Activity of immobilized Thermomyces lanuginosus and Candida antarctica B Lipases in Interesterification Reactions: Effect of the Aqueous Microenvironment

Abstract

Lipases are enzymes used in numerous reactions of industrial interest. Depending on their aqueous microenvironment, lipases can catalyze hydrolysis or, conversely, organic synthesis like interesterification. This reaction can be used as a method to modify the physical and chemical properties of fats and oils, a basic process for production of ''structured lipids''. For such synthesis reactions, thermodynamic water activity (a w ) of the catalyst is generally the most important parameter to control. Actually, it will directly determine the performance of the synthesis, namely its yield, selectivity and stability. Effect of the a w on the activity of immobilized Thermomyces lanuginosus and Candida antarctica B lipases in interesterification reactions was studied. Water sorption and desorption isotherms were determined, showing a phenomenon of hysteresis for the Thermomyces lanuginosus lipase. Evaluation of the influence of a w on reaction yields revealed that the IE activity tends to increase with the water activity of immobilized Thermomyces lanuginosus lipase. In contrast, a w had little influence in the case of the Candida antarctica B lipase.

Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase

“…The behavior of rROL was similar to that observed for commercial immobilized preparation of Thermomyces lanuginosa lipase (Lipozyme TL IM) [30] and for the lipase/ acyltransferase from Candida parapsilosis, which exhibited, at a w 0.97 and in solvent-free medium, an interesterification activity similar to that of the commercial immobilized lipases at low water activity values [31].…”

Immobilization, Regiospecificity Characterization and Application of Aspergillus oryzae Lipase in the Enzymatic Synthesis of the Structured Lipid 1,3-Dioleoyl-2-Palmitoylglycerol

“…Most enzymes become more stable in organic environments, but a low water content on the lipase surface is essential for maintaining the necessary flexibility of protein structure and catalyzing the acyl transfer reactions[ 35 , 42 , 43 ]. In addition, a high water content in the synthetic reaction of TAG will definitely result in hydrolytic side reactions; thus, the water content of the catalytic environment markedly influences the lipase activity and product composition[ 44 ]. The prepared immobilized lipase adsorbed 3.5% water and showed high DAG production in the reaction; therefore, we further determined the influence of the high water content on the acidolysis reaction.…”

Lipophilic phenolic compounds (Lipo-PCs): emerging antioxidants applied in lipid systems

“…83 However, the A w value alone is not always sufficient to predict the biocatalytic behavior and should be correlated with the true water content of the lipase as behavior of some lipases could be different in water sorption and desorption. 84 In brief, differences in solvent effects can be explained by several factors: log P, dielectric constant (3), solubility and hydrophobicity, with log P and dielectric constant (3) being the main determining factors. Above all, the inuence of the nature of the solvent depends on the nature of the avonoid.…”