Methodology: Arginine deiminase (AD), an arginine-degrading enzyme, has been used in the treatment of tumours, sensitive to arginine deprivation, such as malignant melanoma and hepatocellular carcinoma. Proteins of microbial origin are always associated with mild to severe hypersensitivities. Moreover, proteins from terrestrial sources were found to exhibit stability problems at physiological environment. Hence considering the fact that the characteristics of the enzyme depends upon sources from which it has been isolated, we have use marine organism for the present study expecting to yield therapeutically and physiologically stable enzyme. ADI production was carried out under optimal conditions by shake flask method. The enzyme thus obtained was purified by ammonium sulphate fractionation, ion exchange and gel permeation chromatography. The purity of the enzyme was further confirmed by sodium dodecyl sulphate polyacrylamide gel electrophoresis, and it was characterized to know its properties.
Results: It was active at physiological pH, showed high substrate specificity towards l-arginine. It also exhibited high salt and temperature tolerance indicating good scope for its industrial and therapeutic applications.
Conclusions: ADI obtained from Vibrio alginolyticus 1374 can be a good candidate for the treatment of human cancers.
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