Three different coupled enzymatic systems for in situ regeneration of NADPH

被引：16

作者：

Bastos, FD

dos Santos, AG

Jones, J

Oestreicher, EG

Pinto, GF

Paiva, LMC

机构：

[1] Univ Fed Rio de Janeiro, Inst Quim, Dept Bioquim, CT, BR-21945900 Rio De Janeiro, Brazil

[2] Univ Fed Rio de Janeiro, Inst Quim, Dept Quim Organ, Ctr Technol, BR-21945900 Rio De Janeiro, Brazil

来源：

BIOTECHNOLOGY TECHNIQUES | 1999年 / 13卷 / 10期

关键词：

alcohol dehydrogenase; coenzyme regeneration; NADPH regeneration; sulcatone; Thermoanaerobium brockii;

D O I：

10.1023/A:1008957711413

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Three different coupled enzymatic systems used in the reduction of sulcatone by alcohol dehydrogenase from Thermoanaerobium brockii (TBADH), were kinetically compared. The first one involved the use of TBADH for both the principal and recycling reactions and 2-propanol 20%, v/v as the recycling substrate. The other two were based on the use of a different enzyme, glucose- or glucose-6-phosphate dehydrogenases, for in situ regeneration of NADPH. The coupled-substrate approach achieved 100% of conversion against 84% of the other two systems.

引用

收藏

页码：661 / 664

页数：4

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