Comparing soluble Trametes pubescens laccase and cross-linked enzyme crystals (CLECs) for enzymatic modification of cellulose 10th EWLP, Stockholm, Sweden, August 25-28, 2008

被引:10
作者
Patel, Ilabahen [1 ,2 ]
Ludwig, Roland [2 ,3 ]
Mueangtoom, Kitti [2 ,3 ]
Haltrich, Dietmar [2 ]
Rosenau, Thomas [1 ]
Potthast, Antje [1 ]
机构
[1] Univ Nat Resources & Appl Life Sci Vienna, Dept Chem, A-1190 Vienna, Austria
[2] Univ Nat Resources & Appl Life Sci Vienna, Dept Food Sci & Technol, Div Food Biotechnol, A-1190 Vienna, Austria
[3] Res Ctr Appl Biocatalysis, Graz, Austria
基金
奥地利科学基金会;
关键词
cellulose; cross linked enzyme crystals (CLECs); gel permeation chromatography (GPC); laccase; laccase-mediator system (LMS); TEMPO oxidation; TEMPO-MEDIATED OXIDATION; NATIVE CELLULOSE; CARBONYL GROUPS;
D O I
10.1515/HF.2009.073
中图分类号
S7 [林业];
学科分类号
0829 ; 0907 ;
摘要
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.
引用
收藏
页码:715 / 720
页数:6
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