RT Journal Article
T1 Kinetic properties of soluble and immobilized Candida rugosa lipase
A1 Virto, Mar'ia D.
A1 Agud, ISabel
A1 Montero, Sol
A1 Blanco, Alicia
A1 Solozabal, Rodolfo
A1 Lascaray, Jos'e M.
A1 Llama, Mar'ia J.
A1 Serra, Juan L.
A1 Landeta, L. Carlos
A1 De Renobales, Mertxe
AB 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.
SN 0273-2289
YR 1995
FD 1995-02
LK https://hdl.handle.net/11556/4083
UL https://hdl.handle.net/11556/4083
LA eng
NO 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
DS TECNALIA Publications
RD 30 jul 2024