Immobilization of horseradish peroxidase on binary self-assembled monolayers with carboxyl- And hydroxyl-terminal groups: Dependence of the amount of immobilized enzymes and their electrocatalytic activity on the monolayer composition

Shinichiro Imabayashi, Miki Kashiwa, Masayoshi Watanabe

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The amount of covalently immobilized horseradish peroxidase (HRP), FHRP, and its electrocatalytic current, ired, are measured with changing the monolayer composition for two kinds of mixed self-assembled monolayers (SAMs) of COOH- and OH-termmated alkanethiols with different domain structures. In phase-separated SAMs of mercaptopropionic acid (MPA) and 11-mercaptoundecanol (MUOL), HRP is selectively immobilized on the MPA domains and, therefore, both γHRP and ired values increase in proportion to the surface mole fraction of MPA. In homogeneously mixed SAMs of 11-mercaptoundecanoic acid (MUA) and MUOL, HRP is homogeneously immobilized on the entire surface of the SAM, and γHRP and ired values reach constant values at the mole fraction of MUA, χMUA = 0.4. j.

Original languageEnglish
Pages (from-to)186-188
Number of pages3
JournalElectrochemistry
Volume74
Issue number2
Publication statusPublished - 2006
Externally publishedYes

Fingerprint

Immobilized Enzymes
Self assembled monolayers
Horseradish Peroxidase
Hydroxyl Radical
Monolayers
Enzymes
Acids
Chemical analysis
11-mercaptoundecanoic acid

Keywords

  • Binary Self-assembled Monolayer
  • Covalent Immobilization
  • Horseradish Peroxidase
  • Phase Properties

ASJC Scopus subject areas

  • Electrochemistry

Cite this

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title = "Immobilization of horseradish peroxidase on binary self-assembled monolayers with carboxyl- And hydroxyl-terminal groups: Dependence of the amount of immobilized enzymes and their electrocatalytic activity on the monolayer composition",
abstract = "The amount of covalently immobilized horseradish peroxidase (HRP), FHRP, and its electrocatalytic current, ired, are measured with changing the monolayer composition for two kinds of mixed self-assembled monolayers (SAMs) of COOH- and OH-termmated alkanethiols with different domain structures. In phase-separated SAMs of mercaptopropionic acid (MPA) and 11-mercaptoundecanol (MUOL), HRP is selectively immobilized on the MPA domains and, therefore, both γHRP and ired values increase in proportion to the surface mole fraction of MPA. In homogeneously mixed SAMs of 11-mercaptoundecanoic acid (MUA) and MUOL, HRP is homogeneously immobilized on the entire surface of the SAM, and γHRP and ired values reach constant values at the mole fraction of MUA, χMUA = 0.4. j.",
keywords = "Binary Self-assembled Monolayer, Covalent Immobilization, Horseradish Peroxidase, Phase Properties",
author = "Shinichiro Imabayashi and Miki Kashiwa and Masayoshi Watanabe",
year = "2006",
language = "English",
volume = "74",
pages = "186--188",
journal = "Electrochemistry",
issn = "1344-3542",
publisher = "Electrochemical Society of Japan",
number = "2",

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TY - JOUR

T1 - Immobilization of horseradish peroxidase on binary self-assembled monolayers with carboxyl- And hydroxyl-terminal groups

T2 - Dependence of the amount of immobilized enzymes and their electrocatalytic activity on the monolayer composition

AU - Imabayashi, Shinichiro

AU - Kashiwa, Miki

AU - Watanabe, Masayoshi

PY - 2006

Y1 - 2006

N2 - The amount of covalently immobilized horseradish peroxidase (HRP), FHRP, and its electrocatalytic current, ired, are measured with changing the monolayer composition for two kinds of mixed self-assembled monolayers (SAMs) of COOH- and OH-termmated alkanethiols with different domain structures. In phase-separated SAMs of mercaptopropionic acid (MPA) and 11-mercaptoundecanol (MUOL), HRP is selectively immobilized on the MPA domains and, therefore, both γHRP and ired values increase in proportion to the surface mole fraction of MPA. In homogeneously mixed SAMs of 11-mercaptoundecanoic acid (MUA) and MUOL, HRP is homogeneously immobilized on the entire surface of the SAM, and γHRP and ired values reach constant values at the mole fraction of MUA, χMUA = 0.4. j.

AB - The amount of covalently immobilized horseradish peroxidase (HRP), FHRP, and its electrocatalytic current, ired, are measured with changing the monolayer composition for two kinds of mixed self-assembled monolayers (SAMs) of COOH- and OH-termmated alkanethiols with different domain structures. In phase-separated SAMs of mercaptopropionic acid (MPA) and 11-mercaptoundecanol (MUOL), HRP is selectively immobilized on the MPA domains and, therefore, both γHRP and ired values increase in proportion to the surface mole fraction of MPA. In homogeneously mixed SAMs of 11-mercaptoundecanoic acid (MUA) and MUOL, HRP is homogeneously immobilized on the entire surface of the SAM, and γHRP and ired values reach constant values at the mole fraction of MUA, χMUA = 0.4. j.

KW - Binary Self-assembled Monolayer

KW - Covalent Immobilization

KW - Horseradish Peroxidase

KW - Phase Properties

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