L-asparaginase is an enzyme used in medicine and in the food industry. Its ability to convert L-asparagine to L-aspartic acid and ammonia can be used to treat acute lymphoblastic leukemia and to reduce the amount of acrylamide in food. Currently, L-asparaginase is only available from bacterial sources (Escherichia coli and Erwinia chrysanthemi). Its bacterial origin makes it extremely immunogenic and as such it has many side effects. In my dissertation, I present fungi as a potential source of L-asparaginase. According to the literature, only two fungi appeared interesting. This two L-asparaginases are from Aspergillus oryzae in A. terreus and had comparable biochemical properties to bacterial ones, however their immunogenicity has not been taken into account. There is a lot of research in the field of fungi as a source for L-asparaginase, but the probability that we will find the perfect therapeutic enzyme only through literature search is low. Namely, the enzyme must meet very high criteria, including high affinity for L-asparagine and activity under physiological condition. In addition, the fungal origin of the enzyme does not guarantee lower immunogenicity.
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