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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.C1.071Molecular 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