In this paper the performance of different supports respect to the lipase immobilization was investigated. The used enzyme was the lipase from Rhizomucor miehei (RML - commercial name: Palatase). The immobilization tests on mesoporous materials (MCM-41), de laminated zeolites (ITQ-2 and ITQ-6), Na-Silicalite-1, H-Silicalite-1 and F AU zeolites, were carried out by adsorption. The pore size, morphology, crystal dimension, acidity, hydrophobicity and chemical composition of the supports, strongly influence the amount of the enzyme adsorbed. The Na-silicalite-1 support shows the best lipase immobilization capacity, with an efficiency of c.a. 74% respect to the 41% of MCM-41 and the 27% of ITQ-2 type materials, while no enzyme is retained on the zeolite FAU (zeolite X). The preliminary activity tests using the lipase-support as a catalyst, were carried out for the reaction of hydrolysis of triglycerides. The activity observed for the lipase-Na-Silicalite-1 and the lipase-MCM-41 catalysts is 86% and 78%, respectively, respect to the activity of the free lipase enzyme in solution.

Immobilization of Lipase on microporous and mesoporous materials: studies of the support surfaces

SETTI, LEONARDO
2005

Abstract

In this paper the performance of different supports respect to the lipase immobilization was investigated. The used enzyme was the lipase from Rhizomucor miehei (RML - commercial name: Palatase). The immobilization tests on mesoporous materials (MCM-41), de laminated zeolites (ITQ-2 and ITQ-6), Na-Silicalite-1, H-Silicalite-1 and F AU zeolites, were carried out by adsorption. The pore size, morphology, crystal dimension, acidity, hydrophobicity and chemical composition of the supports, strongly influence the amount of the enzyme adsorbed. The Na-silicalite-1 support shows the best lipase immobilization capacity, with an efficiency of c.a. 74% respect to the 41% of MCM-41 and the 27% of ITQ-2 type materials, while no enzyme is retained on the zeolite FAU (zeolite X). The preliminary activity tests using the lipase-support as a catalyst, were carried out for the reaction of hydrolysis of triglycerides. The activity observed for the lipase-Na-Silicalite-1 and the lipase-MCM-41 catalysts is 86% and 78%, respectively, respect to the activity of the free lipase enzyme in solution.
2005
Oxide Based Materials New sources, novel phases, new applications
381
394
Macario A.; Katovic A.; Giordano G.; L. Forni; F. Carloni; A. Filippini; L. Setti
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/21403
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