Literature DB >> 10486135

Enzymatic reduction of a less water-soluble ketone in reverse micelles with NADH regeneration.

B Orlich1, R Schomaecker.   

Abstract

In enzyme catalysis there is great interest in finding suitable organic media for less water-soluble substrates in order to increase the substrate concentration and, therefore, the reaction rates. These requirements are fulfilled by using microemulsions as reaction media. In this study w/o-microemulsions were used to investigate the kinetics of the reduction of 2-Heptanone to S-2-Heptanol, catalyzed by alcohol dehydrogenase. The required cofactor NADH for this reduction is regenerated by a second enzyme, formate dehydrogenase. The influences of pH, temperature, and the kinetic parameters of the enzymes are presented. It is demonstrated that in microemulsions the reaction rate of ADH is increased up to 12 times compared to water. Copyright 1999 John Wiley & Sons, Inc.

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Year:  1999        PMID: 10486135     DOI: 10.1002/(sici)1097-0290(19991105)65:3<357::aid-bit14>3.0.co;2-3

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  1 in total

1.  NAD(H) recycling activity of an engineered bifunctional enzyme galactose dehydrogenase/lactate dehydrogenase.

Authors:  Virapong Prachayasittikul; Sarah Ljung; Chartchalerm Isarankura-Na-Ayudhya; Leif Bülow
Journal:  Int J Biol Sci       Date:  2006-03-01       Impact factor: 6.580

  1 in total

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