L-ASNases are already approved for marketing. Although L-ASNase is used as a therapeutic agent, immunogenic reactions and other adverse effects continue to limit its use. To enhance yield, L-ASNase isoforms are cloned and expressed in host cells, generating recombinants with distinct physicochemical properties and kinetic parameters. The enzymes' temperature and pH ranges vary from 25 to 100 °C and 6 to 10, respectively. Nowadays, enzymatic modifications, such as immobilization (chemical, physical, and PEGylation), mutagenesis, and PASylation, are used to overcome the limitations of commercialized L-ASNase-based drugs. Therefore, this review is a timely effort to compile and analyze the properties of recombinant L-ASNases and the contemporary techniques used to improve L-ASNase. A comprehensive study would help us better understand the kinetic parameters, biochemical properties, and modification trends of L-ASNase, enabling the development of robust, reliable therapeutics in the future.
Kumar et al. (Fri,) studied this question.