Anotace:
Amidases (L-asparaginase and L-glutaminase) catalyze the deamination process of L-asparagine and L-glutamine to their corresponding acidic form with ammonia releasing. Both enzymes are considered one of the most biomedical and biotechnologically important groups of enzymes, besides their international contributing as an important commercial products. L-asparaginase and L-glutaminase have been receiving more attention as antileukemic agent for treatment of acute lymphoblastic leukemia (ALL) and other types of cancer. On the other hand, these enzymes also used in food manufacture for their hydrolysis effect and is a possible way to decrease the amount of free L-asparagine in the preliminary ingredients of food making, thus minimize the imminent risk of causing neurotoxic and carcinogenic acrylamide compound which formed when food heated above 120 °C. Glutamic and aspartic acid are important amino acids in food processing achieve a delicious, fine, sour and umami taste beside their nutritional important to food. A recent review discusses the mode of action of L-asparaginase and L-glutaminase. Also, this review lists the sources of L-asparaginase and L-glutaminase, production optimization of enzymes, and uses of the two enzymes in cancer therapy and other industrial purposes.