Abstract
Aspartase catalyzes the reversible deamination of aspartic acid to produce fumarate and ammonia and in specific conditions, produce aspartic acid from the products of deamination reaction. Since aspartase is one of the most specific enzymes, an improved process has been developed using aspartase for the production of aspartic acid in 1960. Aspartase is typically a bacterial enzyme and most of the studies on its enzymatic, structural and functional behavior have been carried out on Escherichia coli and Bacillus species. Various attributes at cellular and molecular level, including strain improvements through random mutagenesis and site-directed mutagenesis have been reported to describe the diverse kinetic aspects of the enzyme. In an attempt to provide imperative and comparative knowledge of aspartase from the existing literature, this review covers its sources, production, purification, characterization, immobilization, cloning and expression, crystal structure, applications, and future perspectives. Keywords: Aspartame, aspartase, aspartic acid, catabolic repression, characteristics, crystallization, directed evolution, error prone PCR, functional homology, immobilization, microbial sources, mutant strains, purification, site-directed mutagenesis, structure-function relationship.
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