Chemistry Reference
In-Depth Information
5.2.9
Conclusions
Candida antarctica
lipase B (CALB) was successfully immobilized onto surface
modified silica gel particles. The surface modification of the silica particles was
performed by two different methods—namely a wet method (wet silica in aque-
ous solution) and dry method (dry silica in toluene). The surface modification of
porous silica gel particles was performed using (3-aminopropyl)triethoxysilane
(3-APS) and then the CALB was chemically cross linked using glutaraldehyde.
A high catalytic activity of the CALB immobilized wet-silica and dry-silica par-
ticles was observed when compared to free CALB and Novozym-435. A new excit-
ing bioinspired silica platform for enzyme immobilization was also established and
it exhibited excellent candidate for developing biocatalysts. Novozym-435
®
was
found to have superior thermal stability when compared to free CALB, to CALB
immobilized wet silica and to CALB immobilized dry silica particles.
Acknowledgements
We thank the National Science Foundation (NSF) for Center Funding to two
of us (Clarson and Gross) under the TIE Grant NSF #0631412. SVP thanks the Royal Society for
funding (Grant # TG090299).
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