Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 48, Issue 3-4, Pages 84-89Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2007.06.010
Keywords
protein adsorption; lipase; immobilization
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Immobilization of Candida antarctica B lipase was examined on gold surfaces modified with either methyl- or hydroxyl-terminated self-assembled alkylthiol monolayers (SAMs), representing hydrophobic and hydrophilic surfaces, respectively. Lipase adsorption was monitored gravimetrically using a quartz crystal microbalance. Lipase activity was determined colorimetrically by following p-nitrophenol propionate hydrolysis. Adsorbed lipase topography was examined by atomic force microscopy. The extent of lipase adsorption was nearly identical on either surface (approximately 240 ng cm(-2)), but its specific activity was sixfold higher on the methyl -terminated SAM, showing no activity loss upon immobilization. A uniform, 5.5 nm high, highly packed monolayer of CALB formed on the methyl-tenninated SAM, while the adsorbed protein was disordered on the hydroxyl -terminated SAM. Hydrophobic surfaces thus may specifically orient the lipase in a highly active state. Published by Elsevier B.V.
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