Adsorption properties and activities of lipase on a gold substrate modified by self-assembled monolayers

被引：12

作者：

Kobayashi, A ^{[1
]}

Sato, Y ^{[1
]}

Mizutani, F ^{[1
]}

机构：

[1] Natl Inst Adv Ind Sci & Technol, Tsukuba, Ibaraki 3058566, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2001年 / 65卷 / 11期

关键词：

self-assembled monolayer; lipase; interfacial activation; quartz crystal microbalance;

D O I：

10.1271/bbb.65.2392

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2392 / 2396

页数：5

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