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Covalent immobilization of enzyme on aminated woven poly (lactic acid) via ammonia plasma: evaluation of the optimum immobilization conditions

Authors
Song, Ji EunSong, Wha SoonYeo, Sang YoungKim, Hye RimLee, So Hee
Issue Date
Jun-2017
Publisher
SAGE PUBLICATIONS LTD
Keywords
poly (lactic acid); glutaraldehyde; cross-linking; immobilization; plasma; trypsin
Citation
TEXTILE RESEARCH JOURNAL, v.87, no.10, pp.1177 - 1191
Journal Title
TEXTILE RESEARCH JOURNAL
Volume
87
Number
10
Start Page
1177
End Page
1191
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/8511
DOI
10.1177/0040517516648514
ISSN
0040-5175
Abstract
The present study aims to develop an immobilization support from woven poly (lactic acid) (PLA) and establish the optimum immobilization conditions for trypsin. Woven PLA was modified by ammonia-based plasma treatment in order to incorporate amine groups on its surface. X-ray photoelectron spectroscopy analysis showed that the N1s composition of PLA increased significantly, from 0.66% to 5.92%, after ammonia-based plasma processing. Trypsin from porcine pancreas was immobilized onto modified woven PLA by covalent binding after activating PLA with glutaraldehyde (GA). The results indicated that the optimal GA treatment conditions were as follows: pH of 10.0, 2% GA (v/v), and 180min crosslinking time. In addition, the optimum immobilization conditions were as follows: pH of 8.5, 10% (owf) of trypsin concentration, 30min, and 25?. Under the optimum conditions, the amount of immobilized enzyme on woven PLA was 0.28mg/mg and specific activity was 3.763 U/mg. In addition, the pH and thermal stabilities of the immobilized trypsin were improved. The immobilized trypsin retained approximately 55% of its initial activity after 20 days of storage and exhibited the potential for repetitive use through approximately 15 cycles. GA crosslinking and trypsin immobilization were found to improve the roughness of the PLA surface and increase its hydrophobicity. The data indicate that modified woven PLA, used as an immobilization support, shows suitable properties for use as a biocatalytic material in enzymatic applications.
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