Characterization of a Novel L-Asparaginase from Mycobacterium gordonae with Acrylamide Mitigation Potential.

ABSTRACT: L-asparaginase (E.C.3.5.1.1) is a well-known agent that prevents the formation of acrylamide both in the food industry and against childhood acute lymphoblastic leukemia in clinical settings. The disadvantages of L-asparaginase, which restrict its industrial application, include its narrow range of pH stability and low thermostability. In this study, a novel L-asparaginase from Mycobacterium gordonae (GmASNase) was cloned and expressed in Escherichia coli BL21 (DE3). GmASNase was found to be a tetramer with a monomeric size of 32 kDa, sharing only 32% structural identity with Helicobacter pylori L-asparaginases in the Protein Data Bank database. The purified GmASNase had the highest specific activity of 486.65 IU mg^-1 at pH 9.0 and 50 °C. In addition, GmASNa

SUBMITTER: Chi H 

PROVIDER: S-EPMC8617759 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature