Influence of Diffusion on the Kinetics of an Enzyme-Catalyzed Reaction in Gelatin-Based Gels

Hedström, Gun; Backlund, Sune; Eriksson, Folke

doi:10.1006/jcis.2001.7552

Cited by 8 publications

(5 citation statements)

References 33 publications

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“…The apparent activation energy was calculated and found to be 6 kJ/ mol. The order of magnitude of the activation energy calculated here is similar to that calculated for the same lipase immobilized on organogels based on either HPMC or agar [46] and to the activation energy measured by Hedstro ¨m et al for immobilized C. antarctica lipase [49].…”

Section: Effect Of Incubation Temperaturesupporting

confidence: 88%

(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

Vassiliadi

Aridas

Schmitt

et al. 2022

Molecular Catalysis

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Section: Effect Of Incubation Temperaturesupporting

confidence: 88%

(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

Vassiliadi

Aridas

Schmitt

et al. 2022

Molecular Catalysis

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“…This is in good agreement with the results of the study for temperature influence on reaction rate presented above. The order of magnitude of the activation energies calculated for all systems studied in this work was similar to that measured by Hedström et al (2001) for C. antarctica lipase immobilized in organogels. Moreover, the activation energies for MBGs were lower than those calculated for enzymatic reactions in microemulsions in accordance to Biasutti et al (2008).…”

Section: Activation Energysupporting

confidence: 79%

Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion

et al. 2008

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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.

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“…They attributed this effect to the importance of diffusion distances. Furthermore, Hedström et al [57] conducted a study on the influence of the gel surface area on the initial rate of gelatin AOT MBGs with C. antarctica lipase and were able to show that the extrapolated initial rate of hypothetical pellet gels with infinitely large areas are in good agreement with those obtained for granulated MBGs representing gels where diffusion distances are minimized.…”

Section: Effect Of Gel Compositionmentioning

confidence: 79%

Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide

Blattner

Zoumpanioti

Kröner

et al. 2006

The Journal of Supercritical Fluids

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Lipases from Candida antarctica and Mucor miehei were encapsulated in lecithin water-in-oil (w/o) microemulsion-based organogels (MBG). These gels were formulated with either hydroxypropylmethyl cellulose (HPMC) or gelatin. The esterification of lauric acid and 1-propanol catalyzed by these MBGs was examined in supercritical carbon dioxide (scCO 2 ; 35• C, 110 bar) as solvent for the substrates. The results were compared to those obtained with the reference substrate solvent isooctane. It turned out that the initial rates of this model reaction in scCO 2 were higher than those observed in the reference system. Various parameters affecting the biocatalysis such as pressure, alcohol and acid chain length, and gel composition were investigated. Kinetic studies showed that the ester synthesis catalyzed by the immobilized C. antarctica lipase occurs via a Ping Pong Bi Bi mechanism in which only inhibition by excess of alcohol was identified. Values of all kinetic parameters were determined. In addition, experiments on the reusability of these gels in scCO 2 were carried out and the state of water within the organogel was examined with the help of differential scanning calorimetry. The present study shows that biocatalysis using MBGs in scCO 2 is a promising alternative to other bioconversion processes.

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Influence of Diffusion on the Kinetics of an Enzyme-Catalyzed Reaction in Gelatin-Based Gels

Cited by 8 publications

References 33 publications

(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion

Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide

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