Abstract
The entrapment of lipases in hydrophobic sol-gel materials of RSi(OCH3)3 or mixtures of RSi(OCH3)3 and Si(OCH3)4 results in heterogeneous biocatalysts having dramatically enhanced enzyme activities as measured by the esterification of lauric acid by n-octanol in isooctane. These materials have been characterized by solid state NMR studies, revealing the degree of cross-linking. It is shown that this parameter generally does not correlate with relative enzyme activity. Likewise, the specific surface area or the pore size does not seem to be the decisive factor in determining the relative enzyme activities of the lipase-containing hybrid gels and the corresponding SiO2-gels obtained from Si(OCH3)4. Scanning electron microscopic studies (SEM) show that the hybrid gels all have a similar morphology. On the basis of these studies a model is proposed according to which most of the lipase enzyme is entrapped near the surface of the gel particles, where it is readily accessible by substrate molecules.
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