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Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase
Degradation of cellulosic carbon, the most important natural carbon reservoirs on this planet by cellulase is very essential for valuable soluble sugars. This cellulase has potential biotechnological applications in many industrial sectors. Thus the demand of cellulase is increasing more frequently...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8610336/ https://www.ncbi.nlm.nih.gov/pubmed/34841306 http://dx.doi.org/10.1016/j.crmicr.2020.100013 |
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author | Pramanik, Sajib Kumar Mahmud, Shafi Paul, Gobindo Kumar Jabin, Tabassum Naher, Kamrun Uddin, Md. Salah Zaman, Shahriar Saleh, Md. Abu |
author_facet | Pramanik, Sajib Kumar Mahmud, Shafi Paul, Gobindo Kumar Jabin, Tabassum Naher, Kamrun Uddin, Md. Salah Zaman, Shahriar Saleh, Md. Abu |
author_sort | Pramanik, Sajib Kumar |
collection | PubMed |
description | Degradation of cellulosic carbon, the most important natural carbon reservoirs on this planet by cellulase is very essential for valuable soluble sugars. This cellulase has potential biotechnological applications in many industrial sectors. Thus the demand of cellulase is increasing more frequently than ever. Agro industrial byproducts and suitable microbes are of an important source for the production of cellulase. Bacillus pseudomycoides and sugarcane bagasse were used for the production of cellulase and different process parameters influencing the production of cellulase were optimized here. The bacterium showed maximum cellulase production in the presence of sugarcane bagasse, peptone and magnesium sulfate at pH 7, 40 °C in 72 h of incubation. Primary structures of the cellulase is consists of 400 amino acid residues having molecular weight 44,790 Dalton and the theoretical PI is 9.11. Physiochemical properties of cellulase indicated that the protein has instability index 25.77. Seven hydrogen bonds were observed at multiple sites of the cellulase enzyme; His269, Asp237, Asn235, Tyr271, Ser272, Gln309, Asn233. This protein structure may play first hand in further development of exploring cellulase and cellulose interaction dynamics in Bacillus sp. Thus this bacterium may be useful in various industrial applications owing to its cellulase producing capability. |
format | Online Article Text |
id | pubmed-8610336 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-86103362021-11-26 Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase Pramanik, Sajib Kumar Mahmud, Shafi Paul, Gobindo Kumar Jabin, Tabassum Naher, Kamrun Uddin, Md. Salah Zaman, Shahriar Saleh, Md. Abu Curr Res Microb Sci Research Paper Degradation of cellulosic carbon, the most important natural carbon reservoirs on this planet by cellulase is very essential for valuable soluble sugars. This cellulase has potential biotechnological applications in many industrial sectors. Thus the demand of cellulase is increasing more frequently than ever. Agro industrial byproducts and suitable microbes are of an important source for the production of cellulase. Bacillus pseudomycoides and sugarcane bagasse were used for the production of cellulase and different process parameters influencing the production of cellulase were optimized here. The bacterium showed maximum cellulase production in the presence of sugarcane bagasse, peptone and magnesium sulfate at pH 7, 40 °C in 72 h of incubation. Primary structures of the cellulase is consists of 400 amino acid residues having molecular weight 44,790 Dalton and the theoretical PI is 9.11. Physiochemical properties of cellulase indicated that the protein has instability index 25.77. Seven hydrogen bonds were observed at multiple sites of the cellulase enzyme; His269, Asp237, Asn235, Tyr271, Ser272, Gln309, Asn233. This protein structure may play first hand in further development of exploring cellulase and cellulose interaction dynamics in Bacillus sp. Thus this bacterium may be useful in various industrial applications owing to its cellulase producing capability. Elsevier 2020-11-27 /pmc/articles/PMC8610336/ /pubmed/34841306 http://dx.doi.org/10.1016/j.crmicr.2020.100013 Text en © 2020 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Paper Pramanik, Sajib Kumar Mahmud, Shafi Paul, Gobindo Kumar Jabin, Tabassum Naher, Kamrun Uddin, Md. Salah Zaman, Shahriar Saleh, Md. Abu Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase |
title | Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase |
title_full | Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase |
title_fullStr | Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase |
title_full_unstemmed | Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase |
title_short | Fermentation optimization of cellulase production from sugarcane bagasse by Bacillus pseudomycoides and molecular modeling study of cellulase |
title_sort | fermentation optimization of cellulase production from sugarcane bagasse by bacillus pseudomycoides and molecular modeling study of cellulase |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8610336/ https://www.ncbi.nlm.nih.gov/pubmed/34841306 http://dx.doi.org/10.1016/j.crmicr.2020.100013 |
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