Structural characterization and active site prediction of keratinase from Bacillus flexus

Sixteen keratinolytic bacteria were isolated from poultry farm soil samples. The highest keratinlytic enzyme producers of Bacillus flexus was confirmed with 16S rRNA sequence analysis. It is of interest to understand the binding efficiency of the modelled keratinase from Bacillus flexus with differe...

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Detalles Bibliográficos
Autores principales: Padmavathi, Arumugam, Vijayaraghavan, Ramasamy, Prakash, Balu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10326337/
https://www.ncbi.nlm.nih.gov/pubmed/37426513
http://dx.doi.org/10.6026/97320630018780
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author Padmavathi, Arumugam
Vijayaraghavan, Ramasamy
Prakash, Balu
author_facet Padmavathi, Arumugam
Vijayaraghavan, Ramasamy
Prakash, Balu
author_sort Padmavathi, Arumugam
collection PubMed
description Sixteen keratinolytic bacteria were isolated from poultry farm soil samples. The highest keratinlytic enzyme producers of Bacillus flexus was confirmed with 16S rRNA sequence analysis. It is of interest to understand the binding efficiency of the modelled keratinase from Bacillus flexus with different substrates using molecular docking studies. Data provides insights for the identification of substrate recognition patterns, and the development of suitable enzymes to improve their use in keratin degradation.
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spelling pubmed-103263372023-07-08 Structural characterization and active site prediction of keratinase from Bacillus flexus Padmavathi, Arumugam Vijayaraghavan, Ramasamy Prakash, Balu Bioinformation Research Article Sixteen keratinolytic bacteria were isolated from poultry farm soil samples. The highest keratinlytic enzyme producers of Bacillus flexus was confirmed with 16S rRNA sequence analysis. It is of interest to understand the binding efficiency of the modelled keratinase from Bacillus flexus with different substrates using molecular docking studies. Data provides insights for the identification of substrate recognition patterns, and the development of suitable enzymes to improve their use in keratin degradation. Biomedical Informatics 2022-09-30 /pmc/articles/PMC10326337/ /pubmed/37426513 http://dx.doi.org/10.6026/97320630018780 Text en © 2022 Biomedical Informatics https://creativecommons.org/licenses/by/3.0/This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
spellingShingle Research Article
Padmavathi, Arumugam
Vijayaraghavan, Ramasamy
Prakash, Balu
Structural characterization and active site prediction of keratinase from Bacillus flexus
title Structural characterization and active site prediction of keratinase from Bacillus flexus
title_full Structural characterization and active site prediction of keratinase from Bacillus flexus
title_fullStr Structural characterization and active site prediction of keratinase from Bacillus flexus
title_full_unstemmed Structural characterization and active site prediction of keratinase from Bacillus flexus
title_short Structural characterization and active site prediction of keratinase from Bacillus flexus
title_sort structural characterization and active site prediction of keratinase from bacillus flexus
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10326337/
https://www.ncbi.nlm.nih.gov/pubmed/37426513
http://dx.doi.org/10.6026/97320630018780
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