BIOCATALYTIC PROCESSES OF LOW-TEMPERATURE SYNTHESIS OF ESTERS. MODULATION OF THE FUNCTIONAL PROPERTIES OF LIPASE BY THE CHOICE OF SOLVENT AND SUPPORT FOR IMMOBILIZATION

Biocatalytic processes for the synthesis of valuable products, such as different esters for various purposes, have been studied using heterogeneous biocatalysts prepared by immobilizing the recombinant lipase rPichia/lip on mesoporous silica (SiO2) and macroporous carbon aerogel (MCA). It was found that the functional properties of immobilized lipase, such as enzymatic activity, specificity toward pair of substrates (acid and alcohol), the molecules of which differ in the number of carbon atoms (C), as well as operational stability, depended on the method of adsorptive immobilization, the chemical nature of the support, and polarity of the organic solvent, i.e. logP. The functional properties of rPichia/lip have been shown to be modulated by the selection of an organic solvent and support for lipase immobilization.