Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

A Polyethylene Glycol Derivatized Laccase with Improved Thermal Resistance

Version 1 : Received: 19 August 2023 / Approved: 21 August 2023 / Online: 22 August 2023 (07:44:09 CEST)

How to cite: Mot, A.C.; Botis, A.C.; Silaghi-Dumitrescu, R. A Polyethylene Glycol Derivatized Laccase with Improved Thermal Resistance. Preprints 2023, 2023081498. https://doi.org/10.20944/preprints202308.1498.v1 Mot, A.C.; Botis, A.C.; Silaghi-Dumitrescu, R. A Polyethylene Glycol Derivatized Laccase with Improved Thermal Resistance. Preprints 2023, 2023081498. https://doi.org/10.20944/preprints202308.1498.v1

Abstract

Laccases are versatile and relatively accessible catalysts with practical/industrial applications. Their proteic nature entails limited stability under non-native conditions, especially such as those that would be required for industrial applications. Here, derivatization of a laccase from Sclerotinia sclerotiorum is reported, using an (methyl-PEG12)3-PEG4) N-succinimide ester in order to improve the thermostability of the enzyme. The PEGylated laccase is characterized using gel electrophoresis, size-exclusion chromatography, catalytic parameters and thermal stability. A 50% increase in residual activity after incubation at 50°C for up to two hours was achieved for the PEGylated laccase compared to the native enzyme.

Keywords

laccase; PEG; thermostability

Subject

Biology and Life Sciences, Biochemistry and Molecular Biology

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