Enzymatic Synthesis Of Fatty Esters Research Articles

Enzymatic Synthesis of Fatty Esters by Lipase from Porcine Pancreas

An enzymatic synthesis of aliphatic esters of butyric acid in the waterless environment of organic solvent hexane was carried out with use of the enzyme preparation lipase from porcine pancreas. Aliphatic alcohols with different length of hydrocarbon radical (C4-C11) were used as substrates. Conversion of the esters depending on time of the process and concentration of the enzyme was defined at 30°C of the process. It was found that an increase in length of the hydro carbonic radical of alcohol and branching of a chain complicated enzymatic synthesis. For the lower alcohols the conversion reach more than 90%.

Enzymatic synthesis of fatty esters in 5-caffeoyl quinic acid

Enzymatic synthesis of fatty esters in 5-caffeoyl quinic acid

Enzymatic synthesis of fatty esters in 5-caffeoyl quinic acid

The fatty esters of 5-caffeoyl quinic acid were synthesized by direct esterification biocatalysed by an immobilised lipase obtained from Candida antarctica. Esterification yields (from 40 to 75%) depended on the carbon chain length of the fatty alcohols and whether or not solvent (2-methyl 2-butanol) was present in the reaction medium.

Enzymatic synthesis of fatty esters: Part I. kinetic approach☆

A kinetic study of palmitic acid esterification reaction catalyzed by immobilized lipase Novozym 435 (from Candida antarctica) has been made in a range of 65–75°C temperature and 3–7% of initial catalyst concentration and atmospheric pressure. Influence of operating variables also was studied. Different values of temperature, initial lipase concentration, acid/alcohol molar ratio, and products concentrations were tested. Experiments were carried out in a stirred batch reactor equipped with adequate control systems. Evolution of concentration of the species involved was found by using gas-liquid chromatography. The kinetic characteristics observed in the esterification reaction with isopropanol were found to follow an ordered bi-bi mechanism with competitive inhibition by reactants and products. According to the mechanism maximum reaction rate, Michaelis–Menten constants and inhibition constants were determined. A good quality of fit was observed by fitting experimental rate data to the kinetic model with an average error beneath the 15%. Kinetic constants, as well as enthalpy and entropy values, have been determined for the model proposed for the esterification reaction within the experimental range studied.

Enzymatic synthesis of fatty esters by alkylated lipase

Lipase from Candida rugosa was chemically modified by reductive alkylation with aldehydes of various chain lengths. The derivatised lipases showed a higher esterification activity compared to native enzyme. The degree of activity enhancement depended on the type and molecular weight of the modifiers used and the degree of modification of the enzyme. They exhibited higher activities in non-polar than in polar solvents. The optimum esterification temperature and preference of fatty acids as acyl donors of the derivatised lipases were very similar to those of native enzyme. Lipase derivatised with dodecyldehyde was more thermostable than those modified with acetaldehyde. Alkylated lipases are relatively more stable in organic solvents than the native enzyme.