Neurotoxic Acrylamide Mitigation By L-Asparaginase Enzyme Extracted From Actinomycetes Species.

Abstract

Acrylamide is a chemical that is generated in starchy foods, coffee, and bread, etc during high-temperature cooking processes, such as frying, roasting, and baking and is a major food safety concern. Acrylamide toxicity targets the nervous and reproductive systems, causing symptoms like muscle weakness and numbness therefore there is a need to solve this problem by biological method. Actinomycetes are an excellent source of L-asparaginase, an enzyme which specifically catalyses the breakdown of amino acid L-asparagine to aspartic acid and ammonia. If starchy food products are not treated with L- asparginase enzyme then at high temperature L-asparagine present in food converts to acrylamide. Hence, water and soil samples were obtained from Uran, Sai, and Panvel regions and Actinomycetes were isolated onto Starch Casein Agar plates. Biochemical analyses revealed negative results for TSI, nitrate reduction, and citrate but positive for catalase and starch hydrolysis. Noteworthy enzymatic activity at 2.66µg/ml/min was observed. Optimization was performed with various parameters. Production and purification of L-asparaginase by submerged fermentation, followed by ammonium precipitation, dialysis, and subsequent application to pretreat potatoes. After incubation and frying, high-performance liquid chromatography analysis exhibited a reduction in acrylamide levels. The study's meticulous approach, from isolation to application, addresses critical food safety issues, marking a significant contribution.