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Volume 7, Issue 1 (Suppl)

J Biotechnol Biomater

ISSN: 2155-952X JBTBM, an open access journal

March 20-21, 2017 Rome, Italy

&

15

th

World Congress on

2

nd

International Conference on

Biotechnology And Biotech Industries Meet

Enzymology and Molecular Biology

Enzymology & Mol. Biology 2017

Biotechnology Congress 2017

March 20-21, 2017

Fereniki Perperopoulou et al., J Biotechnol Biomater 2017, 7:1(Suppl)

http://dx.doi.org/10.4172/2155-952X.C1.071

Molecular characterization of glutathione transferase M1-1 from the

Camelus dromedarius

Fereniki Perperopoulou

1

, Farid Ataya

2

and

Nikolaos E Labrou

1

1

Agricultural University of Athens, Greece

2

King Saud University, Saudi Arabia

G

lutathione transferases (GSTs, EC. 2.5.1.18) are a large family of multifunctional enzymes, best known for their involvement in

the metabolism and inactivation of a broad range of xenobiotic compounds. GSTs catalyze the nucleophilic attack of the reduced

form of glutathione (γ-L-Glu-L-Cys-Gly, GSH) on the electrophilic center of a variety of compounds such as pesticides, herbicides,

etc. The result of the conjugation of GSH to such molecules is the increase of their solubility and the reduction of their toxicity. GSTs

could be useful tools with a variety of biotechnological applications in many fields. Many studies have been carried out exploiting

the natural ability of the GSTs to interact with xenobiotic compounds in order to develop simple and selective biotechnological

applications. In the present work, we report the cloning, kinetic and structural characterization of the GSTM1-1 from camel

(

Camelus dromedarius

). The Cd-GSΤM enzyme was expressed in

E. coli

and purified by affinity chromatography. The ligand in

function of the enzyme was evaluated by measuring the ability of 47 xenobiotic compounds to bind and inhibit the enzyme activity.

The inhibition potency was measured with the CDNB/GSH assay system. The IC50 value and the kinetic analysis of the compound

that showed the highest inhibition were determined. The results demonstrated that the enzyme exhibits high selectivity towards the

fungicide Zoxium/ zoxamide. Hence, this method can be used as an optical biosensor for the determination of Zoxium/zoxamide in

environmental samples.

Biography

Fereniki Perperopoulou has studied Agricultural Biotechnology from the Agricultural University of Athens. She has done her Master's degree in Bioactive Protein

Products and Technology at the Agricultural Biotechnology department of Agricultural University of Athens. Currently, she is a PhD candidate in the Department of

Biotechnology at the Agricultural University of Athens, working on the protein engineering and molecular study of transferase glutathione.

ferenikip@gmail.com