Abstract
Microperoxidase-11 (MP-11), which is a heme-containing undecapeptide derived from horse heart cytochrome c, was utilized as a peroxidative catalyst in the system of bis(2-ethylhexyl)sulphosuccinate sodium salt (AOT)-reversed micelles to oxidatively decolorize water-insoluble dyes in isooctane. MP-11 entrapped in the reversed micelles exhibited a peroxidative activity in the presence of H2O2, effectively catalyzing the oxidative decolorization of an azo dye Solvent Yellow 7 and an anthraquinone dye Solvent Blue 11 in the hydrophobic organic solvent. H2O2-derived heme bleaching was successfully suppressed by replacing H2O2 with an organic hydroperoxide, tert-butyl hydroperoxide (t-BuOOH), thus sustaining a stable decolorization activity in the system. To optimize the reversed micellar system, the effect of the pH and the molar ratio of H2O/AOT hydration degree (Wo) was examined, indicating that MP-11 exhibited a maximal decolorization activity at pH 8-10 with the Wo value of 20.
| Original language | English |
|---|---|
| Pages (from-to) | 237-241 |
| Number of pages | 5 |
| Journal | Biochemical Engineering Journal |
| Volume | 12 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Dec 1 2002 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Environmental Engineering
- Biomedical Engineering
Cite this
Decolorization of azo and anthraquinone dyes in hydrophobic organic media using microperoxidase-11 entrapped in reversed micelles. / Okazaki, Shin Ya; Nagasawa, Shin Ichiro; Goto, Masahiro; Furusaki, Shintaro; Wariishi, Hiroyuki; Tanaka, Hiroo.
In: Biochemical Engineering Journal, Vol. 12, No. 3, 01.12.2002, p. 237-241.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Decolorization of azo and anthraquinone dyes in hydrophobic organic media using microperoxidase-11 entrapped in reversed micelles
AU - Okazaki, Shin Ya
AU - Nagasawa, Shin Ichiro
AU - Goto, Masahiro
AU - Furusaki, Shintaro
AU - Wariishi, Hiroyuki
AU - Tanaka, Hiroo
PY - 2002/12/1
Y1 - 2002/12/1
N2 - Microperoxidase-11 (MP-11), which is a heme-containing undecapeptide derived from horse heart cytochrome c, was utilized as a peroxidative catalyst in the system of bis(2-ethylhexyl)sulphosuccinate sodium salt (AOT)-reversed micelles to oxidatively decolorize water-insoluble dyes in isooctane. MP-11 entrapped in the reversed micelles exhibited a peroxidative activity in the presence of H2O2, effectively catalyzing the oxidative decolorization of an azo dye Solvent Yellow 7 and an anthraquinone dye Solvent Blue 11 in the hydrophobic organic solvent. H2O2-derived heme bleaching was successfully suppressed by replacing H2O2 with an organic hydroperoxide, tert-butyl hydroperoxide (t-BuOOH), thus sustaining a stable decolorization activity in the system. To optimize the reversed micellar system, the effect of the pH and the molar ratio of H2O/AOT hydration degree (Wo) was examined, indicating that MP-11 exhibited a maximal decolorization activity at pH 8-10 with the Wo value of 20.
AB - Microperoxidase-11 (MP-11), which is a heme-containing undecapeptide derived from horse heart cytochrome c, was utilized as a peroxidative catalyst in the system of bis(2-ethylhexyl)sulphosuccinate sodium salt (AOT)-reversed micelles to oxidatively decolorize water-insoluble dyes in isooctane. MP-11 entrapped in the reversed micelles exhibited a peroxidative activity in the presence of H2O2, effectively catalyzing the oxidative decolorization of an azo dye Solvent Yellow 7 and an anthraquinone dye Solvent Blue 11 in the hydrophobic organic solvent. H2O2-derived heme bleaching was successfully suppressed by replacing H2O2 with an organic hydroperoxide, tert-butyl hydroperoxide (t-BuOOH), thus sustaining a stable decolorization activity in the system. To optimize the reversed micellar system, the effect of the pH and the molar ratio of H2O/AOT hydration degree (Wo) was examined, indicating that MP-11 exhibited a maximal decolorization activity at pH 8-10 with the Wo value of 20.
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UR - http://www.scopus.com/inward/citedby.url?scp=0036883474&partnerID=8YFLogxK
U2 - 10.1016/S1369-703X(02)00074-8
DO - 10.1016/S1369-703X(02)00074-8
M3 - Article
AN - SCOPUS:0036883474
VL - 12
SP - 237
EP - 241
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
SN - 1369-703X
IS - 3
ER -