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 language | English |
|---|---|
| Pages (from-to) | 186-188 |
| Number of pages | 3 |
| Journal | Electrochemistry |
| Volume | 74 |
| Issue number | 2 |
| Publication status | Published - 2006 |
| Externally published | Yes |
Fingerprint
Keywords
- Binary Self-assembled Monolayer
- Covalent Immobilization
- Horseradish Peroxidase
- Phase Properties
ASJC Scopus subject areas
- Electrochemistry
Cite this
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. / Imabayashi, Shinichiro; Kashiwa, Miki; Watanabe, Masayoshi.
In: Electrochemistry, Vol. 74, No. 2, 2006, p. 186-188.Research output: Contribution to journal › Article
}
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
UR - http://www.scopus.com/inward/record.url?scp=33645309390&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33645309390&partnerID=8YFLogxK
M3 - Article
VL - 74
SP - 186
EP - 188
JO - Electrochemistry
JF - Electrochemistry
SN - 1344-3542
IS - 2
ER -