S. Mitchell, J. Pérez-Ramírez / Catalysis Today 168 (2011) 28–37
37
ied thiol functionalized surfaces are found to be most promising,
showing higher degrees of conversion in ester hydrolysis in all
cases. Improvements in enzyme immobilization have previously
been reported for thiol terminated surfaces [47]. This has been
related to improved enzyme stability due to increased surface
hydrophobicity or due to interaction of the thiol groups with –SH
or other S-containing groups present on the enzyme surface (e.g.
lipase enzymes are also known to require interfacial activation in
order for the active site to be accessible. ‘Hyperactivation’ of the
enzyme (i.e. where the supported enzyme adopts a conformation
in which the active site is exposed) is another common explana-
tion [49,67]. No such activity enhancement was observed for lipases
immobilized on amine functionalized supports or for those modi-
fied with glutaraldehyde whose activities were found to reflect the
amount of supported enzyme.
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6. Conclusions
Mesopores present in hierarchical zeolites prepared by desili-
cation are accessible to lipase enzymes and have tunable surface
properties, extending their potential as hosts to larger guest
species. Enhancement in the enzyme uptake and biocatalytic activ-
ity with respect to purely microporous zeolites may be directly
correlated to the increased mesoporous surface area. Surface func-
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cross-linking agent glutaraldehyde was found to be imperative in
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Appendix A. Supplementary data
Supplementary data associated with this article can be found, in
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