KINETIC STUDIES OF L-ASPARAGINASE FROM Penicillium digitatum

Abstract

L-Asparaginase is an enzyme used in the treatment of acute lymphoblastic leukemia and other related malignancies. Its further use includes reduction of asparagine concentration in food products, which may lead to formation of acrylamide. Currently bacterial asparaginase is produced at industrial scale, but the enzyme isolated from bacterial origin is often associated with adverse reactions. These side effects require development of asparaginase from alternative sources. In the present study, Penicillium digitatum was explored for the production of extracellular L-asparaginase using modified Czapek–Dox media. The enzyme was purified about 60.95-fold and then kinetic study showed that the Km value of the enzyme was 1 × 10⁻⁵ M. The optimum pH and temperature for the enzyme were 7.0 and 30°C, respectively. The optimum incubation period for L-asparaginase was 15 min. This work concludes that this enzyme can be a suitable candidate due to its strong kinetic properties, and further research can usher into development of asparaginase formulation from fungal origin with less adverse effects.

Keywords:

• anticancer
• enzyme kinetics
• L-Asparaginase
• Penicillium
• purification

Notes

Note. Total enzyme activity: enzyme activity multiplied by volume. Specific activity: micromoles ammonia released per minute per milligram of protein. Fold purification: the ratio of specific activity of crude extract versus specific activity of fractions. Recovery (%): the ratio of total activity of crude extracts versus total activity of fractions, multiplied by 100.