Journal
BIOCATALYSIS AND BIOTRANSFORMATION
Volume 25, Issue 2-4, Pages 328-335Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/10242420701444256
Keywords
lipase; zeolites; adsorption; covalent binding; biodiesel; transesterification
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In order to understand the role of the acid-base, electrostatic and covalent interactions between enzyme and support, the catalytic behavior of the Rhizomucor miehei lipase (RML) immobilized on zeolite materials has been studied. The highest lipase activities were obtained when this enzyme, immobilized by adsorption, interacts through acid-base binding forces with the support surface, resulting in activation of the enzyme catalytic center. Due to the interest in biodiesel production by mild enzymatic transesterification, this heterogeneous biocatalyst has been used in transesterification of fatty acids contained in olive oil. The results show a high oleic acid conversion for several reaction cycles with a higher total biodiesel productivity compared to that using the free enzyme.
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