Title

An analysis of horseradish peroxidase enzyme for effluent treatment

Authors

Hanumalal Nunavath1, Chandrasekhar Banoth1, Venkateswar Rao Talluri2, Bhima Bhukya1*

Affiliation

1Department of Microbiology, Osmania University, Hyderabad - 500 007, India; 2Professor TNA Innovation Center, VBTIPL, Sy. No. 253/A, Jiblakpally, Pochampally - 508284, Nalgonda (Dist.), Telangana, India

Email

Bhima Bhukya – Email: bhima.ou@gmail.com; Phone: +9140-27090661, Mob: +91-9494441624; *Corresponding author

Article Type

Hypothesis

Date

Received July 12, 2016; Revised August 27, 2016; Accepted August 31, 2016; Published October 10, 2016

The present study explains computational methods to design thermostable horseradish peroxidase enzyme using the crystal structure available from Protein Data Bank (PDB ID: 6ATJ). Multiple mutations were introduced to the original enzyme and developed a model by using Modeler9.14. After designing the model functional effect was confirmed in terms of protein ligand binding by molecular docking using Autodock 4.2. The implementation of modeling steps is demonstrated in the context of performing mutations for particular amino acid residue on the ligand pocket of the horseradish peroxidase, to derive the desired ligand binding properties. The docking investigation of modelled HRP with Quercetindihydroxide using Autodock 4.2 software that six amino acid residues, P139, H42, A31, L174, A38, and G169 are involved in hydrogen bonding. More importantly, it provides insight into understanding and properly interpreting the data produced by these methods. The 3D model was docked with Quercetindihydroxide (a known horseradish modulator) to understand molecular interactions at the active site region.

Keywords

de-colourization, homology modeling, horseradish peroxidase, and industrial effluents.

Citation

Nunavath et al. Bioinformation 12(6): 318-323 (2016)

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.