alexa Docking of Polyaniline with D-Amino Acid Oxidase of Rhodosporidium toruloides and Pig Kidney-An Insight into the Mechanism of Binding for Immobilization in Polyaniline Supports
ISSN: 1948-5948

Journal of Microbial & Biochemical Technology
Open Access

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Research Article

Docking of Polyaniline with D-Amino Acid Oxidase of Rhodosporidium toruloides and Pig Kidney-An Insight into the Mechanism of Binding for Immobilization in Polyaniline Supports

Susmita Singh1 and Alak K Buragohain1,2*

1Department of Molecular Biology and Biotechnology, Tezpur (Central) University, Assam, India

2Dibrugarh University, Dibrugarh-786004, Assam, India

*Corresponding Author:
Alak Kumar Buragohain
Department of Molecular Biology and Biotechnology
Tezpur (Central) University, Tezpur
P.O.-Napaam-784028, Sonitpur, Assam
Tel: +91-9954115220/+9103732370239
Fax: +9103732370323
E-mail: [email protected]

Received date: July 21, 2014; Accepted date: August 22, 2014; Published date: August 29, 2014

Citation: Singh S, Buragohain AK (2014) Docking of Polyaniline with D-Amino Acid Oxidase of Rhodosporidium toruloides and Pig Kidney-An Insight into the Mechanism of Binding for Immobilization in Polyaniline Supports. J Microb Biochem Technol S4:003. doi: 10.4172/1948-5948.S4-003

Copyright: © 2014 Singh S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

The interaction of Polyaniline (PAni) with Rhodosporidium toruloides D-amino acid oxidase (RtDaao) and pig kidney D-aao (PkDaao) was studied by bioinformatics approach. The interaction of PAni with RtDaao does not interfere with the substrate binding and hence the D-amino acid oxidase (D-aao) activity is unaffected by the ligand. The active site cavity of pig kidney D-aao (PkDaao) is comprised of the residues Leu 51, Tyr 224, Tyr 228, Arg 283 and Gly 313. PAni interacts with Leu 51 and Thr 317 of chain G of the PkDaao with interaction energy of -2.5 and -1.09 kcal/mol respectively. D-aao was immobilized onto PAni-sodium alginate beads using glutaraldehyde as the crosslinking agent. 1g of the PAni-sodium alginate D-aao beads contained 0.093 ml or 0.385 U of the D-aao enzyme. The Activity Yield (AY) was calculated as 18.92% as determined by the pyruvate method of detection while, the AY was calculated as 17.3% as determined by the o-PDA method of D-aao assay of the beads. The PAni-sodium alginate D-aao beads were characterized by Fourier Transform Infrared spectroscopy (FTIR), X-ray Diffraction (XRD), Energy Dispersive X-ray Diffraction (EDX), Thermogravimetric Analysis (TGA) and Scanning Electron Microscopic analysis.

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