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ISSN: 1948-5948

Journal of Microbial & Biochemical Technology
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Research Article

Aspergillus fumigatus L-Amino Acid Oxidase-Two Step Purification and Characterization of the Enzyme

Susmita Singh1,2*, Binod Kumar Gogoi1 and Rajib Lochan Bezbaruah1

1Biotechnology Division, North East Institute of Science and Technology (CSIR), Assam, India

2Department of Molecular Biology & Biotechnology, Tezpur University, Assam, India

*Corresponding Author:
Dr. Susmita Singh
Department of Molecular Biology & Biotechnology
Tezpur University, Napaam-784028, Assam, India
Tel: +91- 9957722523
E-mail: [email protected]

Received date: December 13, 2013; Accepted date: February 06, 2014; Published date: February 11, 2014

Citation: Singh S, Gogoi BK, Bezbaruah RL (2014) Aspergillus fumigatus L-Amino Acid Oxidase-Two Step Purification and Characterization of the Enzyme. J Microb Biochem Technol 6:096-101. doi: 10.4172/1948-5948.1000128

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

L-amino acid oxidase (L-aao) obtained from Aspergillus fumigatus was purified by ion exchange and gel filtration chromatographies. The yield of L-aao in the ion- exchange chromatography was 24.40 % while the recovery of purified L-aao by gel filtration was 18.70 % of the crude enzyme. The molecular mass of the purified enzyme was estimated to be 55 kDa by SDS PAGE and 93 kDa by gel filtration. The enzyme was stable up to 40ºC and over a broad pH range of 5.6-9.2. The enzyme has higher specificity towards hydrophobic aromatic L-amino acids namely tyrosine and phenylalanine. The kinetic parameters, Km and Vmax were determined as 43.47 mM and 0.0434 μmol/ min/mL respectively. Ten mM Benzoic acid and EDTA completely inhibited the enzyme, while minimum inhibition with glycine (29.56%) and α-napthol (12.4%) were observed. Riboflavin, sodium azide and 8-hydroxyquinoline inhibit the enzyme up to 44.89%, 49.63% and 70.07% respectively. MgSO4 at 10-4 M and 10-3 M increased the enzyme activity by 1.72 and 2.22 fold respectively, while CuSO4 at 10-3 M increased the activity by 1.65 fold. This is the first report of purification of L-aao from Aspergillus fumigatus.

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