A Comprehensive Study of Recombinant L Asparaginase I and Ii from Lactobacillus Species

Abstract

L-asparaginases are hydrolytic enzymes which hydrolyze L-asparagine to L-aspartic acid and ammonia. They are widely used in leukemic treatment and in food industry. In leukemic treatment they deplete the L-asparagine amino acid in the blood stream and cancer cells which depend on the external L-asparagine for their growth and proliferation become deficient and die. In food industry, the foods with high starch content are known to form acrylamide a potent carcinogen during high temperature treatments of L-asparagine in them. This is reduced by pre-treating with L-asparaginase which indirectly reduces the formation of acrylamide. The aim of the present study is to clone express characterize and evaluate the efficiency of L-asparaginase I and II from Lactobacillus reuteri DSM 20016 and Lactobacillus casei subsp. casei ATCC 393 respectively. Lactobacillus species are recognized as probiotics and employed in food industry for ages. The presence of this commercially important enzyme in well-established probiotic is an advantage over the organisms from which these enzymes are obtained till date for commercial purpose newline