International Journal of Biotechnology Research Vol. 3(4), pp. 065-072, June 2015 ISSN 2328-3505 ©2015 Academe Research Journals

Full Length Research Paper

Purification of an epoxide hydrolase from A. tubingensis TF1 and effects of metal ions on its activity towards styrene oxide

Aparajita Duarah¹*, Soneswar Sarma², Archana Yadav¹, Binod Kumar Gogoi¹ and Tarun Chandra Bora¹

¹CSIR-North East Institute of Science and Technology, Jorhat-785006, Assam, India.

²Department of Biotechnology, Gauhati University, Guwahati-781014, Assam, India.

*Corresponding author E-mail: aparaitasduarah@rediffmail.com. Tel: 9864269370.

Accepted 23 March, 2015

Abstract

The present study aims at investigating the filamentous fungus Aspergillus tubingensis TF1 for its ability to produce epoxide hydrolases (EHs) under various reaction parameters. Under optimum media conditions, the highest activity obtained was 6.47 U/mL for phenyloxirane as the substrate. This enzyme was purified up to a purification fold of 4.33 with 0.2 U/mg of specific activity. After SDS-PAGE analysis, a band of approximately 47 kDa appeared when compared with the standard proteins. The effect of metal ions and surfactants on whole cells and the purified enzyme was investigated. The characteristics shown by A. tubingensis TF1 EH would be useful for the large scale production of this important enzyme in bioreactors.

Key words: Enantiopure diols, epoxide hydrolase, metal ions, specific activity, surfactants.