Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts

A support for enzyme immobilization was prepared by functionalization of mesoporous silica with octyltriethoxysilane. The features of the surface enables the adsorption of lipase from Candida antarctica B via strong hydrophobic interactions, enhancing the stability of the adsorbed enzyme molecules....

Full description

Saved in:
Bibliographic Details
Published inJournal of molecular catalysis. B, Enzymatic Vol. 30; no. 2; pp. 83 - 93
Main Authors Blanco, Rosa M, Terreros, Pilar, Fernández-Pérez, Mónica, Otero, Cristina, Dı́az-González, Guadalupe
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 03.08.2004
Elsevier Science
Subjects
Adsorption
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Candida antarctica B
Ethanolamine
Fundamental and applied biological sciences. Psychology
Immobilization
Lipase
Methods. Procedures. Technologies
Silica
Immobilization
Ethanolamine
Adsorption
Lipase
Silica
Candida antarctica B
candida antarctica
Support
Enzyme
Triacylglycerol lipase
Esterases
Carboxylic ester hydrolases
Fungi
Characterization
Functionalization
Hydrolases
Fungi Imperfecti
Catalyst
Thallophyta
Online AccessGet full text

Cover

More Information
Summary:A support for enzyme immobilization was prepared by functionalization of mesoporous silica with octyltriethoxysilane. The features of the surface enables the adsorption of lipase from Candida antarctica B via strong hydrophobic interactions, enhancing the stability of the adsorbed enzyme molecules. Derivatives with a high enzyme loading (200 mg protein/g of silica) can be obtained due to the high porosity and surface properties of the support while the immobilization occurs in a monolayer fashion. The lack of inactive enzyme aggregates, together with the high enzyme loading, are responsible for the high catalytic activity achieved by these species. Derivatives were prepared with different lipase loading, and the activities were tested and compared to the commercial derivative Novozym 435. The stability of the catalyst and hence its industrial applicability were tested by performing subsequent reaction cycles of acylation of ethanolamine with lauric acid in acetonitrile. Conversion was quantitative even after 15 reaction cycles.
ISSN:1381-1177
1873-3158
DOI:10.1016/j.molcatb.2004.03.012