide and skins of goat, pig and rabbit in 8–12 h without causing significant damage to hairs and grain surface. Our results suggest that AprA-PPC may have great potentials for ecofriendly dehairing of animal skins in the leather industry.Cheng ZhouHongliang QinXiujuan ChenYan ZhangYanfen XueYanhe MaNature PortfolioarticleAlkaline ProteaseEnzymatic DehairingCattle HidesSecretory ExpressionSoda LakesMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-18 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Alkaline Protease Enzymatic Dehairing Cattle Hides Secretory Expression Soda Lakes Medicine R Science Q
spellingShingle	Alkaline Protease Enzymatic Dehairing Cattle Hides Secretory Expression Soda Lakes Medicine R Science Q Cheng Zhou Hongliang Qin Xiujuan Chen Yan Zhang Yanfen Xue Yanhe Ma A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
description	Abstract Alkaline proteases have a myriad of potential applications in many industrial processes such as detergent, food and feed production, waste management and the leather industry. In this study, we isolated several alkaline protease producing bacteria from soda lake soil samples. A novel serine alkaline protease (AprA) gene from alkaliphilic Idiomarina sp. C9-1 was cloned and expressed in Escherichia coli. The purified AprA and its pre-peptidase C-terminal (PPC) domain-truncated enzyme (AprA-PPC) showed maximum activity at pH 10.5 and 60 °C, and were active and stable in a wide range of pH and temperature. Ca2+ significantly improved the thermostability and increased the optimal temperature to 70 °C. Furthermore, both AprA and AprA-PPC showed good tolerance to surfactants and oxidizing and reducing agents. We found that the PPC domain contributed to AprA activity, thermostability and surfactant tolerance. With casein as substrate, AprA and AprA-PPC showed the highest specific activity of 42567.1 U mg−1 and 99511.9 U mg−1, the K m values of 3.76 mg ml−1 and 3.98 mg ml−1, and the V max values of 57538.5 U mg−1 and 108722.1 U mg−1, respectively. Secreted expression of AprA-PPC in Bacillus subtilis after 48 h cultivation resulted in yield of 4935.5 U ml−1 with productivity of 102.8 U ml−1 h−1, which is the highest reported in literature to date. Without adding any lime or sodium sulfide, both of which are harmful pollutants, AprA-PPC was effective in dehairing cattle hide and skins of goat, pig and rabbit in 8–12 h without causing significant damage to hairs and grain surface. Our results suggest that AprA-PPC may have great potentials for ecofriendly dehairing of animal skins in the leather industry.
format	article
author	Cheng Zhou Hongliang Qin Xiujuan Chen Yan Zhang Yanfen Xue Yanhe Ma
author_facet	Cheng Zhou Hongliang Qin Xiujuan Chen Yan Zhang Yanfen Xue Yanhe Ma
author_sort	Cheng Zhou
title	A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
title_short	A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
title_full	A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
title_fullStr	A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
title_full_unstemmed	A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
title_sort	novel alkaline protease from alkaliphilic idiomarina sp. c9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/5707edf1dae549229779efd7d12dceb1
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A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

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