Effect of the thermodynamic water activity and the reaction medium hydrophobicity on the enzymatic synthesis of ascorbyl palmitate

Humeau, Catherine; Girardin, Michel; Rovel, B.; Miclo, A

doi:10.1016/s0168-1656(98)00069-8

Cited by 52 publications

(31 citation statements)

References 22 publications

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“…Previous reports for the hydrolysis of other hydrophobic substrates have not shown evidence of such anomalous behavior (Humeau et al, 1998). Specifically, Wehtje and Adlercreutz (1997a) studied the activity of three different lipases in esterification, hydrolysis and transesterification reactions.…”

Section: Resultsmentioning

confidence: 99%

“…Water content is a critical variable in lipase catalysis in nonaqueous media (Graber et al, 2003;Humeau et al, 1998;Ma et al, 2002;Persson et al, 2002;Valivety et al, 1992;Wehtje and Adlercreutz, 1997a,b). In the present case, the system is constrained to the use of small concentrations of water necessary for the stoichiometric hydrolysis of lutein esters, yet still providing sufficient enzyme hydration to maintain catalytic function.…”

Section: Introductionmentioning

confidence: 99%

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The lipase‐catalyzed hydrolysis of lutein diesters in non‐aqueous media is favored at extremely low water activities

Mora-Pale

Pérez-Munguía

González-Mejía

et al. 2007

Biotech & Bioengineering

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The enzymatic hydrolysis of a mixture of lutein diesters from Marigold flower (Tagetes erecta) was performed both in organic solvents and supercritical CO(2) (SC-CO(2)) using two commercial lipases: lipase B from Candida antarctica (Novozym 435) and the lipase from Mucor miehei (Lipozyme RM IM). Both lipases showed an unexpected dependence of initial reaction rate with the initial water activity (a(wi)) in hexane, with the highest rates of hydrolysis taking place at the lowest a(wi) of the biocatalyst particles. The same result was observed using isooctane, toluene, or SC-CO(2). It is proposed that an increase in a(wi) generates a hydrophilic microenvironment that prevents efficient partitioning of the highly hydrophobic lutein diesters to the enzyme. The critical role of water in this system has not been reported for other hydrolytic reactions in low water media. Calculations of water available for hydrolysis from isotherm analysis, Karl-Fischer titration, and substrate conversion at a(wi) = 0.13, indicate that the extent of reaction is not limited by the amount of available water. Accordingly, the enzyme that holds the largest amount of water after prehydration at the same a(wi) (0.13) will yield the greatest substrate conversion and concentration of the free lutein product. The highest conversion occurred in SC-CO(2), which opens up new opportunities to develop a combined extraction-reaction process for the environmentally benign synthesis of lutein, an important nutraceutical compound.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The lipase‐catalyzed hydrolysis of lutein diesters in non‐aqueous media is favored at extremely low water activities

Mora-Pale

Pérez-Munguía

González-Mejía

et al. 2007

Biotech & Bioengineering

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“…Generally, lipases capable of ascorbyl ester synthesis are very rare, hence enzyme preparation used in our study Novozyme ® 435 was used in majority of reported studies 2,10,12,13,24 so comparison with results is simple. Applied enzyme concentrations were usually high, up to 2 w/v .…”

Section: Enzyme Loading Effectmentioning

confidence: 99%

Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability

et al. 2013

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“…It can affect the equilibrium between esterification and hydrolysis of the presumed acyl-enzyme intermediate by shifting the equilibrium to the reactants. 28 In addition, increasing water activity will decrease enzyme stability in organic media, thus denaturing the enzyme and leading to low conversion. 27,29,30 The effect of temperature on the conversion rate was monitored in the range 53.11-76.89…”

Section: Effects Of Single Variables On Conversion Ratementioning

confidence: 99%

Study of lipase‐catalysed synthesis of ascorbyl benzoate in cyclohexanone using response surface methodology

Chen

2008

J Sci Food Agric

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BACKGROUND: Compared with ascorbic acid, ascorbyl esters exhibit many advantages. Their biosynthesis in organic media has been widely studied owing to its many advantages over chemosynthesis. However, since the natural substrates of lipase are fatty acid triacylglycerols, few data are available on the lipase-catalysed esterification of ascorbic acid with aromatic acids. Furthermore, although many reports can be found on the biosynthesis of ascorbic acid with fatty acids, few deal with the interactions between important reaction factors. The aim of the present study was to optimise the biosynthesis process of ascorbic acid with an aromatic acid, benzoic acid, in cyclohexanone using a statistical approach and to investigate the interactions among variables.

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Effect of the thermodynamic water activity and the reaction medium hydrophobicity on the enzymatic synthesis of ascorbyl palmitate

Cited by 52 publications

References 22 publications

The lipase‐catalyzed hydrolysis of lutein diesters in non‐aqueous media is favored at extremely low water activities

The lipase‐catalyzed hydrolysis of lutein diesters in non‐aqueous media is favored at extremely low water activities

Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability

Study of lipase‐catalysed synthesis of ascorbyl benzoate in cyclohexanone using response surface methodology

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