Towards catalyst compartimentation in combined chemo- and biocatalytic processes: immobilization of alcohol dehydrogenases for the diastereoselective reduction of a ß-hydroxy ketone obtained from an organocatalytic aldol reaction.
J Biotechnol
; 168(3): 271-6, 2013 Nov.
Article
em En
| MEDLINE
| ID: mdl-24036136
ABSTRACT
The alcohol dehydrogenases (ADHs) from Lactobacillus kefir and Rhodococcus sp., which earlier turned out to be suitable for a chemoenzymatic one-pot synthesis with organocatalysts, were immobilized with their cofactors on a commercially available superabsorber based on a literature known protocol. The use of the immobilized ADH from L. kefir in the reduction of acetophenone as a model substrate led to high conversion (>95%) in the first reaction cycle, followed by a slight decrease of conversion in the second reaction cycle. A comparable result was obtained when no cofactor was added although a water rich reaction media was used. The immobilized ADHs also turned out to be suitable catalysts for the diastereoselective reduction of an organocatalytically prepared enantiomerically enriched aldol adduct, leading to high conversion, diastereomeric ratio and enantioselectivity for the resulting 1,3-diols. However, at a lower catalyst and cofactor amount being still sufficient for biotransformations with "free" enzymes the immobilized ADH only showed high conversion and >99% ee for the first reaction cycle whereas a strong decrease of conversion was observed already in the second reaction cycle, thus indicating a significant leaching effect of catalyst and/or cofactor.
Palavras-chave
ADH; Alcohol; Alcohol dehydrogenase; Enzyme catalysis; Immobilization; NAD(+); NADH; NADP(+); NADPH; Reduction; alcohol dehydrogenase; nicotinamide adenine dinucleotide oxidized form; nicotinamide adenine dinucleotide phosphate oxidized form; nicotinamide adenine dinucleotide phosphate reduced form; nicotinamide adenine dinucleotide reduced form
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Acetofenonas
/
Álcool Desidrogenase
/
Aldeídos
/
Enzimas Imobilizadas
/
Cetonas
Idioma:
En
Revista:
J Biotechnol
Assunto da revista:
BIOTECNOLOGIA
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Alemanha