Effect of the Immobilization Method of Lipase from Thermomyces lanuginosus on Sucrose Acylation |
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Authors: | Manuel Ferrer Francisco J. Plou Gloria Fuentes M. Angeles Cruces Lotte Andersen Ole Kirk |
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Affiliation: | 1. Departamento de Biocatálisis, Instituto de Catálisis, CSIC, Cantoblanco 28049, Madrid, Spain;2. Novozymes A/S, Novó Allé 2880, Bagsvaerd, Denmark |
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Abstract: | Lipase from Thermomyces lanuginosus (formerly Humicola lanuginosa ) was immobilized using granulation by incubating low-particle-size silica with the lipase. Granules with a particle diameter in the range 0.3-1 u mm were obtained. The immobilized lipase was tested in the acylation of sucrose with vinyl laurate in mixtures of tert -amyl alcohol: dimethyl sulfoxide. Results were compared with immobilization of enzyme by adsorption on polypropylene (Accurel EP100), deposition on Celite by precipitation, and covalent attachment to Eupergit C. Granulated lipase converted >95% of sucrose into 6- O -lauroylsucrose in 6 u h. Accurel-lipase was also very active, converting 70% of sucrose into monoester in 2 u h. The residual activity of granules after five reaction cycles under the best reaction conditions was 72%; this value was considerably higher than the one observed for the same lipase adsorbed on Accurel (15% residual activity after five cycles). |
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Keywords: | Immobilization Adsorption Granulation Lipases Sucrose Esters Lipase Stability |
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