Comparing soluble Trametes pubescens laccase and cross-linked enzyme crystals (CLECs) for enzymatic modification of cellulose 10th EWLP, Stockholm, Sweden, August 25–28, 2008 : Holzforschung Jump to ContentJump to Main Navigation
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Comparing soluble Trametes pubescens laccase and cross-linked enzyme crystals (CLECs) for enzymatic modification of cellulose 10th EWLP, Stockholm, Sweden, August 25–28, 2008

Ilabahen Patel1, 2 / Roland Ludwig2, 3 / Kitti Mueangtoom2, 3 / Dietmar Haltrich2 / Thomas Rosenau1 / Antje Potthast1

1Department of Chemistry, University of Natural Resources and Applied Life Sciences Vienna (BOKU), Vienna, Austria

2Department of Food Sciences and Technology, Division of Food Biotechnology, University of Natural Resources and Applied Life Sciences Vienna (BOKU), Vienna, Austria

3Research Center Applied Biocatalysis, Graz, Austria

Corresponding author. Department of Chemistry, University of Natural Resources and Applied Life Sciences Vienna (BOKU), Muthgasse 18, A-1190 Vienna, Austria Phone: +43-1-36006 6071 Fax: +43-1-36006 6059

Citation Information: Holzforschung. Volume 63, Issue 6, Pages 715–720, ISSN (Online) 1437-434X, ISSN (Print) 0018-3830, DOI: 10.1515/HF.2009.073, November 2009

Publication History

Received:
2008-12-03
Accepted:
2009-02-11
Published Online:
2009-11-15

Abstract

Three types of preparations – enzyme immobilized on Eupergit C, cross-linked enzyme crystals (CLECs) and lyophilized enzyme – have been obtained from Trametes pubescens laccase. Their activity in organic solvents has been comparatively evaluated, whereby the CLECs showed a significantly higher activity compared to the immobilized and the lyophilized variant. The soluble, lyophilized laccase and the CLECs were compared for their activity in the oxidation of cellulose in the laccase/TEMPO system. The “double heterogeneous” CLEC system – both the CLECs and the cellulose substrates are solids and only the mediator is homogeneously dissolved – showed similar reactivity to the conventional enzyme system. Laccase CLECs, being a solid, robust and highly active immobilized enzyme form can be conveniently used to modify (protected) low-molecular weight carbohydrates or cellulosics also in (aqueous-)organic media, and they offer many practical advantages: operational stability and ease of recycling coupled with high volumetric productivity.

Keywords: cellulose; cross-linked enzyme crystals (CLECs); gel permeation chromatography (GPC); laccase; laccase-mediator system (LMS); TEMPO oxidation

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