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Title

Structural characterization and active site prediction of keratinase from Bacillus flexus

 

Authors

Arumugam Padmavathi1, Ramasamy Vijayaraghavan2* & Balu Prakash3,*

 

Affiliation

1Department of Microbiology, Nehru Arts & Science College Coimbatore, TN, India; 2Department of Microbiology, PSG College of Arts and Science,  Coimbatore, TN, India; 3Department of Biotechnology, School of Life Sciences, Vels Institute of Science, Technology and Advanced Studies [VISTAS], Pallavaram, Chennai, Tamil Nadu, India. *Corresponding author:

 

Email

A. Padmavathi - E-mail: padma.sph23@gmail.com; Phone: +91 9940238388

R. Vijayaraghavan - E-mail: nascvijayaraghavan@nehrucolleges.com &

                            E-mail: metarrhizium@yahoo.co.in; Phone: +91 9865057610

B. Prakash – E-mail: prakazbt@gmail.com, prakashbsls@velsuniv.ac.in; Phone: +91 9443204101

 

Article Type

Research Article

 

Date

Received July 2, 2022; Revised September 30, 2022; Accepted September 30, 2022, Published September 30, 2022

 

Abstract

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.

 

Keywords

Structural characterization, active site prediction, keratinase, Bacillus flexus

 

Citation

Padmavathi et al. Bioinformation 18(9): 780-785 (2022)

 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

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.