Heterogeneous biocatalytical esterification by recombinant Thermomyces lanuginosus lipase immobilized on macroporous carbon aerogel

摘要: Abstract Heterogeneous biocatalysts prepared by immobilizing recombinant lipases are promising for implementation in organic synthesis of various esters used as fragrances, emollients, emulsifiers, non-ionic surfactants, plasticizers, etc. For this research, the Thermomyces lanuginosus lipase produced authoring Pichia pastoris strain was adsorbed on macroporous carbon aerogel. The were studied periodic processes enzymatic esterification carried out nonconventional anhydrous media solvents at ambient conditions (22 ± 2 °C, 1 bar). Biocatalytical activities depended strongly both selected pair substrates (acid and alcohol) involved reaction solvent esterification. rates fatty C7 acid with double triple bond C3 alcohols, such allyl propargyl found to be 2–4 times lower than aliphatic propanol. Isomerism an (not molecule greatly affected rates. It observed that isomers C4 C5 acids (iso-butyric iso-valeric) practically did not react butanol. polarity characterized parameter logP. With increase from non-polar hexane polar acetone, rate decreased two orders magnitude. lipase-active had a sufficiently high operational stability under chosen optimal conditions; their stationary activity (300 100 U·g–1) change cycles during several tens hours.