Stabilities and rates in the laccase/TEMPO-catalyzed oxidation of alcohols

被引：39

作者：

Arends, Isabel W. C. E. ^{[1
]}

Li, Yu-Xin ^{[1
]}

Sheldon, Roger A. ^{[1
]}

机构：

[1] Delft Univ Technol, Dept Biotechnol, Lab Biocatalysis & Organ Chem, NL-2628 BL Delft, Netherlands

来源：

BIOCATALYSIS AND BIOTRANSFORMATION | 2006年 / 24卷 / 06期

关键词：

alcohol; laccase; oxoammonium; TEMPO;

D O I：

10.1080/10242420601040683

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The influence of alcohol, 4-acetylamino,2,2,6,6'-tetramethylpiperidinyloxy (4-acetylamino-TEMPO) and laccase (from Trametes versicolor, TvL) concentration in the aerobic oxidation of furfuryl alcohol was investigated. Studies show that the K-m for 4-acetylamino-TEMPO is around 6.3 mM (V-max=0.18 mM min(-1)) using 6.6 U mL(-1) of laccase and a furfuryl alcohol concentration of 140 mM. Under these optimized conditions, the reaction rate is still dependent on the concentration of enzyme in solution. Laccase can be reused, with a residual activity of around 25%. An important conclusion is that laccase is not stable in the presence of oxoammonium salts, presumably due to degradation via oxidation of essential amino acid residues or the glycosyl moieties on the periphery of the enzyme.

引用

页码：443 / 448

页数：6

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