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Microbial L-asparaginase: purification, characterization and applications.

Faizan Muneer1, Muhammad Hussnain Siddique1, Farrukh Azeem1

  • 1Department of Bioinformatics and Biotechnology, Government College University, Faisalabad, Pakistan.

Archives of Microbiology
|February 14, 2020
PubMed
Summary

L-asparaginase is an enzyme with anti-cancer properties, crucial for treating leukemia and reducing carcinogens in food. This review summarizes its diverse microbial and plant sources, properties, and purification methods.

Keywords:
AcrylamideAsparagineBiosensorBiosynthesisChromatographyHodgkin’s lymphomaLymphoblastic leukemiaMillard reactionPhylogenetic tree

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Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • L-asparaginase (E.C.3.5.1.1) is a vital enzyme with established anti-cancer activity against lymphoproliferative disorders like acute lymphoblastic leukemia (ALL).
  • Its mechanism involves converting L-asparagine to aspartic acid and ammonia, crucial for its therapeutic effect.
  • Beyond medicine, L-asparaginase is used in the food industry to mitigate acrylamide formation in high-carbohydrate foods.

Purpose of the Study:

  • To review and summarize the various sources of L-asparaginase, including microorganisms and plants.
  • To analyze the phylogenetic relationships, purification techniques, and physiochemical properties of L-asparaginase from different origins.
  • To consolidate data on kinetic parameters and molecular masses of L-asparaginase.

Main Methods:

  • Literature review of existing studies on L-asparaginase.
  • Compilation and comparison of data on enzyme sources, purification strategies, and characterization.
  • Analysis of physiochemical properties, kinetic parameters, and molecular masses.

Main Results:

  • L-asparaginase is produced by a wide range of organisms, including bacteria, fungi, algae, and plants.
  • Enzymes from different sources exhibit varying physiochemical properties and kinetic parameters, with optimal pH between 6-10 and temperatures of 37-85°C.
  • Molecular masses range from 36.27 kDa (Yersinia pseudotuberculosis) to 205 ± 3 kDa (Pseudomonas otitidis).

Conclusions:

  • This review consolidates information on L-asparaginase sources, properties, and applications.
  • Understanding the diversity of L-asparaginase is key to optimizing its use in cancer therapy and food processing.
  • Further research into phylogenetic relationships and purification methods can enhance enzyme efficacy and application.