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Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion
Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion
- Publication Year :
- 2008
-
Abstract
- Rhizomucor miehei lipase was immobilized in hydroxy(propylmethyl) cellulose or agar gels containing lecithin or AOT microemulsions. The effect of the diffusion of substrates and products to this catalyst was studied, as well as the effect of temperature on the initial rate of ester synthesis. The composition of the gel affects the reaction rate due to mass transport phenomena. The apparent activation energies were higher for the systems based on agar, independently of the microemulsion used, and lower for the systems based on AOT microemulsions, independently of the polymer used. Biotechnology Letters
- Subjects :
- Immobilized enzyme
Triacylglycerol lipase
Rhizomucor miehei
organogels
Bioengineering
1-Propanol
Methylcellulose
Applied Microbiology and Biotechnology
Catalysis
Substrate Specificity
Reaction rate
Diffusion
Hypromellose Derivatives
Lecithins
lipase
Organic chemistry
Microemulsion
Lipase
Rhizomucor
biology
Esterification
catalysis
Chemistry
diffusion
Temperature
Substrate (chemistry)
Lauric Acids
temperature
General Medicine
biology.organism_classification
Enzymes, Immobilized
gels
Enzyme Activation
Kinetics
activation energy
kinetics
in-oil microemulsions
microemulsion-based organogels
biology.protein
Emulsions
Gels
Heptanol
Biotechnology
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....8093e0f0e9eebed50081898ee73f7c1a