title: Recent research progress on microbial L-asparaginases.
abstract: L-Asparaginases (EC 3.5.1.1) are enzymes that catalyze the hydrolysis of L-asparagine to L-aspartic acid and found in a variety of organisms from microorganisms to mammals. However, they are mainly expressed and produced by microorganisms. Microbial L-asparaginases have received sustained attention due to their irreplaceable role in the therapy of acute lymphoblastic leukemia and for their inhibition of acrylamide formation during food processing. In this article, we review the application of microbial L-asparaginases in medical treatments and acrylamide mitigation. In addition, we describe in detail recent advances in the existing sources, purification, production, properties, molecular modification, and immobilization of L-asparaginase.
authors.affiliation: State Key Laboratory of Food Science and Technology, Ministry of Education Key Laboratory of Carbohydrate Chemistry and Biotechnology, Jiangnan University, Wuxi, Jiangsu, 214122, China.
authors.forename: Shaohua
authors.initials: S
authors.lastname: Zuo
authors.forename: Tao
authors.initials: T
authors.lastname: Zhang
authors.forename: Bo
authors.initials: B
authors.lastname: Jiang
authors.forename: Wanmeng
authors.initials: W
authors.lastname: Mu
mesh_terms: D020106:Acrylamide / Q000378:metabolism; D001215:Asparaginase / Q000378:metabolism* / Q000627:therapeutic use*; D001216:Asparagine / Q000378:metabolism*; D001224:Aspartic Acid / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology; D005658:Fungi / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D054198:Precursor Cell Lymphoblastic Leukemia-Lymphoma / Q000188:drug therapy*
chemical_list: D020106:Acrylamide; D001224:Aspartic Acid; D001216:Asparagine; D001215:Asparaginase