Activity Improvement and Thermal Stability Enhancement of D-Aminoacylase Using Protein-Polymer Conjugates

In this study, the synthesis of new polymer-protein conjugates using a grafting-from strategy was performed by employing photo-induced electron transfer reversible addition-fragmentation chain transfer (PET-RAFT) polymerization. D-aminoacylase is an industrially significant enzyme for the preparation of chiral amino acids and it is coupled with reversible addition-fragmentation (RAFT) chain transfer agent (CTA) using activated ester chemistry. The effects of polymeric side chain compositions on the activity of D-aminoacylase were studied with two different polymeric side chain lengths. For this reason, two monomers, a hydrophilic N-(2-aminoethyl acrylamide) and a hydrophobic and N- (iso-butoxymethyl) acrylamide were used, respectively. It was found that modification by grafting from strategy increased the thermal stability of D-aminoacylase enzyme. Additionally, the hydrophobic monomer conjugate has been reported to increase the activity of the enzyme more than the hydrophilic monomer.