Optimization of adsorptive immobilization of alcohol dehydrogenases.
J Biosci Bioeng
; 99(4): 340-7, 2005 Apr.
Article
em En
| MEDLINE
| ID: mdl-16233799
ABSTRACT
In this work, a systematic examination of various parameters of adsorptive immobilization of alcohol dehydrogenases (ADHs) on solid support is performed and the impact of these parameters on immobilization efficiency is studied. Depending on the source of the enzymes, these parameters differently influence the immobilization efficiency, expressed in terms of residual activity and protein loading. Residual activity of 79% was achieved with ADH from bakers' yeast (YADH) after optimizing the immobilization parameters. A step-wise drying process has been found to be more effective than one-step drying. A hypothesis of deactivation through bubble nucleation during drying of the enzyme/glass bead suspension at low drying pressure (<45 kPa) is experimentally verified. In the case of ADH from Lactobacillus brevis (LBADH), >300% residual activity was found after drying. Hyperactivation of the enzyme is probably caused by structural changes in the enzyme molecule during the drying process. ADH from Thermoanaerobacter species (ADH T) is found to be stable under drying conditions (>15 kPa) in contrast to LBADH and YADH.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Álcool Desidrogenase
/
Materiais Revestidos Biocompatíveis
/
Thermoanaerobacter
/
Enzimas Imobilizadas
/
Lactobacillus
Idioma:
En
Revista:
J Biosci Bioeng
Assunto da revista:
ENGENHARIA BIOMEDICA
/
MICROBIOLOGIA
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Alemanha