Study on physicochemical properties of biocatalysts with thermostable lipase activity and final products of triglycerides’ interesterification

The physicochemical properties of multicomponent biocatalysts for triglycerides’ interesterification have been studied. They were prepared by entrapment of partially or completely destructed cells of a recombinant rE.coli/lip strain—the producer of a thermostable lipase from Thermomyces lanuginosus—inside silica xerogel. The functional role and optimum contents of components included such as whole cells or cells’ lysates, water, water-retaining agents, and nanostructured carbon forms (nanotubes, nanospheres) were investigated. The optimum composition of biocatalysts prepared on the basis of rE.coli/lip cells’ lysates, which possess enzymatic activity in water-free media, was selected. The half-inactivation time of the prepared biocatalysts in the process of interesterification of oil-fat blends in a flow packed-bed reactor was ∼70 h at 70–75°C.