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Poly(2-oxazoline)s with a 2,2'-Iminodiacetate End Group Inhibit and Stabilize Laccase.

Authors :
Hijazi M
Türkmen E
Tiller JC
Source :
Chembiochem : a European journal of chemical biology [Chembiochem] 2020 Mar 16; Vol. 21 (6), pp. 874-882. Date of Electronic Publication: 2019 Dec 13.
Publication Year :
2020

Abstract

Poly(2-oxazoline)s (POxs) with 2,2'-iminodiacetate (IDA) end groups were investigated as inhibitors for laccase. The polymers with the IDA end groups are reversible, competitive inhibitors for this enzyme. The IC <subscript>50</subscript> values were found to be in a range of 1-3 mm. Compared with IDA alone, the activity was increased by a factor of more than 30; thus indicating that attaching a polymer chain to an inhibitor can already improve the activity of the former. The enzyme activity drops to practically zero upon increasing the concentration of the most active telechelic inhibitor, IDA-PEtOx <subscript>30</subscript> -IDA (PEtOx: poly(2-ethyl-2-oxazoline)), from 5 to 8 mm. This unusual behavior was investigated by means of dynamic light scattering, which showed specific aggregation above 5 mm. Furthermore, the laccase could be stabilized in the presence of POx-IDA, upon addition at a concentration of 20 mm and higher. Whereas laccase becomes completely inactive at room temperature after one week, the stabilized laccase is fully active for at least a month in aqueous solution.<br /> (© 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.)

Details

Language :
English
ISSN :
1439-7633
Volume :
21
Issue :
6
Database :
MEDLINE
Journal :
Chembiochem : a European journal of chemical biology
Publication Type :
Academic Journal
Accession number :
31614070
Full Text :
https://doi.org/10.1002/cbic.201900561