Production and purification of glutaminase free L-asparaginase from Lysinibacillus fusiformis and its appraisal in acrylamide mitigation of starchy foods

Abstract

L-asparaginase (EC 3.5.1.1.) is at the leading edge in microbial catalysis and biotechnology, as it possess range of applications in biomedical and food sectors. The L-asparaginase manifests versatile applications in the treatment of cancers and acrylamide reduction in fried and baked food. However, availability of limited enzyme producers, lower activity and stability reduces the commercial exploitation of asparaginase. L-asparaginase was produced and purified from the newly isolated bacterial strain Lysinibacillus fusiformis NP_MK3. The enzyme was partially purified using the DEAE Sepharose column chromatography and gel electrophoresis revealed production of asparaginase isozymes by L. fusiformis. The enzyme activity was enhanced up to twofold (10.55 Ul−1) with the addition of fructose as a carbon source. L-asparaginase exhibited optimal activity at 35 °C and pH 8. Pretreatment of potato chips with purified L-asparaginase had resulted into considerable decrease in acrylamide content. L. fusiformis asparaginase could potentially be employed as a robust biological pretreatment strategy to lessen the acrylamide content in fried and baked foods and thus in a long term reducing the risks of cancer incidence by consumption of such food products.