Title

Authors

Affiliation

¹Department of Biotechnology, Faculty of Advanced science and technologies, University of Isfahan, Hezarjarib St, 81746-73441, Isfahan, Iran, and National Institute of Genetic Engineering and Biotechnology, Tehran, Iran; ²Department of Biology, Faculty of Sciences, University of Isfahan, Hezarjarib St, 81746-73441, Isfahan, I.R. Iran.

Email

z.etemadifar@sci.ui.ac.ir; *Corresponding author

Article Type

Prediction model

Date

Received December 06, 2011; Accepted January 01, 2012; Published March 17, 2012

Desulfurization protein named DszC from Rhodococcus erythropolis is the key enzyme for biodesulforization of dibenzothiophene (DBT) in 4S pathway, which is a pathway with four enzymes. DszC enzyme biodesulfurizes DBT and its derivatives in oil components and biphasic systems. It functions well at the oil- water interface. In this study point mutation performed in DszC enzyme regarding to increase protein hydrophobicity and stability for application in immobilized form. 3D model of DszC predicted using Phyre2, SAM-T08 and M4t servers. I-Mutant 2 server used to determine potential spots for point mutation, and Molegro Virtual Docker (MVD) used for performing point mutation on 3D model. Hydrophobicity plots generated by Bioedit version 7.0.8.0 in Kyte-Doolittle scale indicated that protein hydrophobicity is increased after mutation. Also protein stability increased 26.11 units in scale of DDC2.

Citation

Torktaz et al. Bioinformation 8(5): 246-250 (2012)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.