Enzyme activation in organic solvents: Co-lyophilization of subtilisin Carlsberg with methyl-β-cyclodextrin renders an enzyme catalyst more active than the cross-linked enzyme crystals

In this study we explored the efficiency of the additive methyl‐β‐cyclodextrin (MβCD) to enhance the activity and enantioselectivity of the serine protease subtilisin Carlsberg in organic solvents. These two parameters, measured for different transesterification reactions and in several solvents, ar...

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Bibliographic Details
Published in:Biotechnology and bioengineering 2002-04, Vol.78 (1), p.53-59
Main Authors: Montañez-Clemente, Ileana, Alvira, Edgardo, Macias, Minedys, Ferrer, Amaris, Fonceca, Maricely, Rodriguez, Jessica, Gonzalez, Anicele, Barletta, Gabriel
Format: Article
Language:English
Subjects:
beta-Cyclodextrins
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Catalysis
Computer Simulation
cross-linked enzyme crystals
Cross-Linking Reagents - chemistry
Cross-Linking Reagents - metabolism
Crystallization
Cyclodextrins - metabolism
Cyclodextrins - pharmacology
Dioxanes - pharmacology
enantio selectivity
Enzyme Activation - drug effects
Esterification
Freeze Drying - methods
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
lyophilized powder
Methods. Procedures. Technologies
methyl-β-cyclodextrin
Models, Biological
Models, Molecular
Molecular Conformation
Sensitivity and Specificity
Solvents - pharmacology
Substrate Specificity
Subtilisins - chemistry
Subtilisins - drug effects
Subtilisins - metabolism
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Summary:In this study we explored the efficiency of the additive methyl‐β‐cyclodextrin (MβCD) to enhance the activity and enantioselectivity of the serine protease subtilisin Carlsberg in organic solvents. These two parameters, measured for different transesterification reactions and in several solvents, are compared with results obtained by using two additional preparations of the same enzyme: lyophilized powder and cross‐linked enzyme crystals (CLEC). The results suggest that co‐lyophilization of subtilisin with MβCD preserves the enzyme's active site tertiary structure rendering a highly active and enantioselective catalyst. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 78: 53–59, 2002; DOI 10.1002/bit.10182
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.10182