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Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV
Cow dung, a cheap and easily available source of energy, was used as the substrate for the production of alkaline protease by solid-state fermentation using the Bacillus subtilis strain VV. In order to achieve the maximum yield of this enzyme, the following optimum process parameters are needed: fer...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer International Publishing AG
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3725921/ https://www.ncbi.nlm.nih.gov/pubmed/23961375 http://dx.doi.org/10.1186/2193-1801-1-76 |
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author | Vijayaraghavan, Ponnuswamy Vijayan, Aija Arun, Arumugaperumal Jenisha, John Kennady Vincent, Samuel Gnana Prakash |
author_facet | Vijayaraghavan, Ponnuswamy Vijayan, Aija Arun, Arumugaperumal Jenisha, John Kennady Vincent, Samuel Gnana Prakash |
author_sort | Vijayaraghavan, Ponnuswamy |
collection | PubMed |
description | Cow dung, a cheap and easily available source of energy, was used as the substrate for the production of alkaline protease by solid-state fermentation using the Bacillus subtilis strain VV. In order to achieve the maximum yield of this enzyme, the following optimum process parameters are needed: fermentation period (72 h), pH (10.0), moisture content (140%), inoculum (25%), temperature (30–40°C), carbon source (2% (w/w) maltose) and nitrogen source (1% (w/w) urea). The protease was stable over a broad temperature range (30–50°C) and pH (8.0-10.0), with maximum activity at 50°C and pH 10.0. Among the divalent ions tested, Ca(2+) (0.01 M) increased enzyme activity. The purified protease, after being subjected to sodium dodecyl sulphate-polyacrylamide gel electrophoresis, was found to have a molecular mass of 38.5 kDa. The enzyme was solvent-and surfactant-stable and showed activity even after 24 h incubation along with various commercially available detergents. This enzyme possessed dehairing properties for animal hide after 16 h of incubation at room temperature. From these results it is evident that cow dung is a potential substrate for the production of a detergent-stable, dehairing protease by B. subtilis. This enzyme has a lot of potential applications in the detergent and leather-processing industries. |
format | Online Article Text |
id | pubmed-3725921 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Springer International Publishing AG |
record_format | MEDLINE/PubMed |
spelling | pubmed-37259212013-07-30 Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV Vijayaraghavan, Ponnuswamy Vijayan, Aija Arun, Arumugaperumal Jenisha, John Kennady Vincent, Samuel Gnana Prakash Springerplus Research Cow dung, a cheap and easily available source of energy, was used as the substrate for the production of alkaline protease by solid-state fermentation using the Bacillus subtilis strain VV. In order to achieve the maximum yield of this enzyme, the following optimum process parameters are needed: fermentation period (72 h), pH (10.0), moisture content (140%), inoculum (25%), temperature (30–40°C), carbon source (2% (w/w) maltose) and nitrogen source (1% (w/w) urea). The protease was stable over a broad temperature range (30–50°C) and pH (8.0-10.0), with maximum activity at 50°C and pH 10.0. Among the divalent ions tested, Ca(2+) (0.01 M) increased enzyme activity. The purified protease, after being subjected to sodium dodecyl sulphate-polyacrylamide gel electrophoresis, was found to have a molecular mass of 38.5 kDa. The enzyme was solvent-and surfactant-stable and showed activity even after 24 h incubation along with various commercially available detergents. This enzyme possessed dehairing properties for animal hide after 16 h of incubation at room temperature. From these results it is evident that cow dung is a potential substrate for the production of a detergent-stable, dehairing protease by B. subtilis. This enzyme has a lot of potential applications in the detergent and leather-processing industries. Springer International Publishing AG 2012-12-22 /pmc/articles/PMC3725921/ /pubmed/23961375 http://dx.doi.org/10.1186/2193-1801-1-76 Text en © Vijayaraghavan et al.; licensee Springer. 2012 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Vijayaraghavan, Ponnuswamy Vijayan, Aija Arun, Arumugaperumal Jenisha, John Kennady Vincent, Samuel Gnana Prakash Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV |
title | Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV |
title_full | Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV |
title_fullStr | Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV |
title_full_unstemmed | Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV |
title_short | Cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic Bacillus subtilis strain VV |
title_sort | cow dung: a potential biomass substrate for the production of detergent-stable dehairing protease by alkaliphilic bacillus subtilis strain vv |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3725921/ https://www.ncbi.nlm.nih.gov/pubmed/23961375 http://dx.doi.org/10.1186/2193-1801-1-76 |
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