Immobilization of His-tagged endoglucanase on gold via various Ni-NTA self-assembled monolayers and its hydrolytic activity
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Updated: Jun 10, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Itsuko Nakamura1, Akira Makino, Masashi Ohmae
1Department of Material Chemistry, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku-Katsura, Nishikyo-ku, Kyoto, Japan.
Abstract:
A genetically modified His-tagged endoglucanase, EGII(core2), with two active sites in series was immobilized on gold via three different kinds of anchor molecules, and its hydrolytic activity was studied. Immobilization of EGII(core2) was influenced by the chain length and hydrophilicity of anchor molecules. The hydrolytic activity of the immobilized EGII(core2) was nearly the same on either anchor molecule. Interestingly, the immobilized EGII(core2) apparently retained the inherent hydrolytic activity similarly to free EGII(core2). It is therefore considered that the local high concentration of EGII(core2) on the surface should promote the successive hydrolysis of the transient products to show the high hydrolytic activity despite of immobilization.
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