Alcoholysis catalyzed by Candida antarctica lipase B in a gas/solid system: effects of water on kinetic parameters

The influence of water on the kinetics of alcoholysis of methyl propionate and n-propanol catalyzed by immobilized lipase B from Candida antarctica was studied in a continuous solid/gas reactor. In this reactor, the solid phase is composed of a packed enzymatic sample which is percolated by gaseous...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2003-05, Vol.1648 (1), p.24-32
Main Authors: Graber, Marianne, Bousquet-Dubouch, Marie-Pierre, Lamare, Sylvain, Legoy, Marie-Dominique
Format: Article
Language:English
Subjects:
1-Propanol - chemistry
1-Propanol - metabolism
alcoholysis
Biotechnology
Candida antarctica
Catalysis
Computer Science
Data Interpretation, Statistical
Enzyme Stability
Fungal Proteins
Hydration
Kinetics
Life Sciences
Lipase - chemistry
Lipase - metabolism
lipase B
Lipase B from Candida antarctica
Methyl Ethers - chemistry
Methyl Ethers - metabolism
methyl propionate
n-propanol
Propionates - chemistry
Propionates - metabolism
Solid/gas biocatalysis
Substrate Specificity
Transesterification
Water
Water - chemistry
Water - metabolism
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Summary:The influence of water on the kinetics of alcoholysis of methyl propionate and n-propanol catalyzed by immobilized lipase B from Candida antarctica was studied in a continuous solid/gas reactor. In this reactor, the solid phase is composed of a packed enzymatic sample which is percolated by gaseous nitrogen, simultaneously carrying gaseous substrates to the enzyme while removing reaction products. In this system, interactions between the enzyme and nonreacting molecules are avoided, since no solvent is present, and it is thus more easy to assess the role of water. To this end, alcohol inhibition constant, substrates dissociation constants as well as acylation rate constant and ratio of acylation to deacylation rate constants have been determined as a function of water activity ( a w). Data obtained highlight that n-propanol inhibition constant and dissociation constant of methyl propionate are a lot affected by a w variations whereas water has no significant effect on the catalytic acylation step nor on the ratio of acylation to deacylation rate constants. These results suggest the water-independent character of the transition step.
ISSN:1570-9639
0006-3002
1878-1454
DOI:10.1016/S1570-9639(03)00027-X