Journal of Applied Bioinformatics & Computational BiologyISSN: 2329-9533

Short Communication, J Appl Bioinform Comput Biol Vol: 3 Issue: 1

Homology Modeling of Versatile Peroxidases from Pleurotus sapidus Reveals Residues for Site Directed Mutagenesis to Enhance the Bioremediation Ability

Chockalingam Nirmala, Chelvaraya Kannan Hindumathy and Shanmugam Anusuya*
Assistant Professor, Department of Biotechnology, VMKV Engineering College, Vinayaka Missions University, Salem-636 308, India
Corresponding author : Shanmugam Anusuya
Associate Professor, Department of Bioinformatics, VMKV Engineering College, Vinayaka Missions University, Salem-636 308, India
Tel: + 91-427-247-7540; Fax: + 91-427-247-7903
Email: [email protected]
Received: January 08, 2014 Accepted: March 29, 2014 Published: April 05, 2014
Citation: Nirmala C, Hindumathy CK, Anusuya S (2014) Homology Modeling of Versatile Peroxidases from Pleurotus sapidus Reveals Residues for Site Directed Mutagenesis to Enhance the Bioremediation Ability. J Appl Bioinform Comput Biol 3:1. doi:10.4172/2329-9533.1000108

Abstract

Homology Modeling of Versatile Peroxidases from Pleurotus sapidus Reveals Residues for Site Directed Mutagenesis to Enhance the Bioremediation Ability

Ligninolytic enzymes have potential applications in many fields and they are involved in the degradation of various xenobiotic compounds and dyes. Versatile peroxidases, a fungal enzyme, are industrially attractive and their applications have expanded to the field of bioremediation. Designing an enzyme that have higher catalytic activity, stability and fitting well with the required conditions are one of the challenges of today’s biotechnology. Versatile peroxidases are known to efficiently oxidize non-natural substrates like polycyclic aromatic hydrocarbons (PAHs). The accessibility of the PAHs to microbial cells is less. Hence by increasing the hydrophobicity of versatile peroxidases, the chance of the enzyme to meet the hydrophobic substrates such as PAHs in a contamination site can be increased. We have used an insilico approaches for optimal designing of versatile peroxidase to enhance its bioremediation ability.

Keywords: Versatile peroxidases; Polycyclic aromatic hydrocarbons (PAHs); Evolutionary trace server; Hydrophobicity; Mutation

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