Full model for reversible kinetics of lipase-catalyzed sugar- ester synthesis in 2-methyl 2-butanol

M.V. Flores, P.J. Halling

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

A kinetic model derived from the ping-pong bi-bi reversible mechanism is proposed to described the acylation of glucose by lauric acid in 2-methyl 2-butanol mediated by Candida antarctica lipase at 60degreesC. The model accounts for the effect of all four compounds in the reaction mixture, namely lauric acid, glucose, water, and lauroyl glucose ester. A supersaturated glucose solution was used to avoid limitations by glucose dissolution rate. Experiments with varied initial water content were performed to determine the effect of water on the initial reaction rate. The full time course of ester formation is described by five parameters: (a) three parameters evaluated from initial rate measurements; (b) the equilibrium constant, independently evaluated; and (c) one extra parameter fitted to the progress curve of ester formation. This reduced form of a full reversible kinetic model based on the ping-pong bi-bi mechanism is able to describe the complete course of lauroyl glucose ester synthesis. The proposed model provides a good fit for the experimental results.
LanguageEnglish
Pages794-800
Number of pages6
JournalBiotechnology and Bioengineering
Volume78
Issue number7
DOIs
Publication statusPublished - 30 Jun 2002

Fingerprint

Enzyme kinetics
Lipases
Lipase
Butenes
Sugars
Glucose
Esters
lauric acid
Kinetics
Water
Acylation
Acids
Candida
Equilibrium constants
Water content
Reaction rates
tert-amyl alcohol
Dissolution

Keywords

  • kinetics
  • sugar esters
  • lipase Supersaturated substrate solutions
  • candida-antarctica lipase
  • fatty-acid esters
  • immobilized lipase
  • organic media
  • enzymatic transformations
  • normal-hexane
  • esterification
  • glucose
  • transesterification

Cite this

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title = "Full model for reversible kinetics of lipase-catalyzed sugar- ester synthesis in 2-methyl 2-butanol",
abstract = "A kinetic model derived from the ping-pong bi-bi reversible mechanism is proposed to described the acylation of glucose by lauric acid in 2-methyl 2-butanol mediated by Candida antarctica lipase at 60degreesC. The model accounts for the effect of all four compounds in the reaction mixture, namely lauric acid, glucose, water, and lauroyl glucose ester. A supersaturated glucose solution was used to avoid limitations by glucose dissolution rate. Experiments with varied initial water content were performed to determine the effect of water on the initial reaction rate. The full time course of ester formation is described by five parameters: (a) three parameters evaluated from initial rate measurements; (b) the equilibrium constant, independently evaluated; and (c) one extra parameter fitted to the progress curve of ester formation. This reduced form of a full reversible kinetic model based on the ping-pong bi-bi mechanism is able to describe the complete course of lauroyl glucose ester synthesis. The proposed model provides a good fit for the experimental results.",
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Full model for reversible kinetics of lipase-catalyzed sugar- ester synthesis in 2-methyl 2-butanol. / Flores, M.V.; Halling, P.J.

In: Biotechnology and Bioengineering, Vol. 78, No. 7, 30.06.2002, p. 794-800.

Research output: Contribution to journalArticle

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AU - Flores, M.V.

AU - Halling, P.J.

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KW - kinetics

KW - sugar esters

KW - lipase Supersaturated substrate solutions

KW - candida-antarctica lipase

KW - fatty-acid esters

KW - immobilized lipase

KW - organic media

KW - enzymatic transformations

KW - normal-hexane

KW - esterification

KW - glucose

KW - transesterification

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