Autori: F. Peter, L. Poppe, C. Kiss, E. Szocs-Biro, G. Preda, C. Zarcula, A. Olteanu
Editorial: Taylor &Francis, Biocatalysis and Biotransformation, 23, p.251-260, 2005.
Sol-gel entrapment of microbial lipases from Candida cylindracea (Cc lipase), Pseudomonas fluorescens (Lipase AK), and
Pseudomonas cepacia (Lipase PS), using as precursors tetraethoxysilane (TEOS) and silanes of type R-Si(OEt)3 with alkyl or aryl R groups, has been investigated. Three different methods using these precursors were tried exhibiting protein immobilization yields in the range of 20/50%. Hydrolysis of emulsified olive oil, esterification of lauric acid with 1-octanol and enantioselective acylation of 2-pentanol have been used as model reactions for testing the properties of the encapsulated
lipases. The recovery yields of the enzyme activity in the esterification reaction were between 20/68%, the best performance being achieved with phenyltriethoxysilane and tetraethoxysilane precursors at 3:1 molar ratio. When testing the entrapped
Lipase AK in the enantioselective acylation reaction of 2-pentanol, activity recovery yields up to 32% related to the free enzyme were obtained and the immobilization increased the enantioselectivity of the enzyme.
Cuvinte cheie: enantioselectivitate, lipaza microbiana, precursor silanic, entrapare sol-gel // enantioselectivity, microbial lipase, silane precursor, sol-gel entrapment