Adsorption properties and activities of lipase on a gold substrate modified by self-assembled monolayers.
The adsorption properties, amount and specific activity of lipase D from Rhizopus delemar were investigated by employing a gold substrate modified with seven kinds of thiol monolayer. Quartz crystal microbalance measurements revealed that the amount of the enzyme adsorbed to the hydrophobic monolayers (e.g. benzenethiol) was much higher than that to the hydrophilic monolayers (e.g. 3-mercaptopropanoic acid). In contrast, lipase D adsorbed to the hydrophilic, 2-amino-1-ethanethiol monolayer showed the highest specific activity, the value being 300-fold higher than for the same enzyme dissolved in an aqueous medium.
Kobayashi
A
A
National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki, Japan.
Sato
Y
Y
Mizutani
F
F
D000327:Adsorption; D001709:Biotechnology; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006046:Gold; D008049:Lipase / Q000378:metabolism*; D012233:Rhizopus / Q000201:enzymology; D013438:Sulfhydryl Compounds; D013499:Surface Properties
D004800:Enzymes, Immobilized; D013438:Sulfhydryl Compounds; D006046:Gold; D008049:Lipase