Enzymatic synthesis of fatty acid ascorbyl esters

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

doi:10.1016/s1381-1177(98)00090-3

Cited by 74 publications

(28 citation statements)

References 10 publications

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“…Another possible assumption was that there might be a limitation in the transfer of vinyl acetate, one of the substrates, to the enzyme due to increase in the size of the water layer around enzyme molecules. Similar results were also reported by Adamczak et al [19] and Humeau et al [20] for the synthesis of ascorbyl esters.…”

Section: Effect Of Water Activitysupporting

confidence: 90%

Kinetic biosynthesis of l-ascorbyl acetate by immobilized Thermomyces lanuginosus lipase (Lipozyme TLIM)

Zhang

Zhi

et al. 2011

Bioprocess Biosyst Eng

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Thermomyces lanuginosus lipase (Lipozyme TLIM)-catalyzed esterification of L-ascorbic acid was studied. It was suggested that Lipozyme TLIM was a suitable biocatalyst for enzymatic esterification of L-ascorbic acid. Three solvents were investigated for the reaction, and acetone was found to be a suitable reaction medium. Furthermore, it was found that water activity could notably affect the conversion. Moreover, pH memory of Lipozyme TLIM lipase for catalyzing L-ascorbic acid esterification in acetone was observed and the effect of pH on the reaction was estimated. In addition, the influences of other parameters such as substrate mole ratio, enzyme loading, and reaction temperature and reusability of lipase on esterification of L-ascorbic acid were also analyzed systematically and quantitatively. Kinetic characterization of Lipozyme TLIM showed that K(m,a) and V(max) were 80.085 mM and 0.747 mM min(-1), respectively. As a result, Lipozyme TLIM-catalyzed esterification of L: -ascorbic acid gave a maximum conversion of 99%.

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Section: Effect Of Water Activitysupporting

confidence: 90%

Kinetic biosynthesis of l-ascorbyl acetate by immobilized Thermomyces lanuginosus lipase (Lipozyme TLIM)

Zhang

Zhi

et al. 2011

Bioprocess Biosyst Eng

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“…6-O-acyl l -ascorbates (Figure 5.9) with long chains between 8 and 18 have been obtained in organic solvents with a low water content. The ascorbates with short acyl chains would be more water soluble and have more potential as emulsifiers for preparing oil-in-water emulsions than those with long acyl chains [111][112][113]. l-Ascorbyl linoleate was successfully prepared by enzymatic esterification and transesterification in a nonaqueous medium using immobilized lipase as the biocatalyst [114].…”

Section: Structure and Synthetic Aspectsmentioning

confidence: 99%

Amino Acids, Lactic Acid and Ascorbic Acid as Raw Materials for Biocompatible Surfactants

Morán

Pérez²,

Pinazo³

et al. 2010

Surfactants From Renewable Resources

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“…Ascorbic acid esters, prepared regioselectively by lipase-catalyzed esterification or interesterification with FA alkyl esters, are potential lipophilic antioxidants with many current and potential uses, e.g., as antibrowning agents in apple juice, as sunscreen ingredients, and in the prevention of the linoleic acid oxidation (298,(353)(354)(355)(356)(357).…”

Section: Tocopherols Sterols and Steryl Estersmentioning

confidence: 99%

Enzyme‐Catalyzed modification of oilseed materials to produce eco‐friendly products

Hayes

2004

J Americ Oil Chem Soc

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Novel products produced from seed oil materials (TAG, phospholipids, and minor components such as tocopherols, sterols, stanols, and fatty acyl esters of the latter two) by enzyme-mediated purification or chemical modification are reviewed. The primary focus is on "value-added products" of current and potential use (particularly in the food, cosmetics, and pharmaceutical industries) that require the selectivity of enzymes and mild operating conditions, the latter being beneficial for polyunsaturated and oxygenated acyl groups. The paper briefly reviews the biochemistry of enzymes in lipid modification (lipases, phospholipases, and lipoxygenases) and discusses and assesses the current and future applications, current state of the art, and areas for future research for the following enzyme-mediated processes: isolation of polyunsaturated and oxygenated FFA; formation of structured TAG as nutraceuticals; formation of MAG, saccharide-FA esters, and other polyhydric alcohol ester as emulsifiers and surfactants; isolation and/or modification of tocopherols and sterols as antioxidants; formation of hydroperoxides as chemical intermediates; and modification of phospholipids for use in liposomes.Agriculturally derived feedstocks will play an increasingly important role in North America and worldwide as the cost of petroleum continues to increase and its availability decreases. Lipids (TAG, phospholipids, sterols, etc.) are an example of such a feedstock. Although lipids are readily modified by chemical means (reviewed in Refs. 1-5) and can be synthesized from petroleum-based feedstocks (6), there is an increased interest in modifying lipids via biocatalysis, particularly to manufacture lipid-based products in the food, cosmetics, and pharmaceutical industries, and for applications focused on environmental friendliness, due to the mild reaction conditions and narrow product distributions. In addition, biocatalysis has also played a role in isolating natural products, for instance, by temporarily modifying the molecule of interest to facilitate downstream separations. Reviews on biocatalytic modification of lipids have appeared during the last 15 yr (7-11) and more recently in two monographs (12,13). In addition, a recent conference entitled Enzymes in Lipid Modification was held in 2003 in Greifswald, Germany (14). The organization and emphasis of the previous reviews focused mostly on the types of biocatalysts; the emphasis here is on the products formed. Preceding the discussion of products is a brief overview of the important biocatalytic tools to be used. BIOCATALYSTS USED FOR LIPID MODIFICATIONLipases (EC 3.1.1.3). Lipases are specifically designed by nature for the hydrolysis and synthesis of ester bonds involving FA, and can form and/or hydrolyze amide, carbonate, and thioester bonds as well. Reactions catalyzed by lipases that involve the ester bond are diagrammed in Figure 1. Lipases are perhaps the most frequently used enzymes for biotransformations because of their ability to function in nonaqueous and aqueous ...

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Enzymatic synthesis of fatty acid ascorbyl esters

Cited by 74 publications

References 10 publications

Kinetic biosynthesis of l-ascorbyl acetate by immobilized Thermomyces lanuginosus lipase (Lipozyme TLIM)

Kinetic biosynthesis of l-ascorbyl acetate by immobilized Thermomyces lanuginosus lipase (Lipozyme TLIM)

Amino Acids, Lactic Acid and Ascorbic Acid as Raw Materials for Biocompatible Surfactants

Enzyme‐Catalyzed modification of oilseed materials to produce eco‐friendly products

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