Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 190, Issue -, Pages -Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2021.106006
Keywords
L-asparaginase; Glutaminase and urease free; Purification; Anti-cancer
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The intracellular L-asparaginase isolated from endophytic fungi Chaetomium sp. exhibited anticancer activity on human blood cancer (MOLT-4) cells after partial purification.
L-asparaginase is a chemotherapeutic drug used in the treatment of acute lymphoblastic leukemia, a malignant disorder in children. L-asparaginase helps in removing acrylamide found in fried and baked foods which is carcinogenic in nature. The search for new therapeutic enzymes is of great interest in both medical and food applications. The present work aims to isolate the intracellular L-asparaginase from endophytic fungi Chaetomium sp. The intracellular enzyme was partially purified by chromatographic techniques. Molecular weight of enzyme was found to be similar to 66 kDa by SDS PAGE analysis. The enzyme is highly specific for L-asparagine and did not show glutaminase and urease activity. Maximum enzyme activity was found to be 58 +/- 5 U/mL at 40 degrees C, pH 7.0 with 2 mu g of protein. Intracellular L-asparaginase from Chaetomium sp. exhibited anticancer activity on human blood cancer (MOLT-4) cells.
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