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Janny Coca Armas1, JosйLuis Martнnez Hernбndez2, Julio Dustet Mendoza1

Study of some catalytic properties of immobilized lipase fromMucor Griseocyanus

Abstract

In this work a fungi, Mucor griseocyanus strain 55.1.1 was used for the production of lipase using different substrates as main carbon sources and ammonium sulphate as nitrogen source. About 0,1 IU/mL of lipolitic activity was obtained on fourth day of fermentation process. The optimum pH for the crude enzyme extract was in the range of 4 to 6 and the optimum and temperature was 60oC. The enzyme extract was stable for 5 hours at moderate temperatures between 20 and 40oC and at pH 6. Studies on the catalytic properties (stereoselectivity and enantioselectivity) of the immobilized lipase using Methyl phenyl glycinate and (R,S)-Methyl mandelate esters showed the excellent properties of the enzyme compared to commercial lipases tested. M. griseocyanus lipase exhibited a greater stereoselectivity towards the R species of methyl phenyl glycinate ester. However with methyl mandelate ester, the enzyme showed a certain preference toward the S-isomer and it was hydrolysed 20 times faster than the R-isomer.
Moscow University Chemistry Bulletin.
2006, Vol. 47, No. 2, P. 103
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
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