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