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 angstroms, so it was large enough to accommodate protein molecules inside the channels. Immobilization by physical adsorption of a commercial lipase preparation from Mucor javanicus was performed at different pH values (pH 5-8). pH 6 gave the highest lipase loading and hydrolytic activity of the corresponding biocatalyst. Chemical modification of the SBA-15 via glutardialdehyde allowed also the enzyme immobilization through chemical adsorption. This preparation was active toward tributyrin hydrolysis. On the contrary, very low activity toward triolein hydrolysis was observed. The reduction of the size of the channels due the immobilization process has been suggested as a possible explanation.
Immobilization of Pseudomonas fluorescens lipase (Pfl) on the chemically modified, or unmodified, surface of SBA‐15 mesoporous silica has been achieved. X‐ray diffraction (XRD), transmission electron microscopy (TEM), and N2 physisorption are used to monitor the effect of surface functionalization on the structural and textural features of the SBA‐15 silica support. The enzyme loading strongly depends on the type of enzyme–support interaction, the maximal loading of the chemisorbed lipase being about twice that of the physisorbed (502 and 256 mgprotein ${{\rm g}{{- 1\hfill \atop {\rm support}\hfill}}}$ respectively). The resulting biocatalysts, regardless of the different loading, are tested with a hydrolytic catalytic assay. Despite the lower loading, the physically immobilized Pfl is more active than that which is chemically immobilized. Both biocatalysts are also active in a green process for biodiesel production, leading to almost full conversion of sunflower oil and ethanol into the corresponding ethyl esters after about 7 h at 30 °C, atmospheric pressure, and in solvent‐free conditions. Recycling experiments showed that the chemically immobilized Pfl was still active after twenty reaction cycles whereas the physically immobilized Pfl lost its activity after the tenth cycle.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.