Enzymes have important catalytic properties: high specificity, high enantio- and regio-selectivity, and mild operation condition. Due to the fact that most of biocatalysts are very expensive for industrial purpose, the possibility to immobilize enzyme allows to reduce the catalyst costs and offers several advantages including reuse, easy product separation, enhancement of enzyme stability and continuous operation. The immobilization route of a particular enzyme has to be carried out considering the three-dimensional enzyme structure, the protein sequence and its mechanism of action. The screening of the suitable support as well the immobilization conditions results limiting factors for developing high performance biocatalysts. In this paper, the binding forces between Lipase from Rhizomucor miehei and inorganic supports, such as Silicalite-1 (synthesized with different mineralizing agents) and MCM-41 materials, are investigated in order to define the best conditions for obtain active and stable immobilized enzyme. The activity of immobilized enzyme has been tested towards hydrolysis of methyl myristate ester to myristic acid.
The role of the micro and mesoporous materials external surface in the Rhizomucor miehei Lipase adsorption, a biocatalyst for biodiesel production / Macario A.; Giordano G.; Frontera P.; Crea F.; Setti L.;. - ELETTRONICO. - (2006), p. s.n.. (Intervento presentato al convegno ZMPC International Symposium on Zeolites and Microporous Crystals tenutosi a Yonago, Japan nel 30 Luglio – 2 Agosto 2006).
The role of the micro and mesoporous materials external surface in the Rhizomucor miehei Lipase adsorption, a biocatalyst for biodiesel production
SETTI, LEONARDO
2006
Abstract
Enzymes have important catalytic properties: high specificity, high enantio- and regio-selectivity, and mild operation condition. Due to the fact that most of biocatalysts are very expensive for industrial purpose, the possibility to immobilize enzyme allows to reduce the catalyst costs and offers several advantages including reuse, easy product separation, enhancement of enzyme stability and continuous operation. The immobilization route of a particular enzyme has to be carried out considering the three-dimensional enzyme structure, the protein sequence and its mechanism of action. The screening of the suitable support as well the immobilization conditions results limiting factors for developing high performance biocatalysts. In this paper, the binding forces between Lipase from Rhizomucor miehei and inorganic supports, such as Silicalite-1 (synthesized with different mineralizing agents) and MCM-41 materials, are investigated in order to define the best conditions for obtain active and stable immobilized enzyme. The activity of immobilized enzyme has been tested towards hydrolysis of methyl myristate ester to myristic acid.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
