Research Article

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

Volume: 43 Number: 4 December 27, 2022
EN TR

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

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.

Keywords

Supporting Institution

Tokat Gaziosmanpaşa Üniversitesi

Project Number

2014/59

References

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Details

Primary Language

English

Subjects

-

Journal Section

Research Article

Publication Date

December 27, 2022

Submission Date

October 1, 2021

Acceptance Date

October 2, 2022

Published in Issue

Year 2022 Volume: 43 Number: 4

APA
Bilgin, S., Gökşen Tosun, N., Alkan, C., Koç, E., & Erden Tayhan, S. (2022). Activity Improvement and Thermal Stability Enhancement of D-Aminoacylase Using Protein-Polymer Conjugates. Cumhuriyet Science Journal, 43(4), 621-628. https://doi.org/10.17776/csj.1003429

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