%0 Journal Article
	%A C. Zarcula and  R. Croitoru and  L. Corîci and  C. Csunderlik and  F. Peter
	%D 2009
	%J International Journal of Chemical and Molecular Engineering
	%B World Academy of Science, Engineering and Technology
	%I Open Science Index 28, 2009
	%T Improvement of Lipase Catalytic Properties by Immobilization in Hybrid Matrices
	%U https://publications.waset.org/pdf/781
	%V 28
	%X Lipases are enzymes particularly amenable for
immobilization by entrapment methods, as they can work equally
well in aqueous or non-conventional media and long-time stability of
enzyme activity and enantioselectivity is needed to elaborate more
efficient bioprocesses. The improvement of Pseudomonas
fluorescens (Amano AK) lipase characteristics was investigated by
optimizing the immobilization procedure in hybrid organic-inorganic
matrices using ionic liquids as additives. Ionic liquids containing a
more hydrophobic alkyl group in the cationic moiety are beneficial
for the activity of immobilized lipase. Silanes with alkyl- or aryl
nonhydrolizable groups used as precursors in combination with
tetramethoxysilane could generate composites with higher
enantioselectivity compared to the native enzyme in acylation
reactions of secondary alcohols. The optimal effect on both activity
and enantioselectivity was achieved for the composite made from
octyltrimethoxysilane and tetramethoxysilane at 1:1 molar ratio (60%
increase of total activity following immobilization and enantiomeric
ratio of 30). Ionic liquids also demonstrated valuable properties as
reaction media for the studied reactions, comparable with the usual
organic solvent, hexane.
	%P 203 - 208