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Abstract

COMPARISON OF L-ASPARAGINASE ENZYME PURIFICATION METHODS FROM RECOMBINANT ESCHERICHIA COLI FOR LEUKEMIA THERAPY: A REVIEW

Soni Muhsinin*, Nurlaella Solihah, Rahma Ziska and Ira Adiyati Rum

Abstract

L-asparaginase is an enzyme used for cancer therapy because it can hydrolyze L-asparaginase into aspartic acid and ammonia, which can cause cancer cells to die due to loss of nutrients. L-asparaginase in nature is found in algae, plants, and microbes. Escherichia coli is used as the first line in the treatment of leukemia. The production of recombinant protein in Escherichia coli has several advantages, including effectiveness and low cost as well as easy transformation and fermentation. The purpose of this scientific article review is to compare the L-asparaginase Enzyme Purification Method from Recombinant Escherichia coli for Leukemia Therapy. Purification of L-asparaginase from Escherichia coli showed the highest specific enzyme activity was 312.8 U/mg by DEAE Sepharose ion chromatography method.

Keywords: L-asparaginase, Escherichia coli, Purification.


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