Activity Improvement and Thermal Stability Enhancement of D-Aminoacylase Using Protein-Polymer Conjugates-Reference-Cited by-同舟云学术

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

Published:2022-12-27 Issue:4 Volume:43 Page:621-628
ISSN:2587-2680
Container-title:Cumhuriyet Science Journal
language:en
Short-container-title:CSJ

Author:

BİLGİN Sema¹,GÖKŞEN TOSUN Nazan¹,ALKAN Cemil¹^ORCID,KOÇ Esra¹,ERDEN TAYHAN Seçil¹

Affiliation:

1. TOKAT GAZİOSMANPAŞA ÜNİVERSİTESİ

Abstract

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.

Publisher

Cumhuriyet University

Subject

General Medicine

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