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Hindi 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: dranusuya12@gmail.com |
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| 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.
