Adsorption Properties and Activities of Lipase on a Gold Substrate Modified by Self-assembled Monolayers.
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- KOBAYASHI Atsushi
- National Institute of Advanced Industrial Science and Technology
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- SATO Yukari
- National Institute of Advanced Industrial Science and Technology
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- MIZUTANI Fumio
- National Institute of Advanced Industrial Science and Technology
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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.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 65 (11), 2392-2396, 2001
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206473868672
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- NII論文ID
- 110002693298
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD3MXovFOgs7g%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 6003821
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- PubMed
- 11791710
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可
