Functional Characterization and Sequence Analysis of Choline Dehydrogenase from Escherichia coli
نویسندگان
چکیده
Choline dehydrogenase catalyzes the oxidation of choline to glycine betaine via betaine aldehyde as intermediate. Biotechnological applications of glycine betaine in transgenic plant improvement have been shown to have enhanced tolerance towards hypersalinity and freezing. It can also restore and maintain osmotic balance of living cells under stress. In this study, choline dehydrogenase (betA) gene from E. coli was cloned and homologously expressed in E. coli M15 (pREP4). The recombinant enzyme was purified by column chromatography using DEAE Sepharose. The purified enzyme showed a fourfold increase in the activity of choline dehydrogenase enzyme with choline as substrate and phenazine methosulfate as electron acceptor, compared to the control strain. The betA gene sequence reported in this study contains several base substitutions with that of reported sequences in GenBank, resulting in the altered amino acid sequences of the translated proteins.
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