L-Asparaginase

The antileukemic properties of L-Asparaginase were first identified in 1963 . Subsequent efforts focused on isolating the enzyme from bacterial sources and scaling up production for clinical trials. By 1978, the enzyme derived from Escherichia coli (E. coli) received approval for medical use in the United States .

L-Asparaginase works by depleting the circulating pool of serum asparagine . Asparagine is a non-essential amino acid for normal cells, which can synthesize it internally. However, certain cancer cells, particularly those in ALL, rely on external sources of asparagine for protein synthesis and survival . By hydrolyzing asparagine, L-Asparaginase effectively starves these cancer cells, leading to reduced protein synthesis and initiation of apoptosis (programmed cell death) .

L-Asparaginase is administered via injection into a vein, muscle, or under the skin . It is often used in combination with other chemotherapy drugs to enhance its efficacy . There are different formulations of L-Asparaginase, including pegylated versions that have a longer half-life and require less frequent dosing .

Common side effects of L-Asparaginase include allergic reactions, pancreatitis, blood clotting problems, high blood sugar, kidney problems, and liver dysfunction . Due to these potential side effects, patients undergoing treatment with L-Asparaginase are closely monitored by healthcare professionals .

Beyond its medical applications, L-Asparaginase is also used in the food industry to reduce acrylamide formation in starchy foods during high-temperature cooking processes . Acrylamide is a potential carcinogen, and the use of L-Asparaginase helps to make food products safer for consumption .