Kinetic properties of soluble and immobilized Candida rugosa lipase

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URI: https://hdl.handle.net/11556/4083
ISSN: 0273-2289
DOI: 10.1007/BF02783449
Publication date
1995-02
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Abstract
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.
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animal fats hydrolysis , Candida rugosa , EC 3.1.1.3 , immobilized enzyme , kinetic parameters , Lipase , organic solvents , Biotechnology , Bioengineering , Biochemistry , Applied Microbiology and Biotechnology , Molecular Biology
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journal article
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Virto , M D , Agud , IS , Montero , S , Blanco , A , Solozabal , R , Lascaray , J M , Llama , M J , Serra , J L , Landeta , L C & De Renobales , M 1995 , ' Kinetic properties of soluble and immobilized Candida rugosa lipase ' , Applied Biochemistry and Biotechnology , vol. 50 , no. 2 , pp. 127-136 . https://doi.org/10.1007/BF02783449