The nature of fatty acid modifies the equilibrium position in the esterification catalyzed by lipase

Flores, María Victoria; Sewalt, J.J.W.; Janssen, A.E.M.; Padt, A. van der

doi:10.1002/(sici)1097-0290(20000205)67:3<364::aid-bit13>3.0.co;2-r

Cited by 29 publications

(14 citation statements)

References 28 publications

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“…In comparison, the experimental results show that the yield of synthesis for the C18 unsaturated fatty acids were higher than for the C18 saturated fatty acid (Table 1). Flores et al [14] reported similar results for the esterification of fatty acids and butanol using C. antarctica lipase in solvent-free medium. There is no straightforward explanation for the fact that for the same chain length, a higher ester yield is found for the unsaturated fatty acid.…”

Section: Resultssupporting

confidence: 64%

Enzymatic synthesis of l-ascorbyl linoleate in organic media

Song

Zhao

et al. 2005

Bioprocess Biosyst Eng

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A novel L-ascorbyl fatty acid ester, L-ascorbyl linoleate was successfully prepared by enzymatic esterification and transesterification in a non-aqueous medium using immobilized lipase as biocatalyst. Changes in enzymatic activity and product yield were studied for the following variable: the nature of the fatty acid, the fatty acid concentration and water content. The yield of synthesis for the C18 unsaturated fatty acids were higher than for the C18 saturated fatty acid. Initial enzyme concentration does not affect the equilibrium of the reaction. And the product yield (33.5%) in the transesterification was higher than that of the esterification (21.8%) at a high-substrate concentration 0.3 M. The medium water content was found to have a distinct influence on the L-ascorbyl linoleate synthesis.

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Section: Resultssupporting

confidence: 64%

Enzymatic synthesis of l-ascorbyl linoleate in organic media

Song

Zhao

et al. 2005

Bioprocess Biosyst Eng

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“…This in turn influences the polarity, flexibility, and accessibility of the active site toward the substrate. The substrate accessibility toward the active site can be influenced by chain-length variation, saturation, and solubility (21). Figure 3 shows the effect of water on the incorporation of lauric and oleic acids.…”

Section: Resultsmentioning

confidence: 99%

Enzymatic acidolysis of tristearin with lauric and oleic acids to produce coating lipids

Sellappan

Akoh

2000

J Americ Oil Chem Soc

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Triacylglycerols with potential for coating application were prepared by acidolysis of tristearin with lauric and oleic acids using Lipozyme IM60 lipase in n-hexane. The effects of reaction parameters such as time, temperature, substrate mole ratio, water content, enzyme load, and enzyme reuse were studied. Five-gram scale synthesis was carried out to obtain the melting profile of products by differential scanning calorimetry (DSC). An acceptable melting profile was obtained for the product obtained with a 1:4:1 (tristearin/lauric acid/oleic acid) mole ratio of reactants. The DSC melting peak for this product was 31.4°C. Synthesis of 1200 g of this product was carried out at a 1:4:1 substrate ratio in a stirred tank batch reactor under optimal conditions. The reaction product, purified by short-path distillation, was coated onto crackers and studied for its moisture inhibition ability, under water vapor-saturated atmosphere, in a desiccator over different time intervals. The effectiveness of the synthesized lipid as a coating material was compared against uncoated crackers as a control and with cocoa butter-coated crackers. The synthesized lipid was better in preventing moisture absorption than cocoa butter.

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“…The applications of lipase include the production of food additives, chiral intermediates, and pharmaceutical products 2. Lipase‐catalyzed condensation reactions in organic solvents are useful for the synthesis of esters 3–8. In the last few years, there has been increasing interest in the use of enzymes for the biosynthesis of molecules in organic media 9–11.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of geranyl butyrate with the poly(acrylic acid‐co‐hydroxy propyl methacrylate‐cl‐ethylene glycol dimethacrylate) hydrogel immobilized lipase of Pseudomonas aeruginosa MTCC‐4713

Kanwar

Gehlot

Verma

et al. 2008

J of Applied Polymer Sci

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Microbial lipases (E.C. 3.1.1.3) are the preferred biocatalysts for the synthesis of various fragrance compounds, such as linalool acetate, citronellal acetate, and geranyl acetate, in organic solvents over chemical synthesis. In this study, a purified alkaline extracellular lipase of Pseudomonas aeruginosa MTCC-4713 was efficiently immobilized onto a synthetic poly(AAc-co-HPMAcl-EGDMA) hydrogel by surface adsorption, and the bound lipase was evaluated for its hydrolytic potential toward various p-nitrophenyl acyl esters, which differed in their C-chain length. Among four series of hydrogels prepared by the variation of the concentrations of monomer and crosslinker, two hydrogels, namely, I 5d and I 20d , that exhibited relatively higher protein (lipase activity) bindings were selected to perform hydrolytic and synthetic (geranyl butyrate) reactions in aqueous and organic solvents. The hydrogel-bound lipase was highly hydrolytic toward p-nitrophenyl ester (C: 16; p-nitrophenyl palmitate). The hydrogel-immobilized lipase was quite stable and retained approximately 57.6% of its original hydrolytic activity after the fifth cycle of reuse under optimized conditions (pH 8.5, 658C). The hydrogel-immobilized lipase when used to perform the esterification of geraniol/butyric acid (400 : 100 mM) in n-heptane resulted in 98.8 mM geranyl butyrate at 658C under shaking (120 rpm) after 15 h of reaction time. The addition of a molecular sieve (3 Å 3 1.5 mm) to the reaction system at a concentration of 100 mg per reaction volume (1 mL) resulted in the complete conversion of the reactants into geranyl butyrate.

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The nature of fatty acid modifies the equilibrium position in the esterification catalyzed by lipase

Cited by 29 publications

References 28 publications

Enzymatic synthesis of l-ascorbyl linoleate in organic media

Enzymatic synthesis of l-ascorbyl linoleate in organic media

Enzymatic acidolysis of tristearin with lauric and oleic acids to produce coating lipids

Synthesis of geranyl butyrate with the poly(acrylic acid‐co‐hydroxy propyl methacrylate‐cl‐ethylene glycol dimethacrylate) hydrogel immobilized lipase of Pseudomonas aeruginosa MTCC‐4713

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