| Abstract
| - In this work a sample of SBA-15 mesoporous silica was synthesized and characterized by TEM, XRD,and N2 adsorption. The sample had a high value of specific surface area (1007 m2 g-1) and total pore volume(2.1 cm3 g-1). The pore diameter was 67 Å, so it was large enough to accommodate protein molecules insidethe channels. Immobilization by physical adsorption of a commercial lipase preparation from Mucor javanicuswas performed at different pH values (pH 5−8). pH 6 gave the highest lipase loading and hydrolytic activityof the corresponding biocatalyst. Chemical modification of the SBA-15 via glutardialdehyde allowed alsothe enzyme immobilization through chemical adsorption. This preparation was active toward tributyrinhydrolysis. On the contrary, very low activity toward triolein hydrolysis was observed. The reduction ofthe size of the channels due the immobilization process has been suggested as a possible explanation.
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