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Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease

The nutrition and flavor of shrimp paste came from hydrolyzation by enzymes that were produced by microorganisms. The salt‐tolerant strain Virgibacillus halodenitrificans ST‐1 isolated from shrimp paste was studied and used in the fermentation of shrimp paste. The strain and the protease produced by...

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Autores principales: Liu, Xueqin, Feng, Yanli, Lai, Xiaohua, Deng, Tian, Liu, Xin, Lyu, Mingsheng, Wang, Shujun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7590317/
https://www.ncbi.nlm.nih.gov/pubmed/33133538
http://dx.doi.org/10.1002/fsn3.1777
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author Liu, Xueqin
Feng, Yanli
Lai, Xiaohua
Deng, Tian
Liu, Xin
Lyu, Mingsheng
Wang, Shujun
author_facet Liu, Xueqin
Feng, Yanli
Lai, Xiaohua
Deng, Tian
Liu, Xin
Lyu, Mingsheng
Wang, Shujun
author_sort Liu, Xueqin
collection PubMed
description The nutrition and flavor of shrimp paste came from hydrolyzation by enzymes that were produced by microorganisms. The salt‐tolerant strain Virgibacillus halodenitrificans ST‐1 isolated from shrimp paste was studied and used in the fermentation of shrimp paste. The strain and the protease produced by ST‐1 were investigated. The optimum pH of the protease was 8.0, and the reaction temperature was 30°C. The protease showed high activity in the range of pH (5.0–11.0) and NaCl concentration (1%–15%). Divalent cations such as Ba(2+), Ca(2+), Mg(2+), Mn(2+), and Si(2+) could enhance the protease activity. Residual activity of protease was more than 90% when it was incubated with PMSF and H(2)O(2). Also, the enzyme retained more than 90% of initial activity after it was incubated with organic solvents. Variety of natural proteins could be substrates of the protease. By analyzing the release rate of free amino acids, it was predicted that the cleavage sites of the protease were mainly Glu, Asp, Gly, Leu, and Lys. Moreover, the hydrolysates of the protease had antioxidant activity, especially for DPPH and superoxide anion radical scavenging. The strain ST‐1 and the protease both were excellent candidates for food industries.
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spelling pubmed-75903172020-10-30 Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease Liu, Xueqin Feng, Yanli Lai, Xiaohua Deng, Tian Liu, Xin Lyu, Mingsheng Wang, Shujun Food Sci Nutr Original Research The nutrition and flavor of shrimp paste came from hydrolyzation by enzymes that were produced by microorganisms. The salt‐tolerant strain Virgibacillus halodenitrificans ST‐1 isolated from shrimp paste was studied and used in the fermentation of shrimp paste. The strain and the protease produced by ST‐1 were investigated. The optimum pH of the protease was 8.0, and the reaction temperature was 30°C. The protease showed high activity in the range of pH (5.0–11.0) and NaCl concentration (1%–15%). Divalent cations such as Ba(2+), Ca(2+), Mg(2+), Mn(2+), and Si(2+) could enhance the protease activity. Residual activity of protease was more than 90% when it was incubated with PMSF and H(2)O(2). Also, the enzyme retained more than 90% of initial activity after it was incubated with organic solvents. Variety of natural proteins could be substrates of the protease. By analyzing the release rate of free amino acids, it was predicted that the cleavage sites of the protease were mainly Glu, Asp, Gly, Leu, and Lys. Moreover, the hydrolysates of the protease had antioxidant activity, especially for DPPH and superoxide anion radical scavenging. The strain ST‐1 and the protease both were excellent candidates for food industries. John Wiley and Sons Inc. 2020-08-22 /pmc/articles/PMC7590317/ /pubmed/33133538 http://dx.doi.org/10.1002/fsn3.1777 Text en © 2020 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Research
Liu, Xueqin
Feng, Yanli
Lai, Xiaohua
Deng, Tian
Liu, Xin
Lyu, Mingsheng
Wang, Shujun
Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease
title Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease
title_full Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease
title_fullStr Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease
title_full_unstemmed Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease
title_short Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease
title_sort virgibacillus halodenitrificans st‐1 for fermentation of shrimp paste and hydrolysates of its protease
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7590317/
https://www.ncbi.nlm.nih.gov/pubmed/33133538
http://dx.doi.org/10.1002/fsn3.1777
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