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Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes
BACKGROUND: The microbial β-mannanases have been increasingly exploited for bioconversion of biomass materials and various potential industrial applications, such as bleaching of softwood pulps, scouring and desizing, food and feed additive, and oil and textile industries. In this paper, a β-mannana...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5074933/ https://www.ncbi.nlm.nih.gov/pubmed/27818862 http://dx.doi.org/10.1186/s40064-016-3496-3 |
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author | Ge, Jingping Du, Renpeng Zhao, Dan Song, Gang Jin, Man Ping, Wenxiang |
author_facet | Ge, Jingping Du, Renpeng Zhao, Dan Song, Gang Jin, Man Ping, Wenxiang |
author_sort | Ge, Jingping |
collection | PubMed |
description | BACKGROUND: The microbial β-mannanases have been increasingly exploited for bioconversion of biomass materials and various potential industrial applications, such as bleaching of softwood pulps, scouring and desizing, food and feed additive, and oil and textile industries. In this paper, a β-mannanase was characterization from the bacteria, Bacillus licheniformis HDYM-04, which was a high β-mannanase-producing strain (576.16 ± 2.12 U/mL at 48 h during fermentation). METHODS: The michaelis constant (K (m)) and maximum velocity (V (max)) of β-mannanase were determined. The effect of organic solvents, inhibitors, detergents, chelating agents, oxidizing agents and reducing agents on the stability of enzyme were determined. The degradation of twenty-two structurally different dyes by the purified β-mannanase produced by HDYM-04 was determined by full spectrum scan among 200–1000 nm at 0 min and 10 min, respectively. RESULTS: β-Mannanase produced by HDYM-04 was highly specific towards glucomannan, where as exhibited low activity towards guar gum. Michaelis constant (K (m)) and maximum velocity (V (max)) of glucomannan substrate were 2.69 mg/ml and 251.41 U/mg, respectively. The activity of different organic solvents showed significantly difference (p < 0.05). It retained > 80 % activity in dimethyl sulfoxide, acetone, chloroform, benzene, hexane. In the presence of solvents, citric acid, ethylene diamine teraacetic acid and potassium iodide, it retained > 80 % residual activity. Twenty-two structurally different dyes could be effectively decolourised by β-mannanase within 12 h, in which methyl orange (99.89 ± 2.87 %), aniline blue (90.23 ± 2.87 %) and alizalin (83.63 ± 2.89 %) had high decolorization rate. CONLUSION: The obtained results displayed that the β-mannanase produced by HDYM-04 showed high stability under different chemical reagents and was found to be capable of decolorizing synthetic dyes with different structures. So, the reported biochemical properties of the purified β-mannanase and its rapid decolorizations of dyes suggested that it might be suitable for industrial wastewater bioremediation. |
format | Online Article Text |
id | pubmed-5074933 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-50749332016-11-04 Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes Ge, Jingping Du, Renpeng Zhao, Dan Song, Gang Jin, Man Ping, Wenxiang Springerplus Research BACKGROUND: The microbial β-mannanases have been increasingly exploited for bioconversion of biomass materials and various potential industrial applications, such as bleaching of softwood pulps, scouring and desizing, food and feed additive, and oil and textile industries. In this paper, a β-mannanase was characterization from the bacteria, Bacillus licheniformis HDYM-04, which was a high β-mannanase-producing strain (576.16 ± 2.12 U/mL at 48 h during fermentation). METHODS: The michaelis constant (K (m)) and maximum velocity (V (max)) of β-mannanase were determined. The effect of organic solvents, inhibitors, detergents, chelating agents, oxidizing agents and reducing agents on the stability of enzyme were determined. The degradation of twenty-two structurally different dyes by the purified β-mannanase produced by HDYM-04 was determined by full spectrum scan among 200–1000 nm at 0 min and 10 min, respectively. RESULTS: β-Mannanase produced by HDYM-04 was highly specific towards glucomannan, where as exhibited low activity towards guar gum. Michaelis constant (K (m)) and maximum velocity (V (max)) of glucomannan substrate were 2.69 mg/ml and 251.41 U/mg, respectively. The activity of different organic solvents showed significantly difference (p < 0.05). It retained > 80 % activity in dimethyl sulfoxide, acetone, chloroform, benzene, hexane. In the presence of solvents, citric acid, ethylene diamine teraacetic acid and potassium iodide, it retained > 80 % residual activity. Twenty-two structurally different dyes could be effectively decolourised by β-mannanase within 12 h, in which methyl orange (99.89 ± 2.87 %), aniline blue (90.23 ± 2.87 %) and alizalin (83.63 ± 2.89 %) had high decolorization rate. CONLUSION: The obtained results displayed that the β-mannanase produced by HDYM-04 showed high stability under different chemical reagents and was found to be capable of decolorizing synthetic dyes with different structures. So, the reported biochemical properties of the purified β-mannanase and its rapid decolorizations of dyes suggested that it might be suitable for industrial wastewater bioremediation. Springer International Publishing 2016-10-21 /pmc/articles/PMC5074933/ /pubmed/27818862 http://dx.doi.org/10.1186/s40064-016-3496-3 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Research Ge, Jingping Du, Renpeng Zhao, Dan Song, Gang Jin, Man Ping, Wenxiang Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes |
title | Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes |
title_full | Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes |
title_fullStr | Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes |
title_full_unstemmed | Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes |
title_short | Kinetic study of a β-mannanase from the Bacillus licheniformis HDYM-04 and its decolorization ability of twenty-two structurally different dyes |
title_sort | kinetic study of a β-mannanase from the bacillus licheniformis hdym-04 and its decolorization ability of twenty-two structurally different dyes |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5074933/ https://www.ncbi.nlm.nih.gov/pubmed/27818862 http://dx.doi.org/10.1186/s40064-016-3496-3 |
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