Browsing by Author "Serra, Juan L."
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Item Hydrolysis of animal fats by immobilized Candida rugosa lipase(1994-01) Virto, María D.; Agud, Isabel; Montero, Sol; Blanco, Alicia; Solozabal, Rodolfo; Lascaray, JoséM M.; Llama, María J.; Serra, Juan L.; Landeta, L. Carlos; de Renobales, Mertxe; Centros PRE-FUSION TECNALIA - (FORMER); Tecnalia Research & InnovationLipase (triacylglycerol ester hydrolase, EC 3.1.1.3) from Candida rugosa was immobilized by adsorption on a commercially available microporous polypropylene support of 200- to 400-μm particle size. A contact period of 90 min allowed the highest degrees of hydrolysis to be achieved, particularly in the second and third hydrolysis reactions. The optimal hydrolysis conditions were 0.10 kg enzyme per kilogram fat, 50% (w/v) fat, and 40°C for 24 h. The immobilized enzyme can be repeatedly used and hydrolysis degrees of 90% or higher can be achieved. Of the three animal fats studied, edible pork lard consistently yielded the highest degrees of hydrolysis (95%) in the first hydrolysis reaction and inedible beef tallow the lowest (65%). The immobilized enzyme lost its activity above 45°C. The support could be easily recovered and reused up to 5 times.Item Kinetic properties of soluble and immobilized Candida rugosa lipase(1995-02) Virto, Mar'ia D.; Agud, ISabel; Montero, Sol; Blanco, Alicia; Solozabal, Rodolfo; Lascaray, Jos'e M.; Llama, Mar'ia J.; Serra, Juan L.; Landeta, L. Carlos; De Renobales, Mertxe; Centros PRE-FUSION TECNALIA - (FORMER); Tecnalia Research & InnovationImmobilized 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.