Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger

A predicted metalloproteinase gene, HypZn, was cloned from Aspergillus niger CGMCC 3.7193 and expressed in Pichia pastoris GS115, and the physicochemical characteristics of recombinant HypZn were investigated after separation and purification. The results showed that the specific activity of the pur...

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Autores principales:	Peng Song, Wei Xu, Kuiming Wang, Yang Zhang, Fei Wang, Xiuling Zhou, Haiying Shi, Wei Feng
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5f7c774a9d5442739cd7a44c3d21ba1f
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spelling	oai:doaj.org-article:5f7c774a9d5442739cd7a44c3d21ba1f2021-11-18T08:14:36ZCloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger1932-6203https://doaj.org/article/5f7c774a9d5442739cd7a44c3d21ba1f2021-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8584677/?tool=EBIhttps://doaj.org/toc/1932-6203A predicted metalloproteinase gene, HypZn, was cloned from Aspergillus niger CGMCC 3.7193 and expressed in Pichia pastoris GS115, and the physicochemical characteristics of recombinant HypZn were investigated after separation and purification. The results showed that the specific activity of the purified HypZn reached 1859.2 U/mg, and the optimum temperature and pH value of HypZn were 35°C and 7.0, respectively. HypZn remained stable both at 40°C and at pH values between 5.0 and 8.0. The preferred substrate of HypZn was soybean protein isolates, and the Km and Vmax values were 21.5 μmol/mL and 4926.6 μmol/(mL∙min), respectively. HypZn was activated by Co2+ and Zn2+ and inhibited by Cu2+ and Fe2+. The degree of soybean protein isolate hydrolysis reached 14.7%, and the hydrolysates were of uniform molecular weight. HypZn could tolerate 5000 mM NaCl and completely lost its activity after 30 min at 50°C. The enzymological characterizations indicated that HypZn has great application potential in the food industry, especially in fermented food processing.Peng SongWei XuKuiming WangYang ZhangFei WangXiuling ZhouHaiying ShiWei FengPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Peng Song Wei Xu Kuiming Wang Yang Zhang Fei Wang Xiuling Zhou Haiying Shi Wei Feng Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger
description	A predicted metalloproteinase gene, HypZn, was cloned from Aspergillus niger CGMCC 3.7193 and expressed in Pichia pastoris GS115, and the physicochemical characteristics of recombinant HypZn were investigated after separation and purification. The results showed that the specific activity of the purified HypZn reached 1859.2 U/mg, and the optimum temperature and pH value of HypZn were 35°C and 7.0, respectively. HypZn remained stable both at 40°C and at pH values between 5.0 and 8.0. The preferred substrate of HypZn was soybean protein isolates, and the Km and Vmax values were 21.5 μmol/mL and 4926.6 μmol/(mL∙min), respectively. HypZn was activated by Co2+ and Zn2+ and inhibited by Cu2+ and Fe2+. The degree of soybean protein isolate hydrolysis reached 14.7%, and the hydrolysates were of uniform molecular weight. HypZn could tolerate 5000 mM NaCl and completely lost its activity after 30 min at 50°C. The enzymological characterizations indicated that HypZn has great application potential in the food industry, especially in fermented food processing.
format	article
author	Peng Song Wei Xu Kuiming Wang Yang Zhang Fei Wang Xiuling Zhou Haiying Shi Wei Feng
author_facet	Peng Song Wei Xu Kuiming Wang Yang Zhang Fei Wang Xiuling Zhou Haiying Shi Wei Feng
author_sort	Peng Song
title	Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger
title_short	Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger
title_full	Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger
title_fullStr	Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger
title_full_unstemmed	Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger
title_sort	cloning, expression and characterization of metalloproteinase hypzn from aspergillus niger
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/5f7c774a9d5442739cd7a44c3d21ba1f
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Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger

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