Enzymatic redox cofactor regeneration in organic media: Functionalization and application of glycerol dehydrogenase and soluble transhydrogenase in reverse micelles

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

An enzymatic system for the regeneration of redox cofactors NADH and NADPH was investigated in nanostructural reverse micelles using bacterial glycerol dehydrogenase (GLD) and soluble transhydrogenase (STH). Catalytic conversion of NAD+ to NADH was realized in the sodium dioctylsulfosuccinate (AOT)/isooctane reverse micellar system harboring GLD and a sacrificial substrate, glycerol. The initial rate of NADH regeneration was enhanced by exogenous addition of ammonium sulfate into the reverse micelles, suggesting that NH4+ acts as a monovalent cationic activator. STH was successfully entrapped in the AOT/isooctane reverse micelles as well as GLD and was revealed to be capable of catalyzing the stoichiometric hydrogen transfer reaction between NADP+ and NADPH in reverse micelles. These results indicate that GLD and STH have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media.

Original languageEnglish
Pages (from-to)1192-1197
Number of pages6
JournalBiotechnology Progress
Volume21
Issue number4
DOIs
Publication statusPublished - Jul 1 2005

Fingerprint

glycerol dehydrogenase
NAD (coenzyme)
Micelles
micelles
NAD
Oxidation-Reduction
Regeneration
NADP
NADP (coenzyme)
Dioctyl Sulfosuccinic Acid
Ammonium Sulfate
Recycling
ammonium sulfate
Glycerol
hydrogen
recycling
glycerol
Hydrogen
Sodium
sodium

All Science Journal Classification (ASJC) codes

  • Biotechnology

Cite this

@article{739c8708e17d4e0a816ff2198f01c80e,
title = "Enzymatic redox cofactor regeneration in organic media: Functionalization and application of glycerol dehydrogenase and soluble transhydrogenase in reverse micelles",
abstract = "An enzymatic system for the regeneration of redox cofactors NADH and NADPH was investigated in nanostructural reverse micelles using bacterial glycerol dehydrogenase (GLD) and soluble transhydrogenase (STH). Catalytic conversion of NAD+ to NADH was realized in the sodium dioctylsulfosuccinate (AOT)/isooctane reverse micellar system harboring GLD and a sacrificial substrate, glycerol. The initial rate of NADH regeneration was enhanced by exogenous addition of ammonium sulfate into the reverse micelles, suggesting that NH4+ acts as a monovalent cationic activator. STH was successfully entrapped in the AOT/isooctane reverse micelles as well as GLD and was revealed to be capable of catalyzing the stoichiometric hydrogen transfer reaction between NADP+ and NADPH in reverse micelles. These results indicate that GLD and STH have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media.",
author = "Hirofumi Ichinose and Noriho Kamiya and Masahiro Goto",
year = "2005",
month = "7",
day = "1",
doi = "10.1021/bp0500765",
language = "English",
volume = "21",
pages = "1192--1197",
journal = "Biotechnology Progress",
issn = "8756-7938",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - Enzymatic redox cofactor regeneration in organic media

T2 - Functionalization and application of glycerol dehydrogenase and soluble transhydrogenase in reverse micelles

AU - Ichinose, Hirofumi

AU - Kamiya, Noriho

AU - Goto, Masahiro

PY - 2005/7/1

Y1 - 2005/7/1

N2 - An enzymatic system for the regeneration of redox cofactors NADH and NADPH was investigated in nanostructural reverse micelles using bacterial glycerol dehydrogenase (GLD) and soluble transhydrogenase (STH). Catalytic conversion of NAD+ to NADH was realized in the sodium dioctylsulfosuccinate (AOT)/isooctane reverse micellar system harboring GLD and a sacrificial substrate, glycerol. The initial rate of NADH regeneration was enhanced by exogenous addition of ammonium sulfate into the reverse micelles, suggesting that NH4+ acts as a monovalent cationic activator. STH was successfully entrapped in the AOT/isooctane reverse micelles as well as GLD and was revealed to be capable of catalyzing the stoichiometric hydrogen transfer reaction between NADP+ and NADPH in reverse micelles. These results indicate that GLD and STH have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media.

AB - An enzymatic system for the regeneration of redox cofactors NADH and NADPH was investigated in nanostructural reverse micelles using bacterial glycerol dehydrogenase (GLD) and soluble transhydrogenase (STH). Catalytic conversion of NAD+ to NADH was realized in the sodium dioctylsulfosuccinate (AOT)/isooctane reverse micellar system harboring GLD and a sacrificial substrate, glycerol. The initial rate of NADH regeneration was enhanced by exogenous addition of ammonium sulfate into the reverse micelles, suggesting that NH4+ acts as a monovalent cationic activator. STH was successfully entrapped in the AOT/isooctane reverse micelles as well as GLD and was revealed to be capable of catalyzing the stoichiometric hydrogen transfer reaction between NADP+ and NADPH in reverse micelles. These results indicate that GLD and STH have potential for use in redox cofactor recycling in reverse micelles, which allows the use of catalytic quantities of NAD(P)H in organic media.

UR - http://www.scopus.com/inward/record.url?scp=23244458805&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=23244458805&partnerID=8YFLogxK

U2 - 10.1021/bp0500765

DO - 10.1021/bp0500765

M3 - Article

C2 - 16080701

AN - SCOPUS:23244458805

VL - 21

SP - 1192

EP - 1197

JO - Biotechnology Progress

JF - Biotechnology Progress

SN - 8756-7938

IS - 4

ER -