Kinetic properties of soluble and immobilized Candida rugosa lipase

Immobilized lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) from Candida rugosa has been immobilized on commercially available microporous polypropylene and used for the batch hydrolysis of different animal fats. The effect of the reaction products at concentrations similar to those obtained at...

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Published inApplied biochemistry and biotechnology Vol. 50; no. 2
Main Authors Virto, M.D. (Universidad del Pais Vasco, Vitoria, Spain.), Agud, I, Montero, S, Blanco, A, Solozabal, R, Lascaray, J.M, Llama, M.J, Serra, J.L, Landeta, L.C, Renobales, M. de
Format Journal Article
LanguageEnglish
Published 01.02.1995
Subjects
ACIDE OLEIQUE
ACIDO OLEICO
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
CANDIDA
CORPS GRAS ANIMAL
GLICEROL
GLYCEROL
GRASAS ANIMALES
IMMOBILISATION
INHIBICION
INHIBITION
INMOVILIZACION
MEDIO DE CULTIVO
MILIEU DE CULTURE
SOLVANT
SOLVENTES
TRIACILGLICEROL LIPASA
TRIACYLGLYCEROL LIPASE
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Summary:Immobilized lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) from Candida rugosa has been immobilized on commercially available microporous polypropylene and used for the batch hydrolysis of different animal fats. The effect of the reaction products at concentrations similar to those obtained at 90% hydrolysis, both on soluble and immobilized lipase, was studied. Glycerol showed low inhibitory effect but oleic acid caused 50% inhibition. A mixture of free fatty acids present in the complete hydrolysis of beef tallow inhibited lipase activity more than 70%. The stability of the enzyme (both soluble and immobilized) was highest in the presence of 20% isooctane. The apparent Michaelis constant for each substrate for the soluble enzyme did not change on immobilization
Bibliography:9615377
Q60
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02783449