Abstract
L-asparaginase (L-asnase) is an amino hydrolase that has been used in the last decades for leukemia treatment, which boosted scientific studies on production, purification and immobilization of this enzyme. More recently, L-asnase has called food industry attention because of its effect on acrylamide formation in fried and baked foods. Several studies have been carried out in order to evaluate the effect of L-asnase in reducing acrylamide formation in different food models. This review brings up an overview in L-asnase kinetic parameters from different sources, immobilization methods, its therapeutic use in leukemia treatment and food processing applications. This review also discusses acrylamide formation in fried and baked foods. Commercial L-asnase is produced by two microorganisms, Escherichia coli and Erwinia sp. However, studies using different microorganisms have shown the possibility of producing this enzyme from different sources, obtaining enzymes with interesting kinetic properties. Immobilization strategies have provided enzymes with greater activity and stability, which could contribute to maintain L-asnase activity in the body for longer periods. Researches applying L-asnase in food products have shown significant reduction in acrylamide production, above 90% in some cases. For this purpose, during enzyme application some variables must be taken into account, as enzyme dose, food matrix, pretreatment, processing time and temperature. Medical and food applications make L-asnase a multipurpose enzyme. Reducing prices, improving enzyme stability and reducing co-lateral effects in leukemia treatment are still challenges to overcome.
Highlights
Special enzymes require greater purification and specificity, as they are targeted for therapeutic, diagnostic, analytical and research use
The use of the biocatalyst L-asparaginase is related to a reduction of the acrylamide compound in thermal processed foods since the availability of free amino acids such as asparagine together with reducing sugars during the Maillard reaction, contributes to the synthesis of acrylamide
Studies in the literature presented in this review showed a diversity of microbial enzyme sources, enzyme kinetic characteristics, stability, immobilization methods and conditions of enzyme applications in food and anticancer efficiency of the enzyme
Summary
Special enzymes require greater purification and specificity, as they are targeted for therapeutic, diagnostic, analytical and research use. As L-asparaginase is able to deplete plasmatic asparagine, it causes death of blast cells In addition to their therapeutic use, the field of applications of L-asparaginases has been expanding. They are used by the food industry to reduce the formation of acrylamide in starch rich foods (Sanghvi et al, 2016). Studies about the kinetic of free and immobilized L-asparaginase, produced by different microorganisms, and studies that investigated the use of this enzyme to reduce acrylamide in food and to treat leukemia were compiled and discussed
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