Abstract
l-Asparaginases catalyze the conversion of l-asparagine to aspartate. Their applications as antineoplastic drug against different types of cancers, as tool for biosensing asparagine levels in blood and food items, and as processing aid for acrylamide mitigation have created special interest in these enzymes. Some of these applications require thermostable l-asparaginases and hyperthermophiles are a good source of such enzymes. A search for homologs of l-asparaginases in the genomes of hyperthermophilic archaea revealed that most of them contain more than one type of l-asparaginase. In fact, two types of l-asparaginases have been characterized from members of Euryarchaeota and Crenarchaeota. This chapter describes l-asparaginases from hyperthermophilic archaea and their potential applications.
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