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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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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. |
format | Online Article Text |
id | pubmed-7590317 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
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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