L-Asparaginase (EC 184.108.40.206) is an amidohydrolase which catalyzes the breakdown of L-asparagine to ammonia and L-aspartic acid. Its broad use in both: food industry and chemotherapy makes it an object of wide research. It can reduce acrylamide formation in the baking of starchy foods and selectively kill tumor cells by depleting asparagine levels in the blood which is essentially required by tumor cells for continuous growth. However, hypersensitivity and toxicity puts a big question mark on L-Asparaginase therapy and raises the need to research for the ideal enzyme which should exhibit lower antigenicity, toxicity and a higher efficacy. Thusall future research should be directed towards lowering or eradicating of the undesirable properties to produce such enzyme for therapy. Some of the promising methods include: Site directed mutagenesis to remove immunogenic epitopes from the enzyme, using Random mutagenesis to increase efficacy of the enzyme or using Poly-L-Asparaginasenano capsules for increased efficacy and delivery with reduced toxicity. Although this subject has been reviewed in the past but an updated review with a comparison with previous studies can serve as fuel and direction for future research. The following review discusses the current research on L-asparaginase, its properties, sources, uses and future implications.