scholarly journals Effect of template type on the preparation of the emeraldine salt form of polyaniline (PANI-ES) with horseradish peroxidase isoenzyme C (HRPC) and hydrogen peroxide

RSC Advances ◽  
2019 ◽  
Vol 9 (57) ◽  
pp. 33080-33095 ◽  
Author(s):  
Tomoyuki Fujisaki ◽  
Keita Kashima ◽  
Sandra Serrano-Luginbühl ◽  
Reinhard Kissner ◽  
Danica Bajuk-Bogdanović ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Emeraldine Salt ◽  
Salt Form ◽  
Peroxidase Isoenzyme ◽  
Different Types

Different types of templates consisting of sulfonate or sulfate groups were compared for the horseradish peroxidase/H2O2-catalysed synthesis of the emeraldine salt form of polyaniline from aniline at pH = 4.3.

scholarly journals Reproduction of vesicles coupled with a vesicle surface-confined enzymatic polymerisation

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Minoru Kurisu ◽  
Harutaka Aoki ◽  
Takehiro Jimbo ◽  
Yuka Sakuma ◽  
Masayuki Imai ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
External Solution ◽  
Molecular Assembly ◽  
Darwinian Evolution ◽  
Assembly Systems ◽  
Emeraldine Salt ◽  
Minimal Cell ◽  
Salt Form ◽  
Reproduction System

Abstract Molecular assembly systems that have autonomous reproduction and Darwinian evolution abilities can be considered as minimal cell-like systems. Here we demonstrate the reproduction of cell-sized vesicles composed of AOT, i.e., sodium bis-(2-ethylhexyl) sulfosuccinate, coupled with an enzymatic polymerisation reaction occurring on the surface of the vesicles. The particular reaction used is the horseradish peroxidase-catalysed polymerisation of aniline with hydrogen peroxide as oxidant, which yields polyaniline in its emeraldine salt form (PANI-ES). If AOT micelles are added during this polymerisation reaction, the AOT - PANI-ES vesicles interact with the AOT molecules in the external solution and selectively incorporate them in their membrane, which leads to a growth of the vesicles. If the AOT vesicles also contain cholesterol, the vesicles not only show growth, but also reproduction. An important characteristic of this reproduction system is that the AOT-based vesicles encourage the synthesis of PANI-ES and PANI-ES promotes the growth of AOT vesicles.

scholarly journals Application of an enzymatic cascade reaction for the synthesis of the emeraldine salt form of polyaniline

2021 ◽  
Author(s):  
Minoru Kurisu ◽  
Reinhard Kissner ◽  
Masayuki Imai ◽  
Peter Walde
Keyword(s):  
Cascade Reaction ◽  
Emeraldine Salt ◽  
Salt Form ◽  
Experimental Conditions ◽  
Peroxidase Isoenzyme ◽  
Large Unilamellar Vesicles ◽  
Dark Green ◽  
Catalyzed Oxidation ◽  
Reference Reaction

AbstractThe synthesis of the emeraldine salt form of polyaniline (PANI-ES) from aniline with Aspergillus sp. glucose oxidase (GOD), d-glucose, dissolved O2, and horseradish peroxidase isoenzyme C (HRPC) in the presence of large unilamellar vesicles of AOT (sodium bis-(2-ethylhexyl)sulfosuccinate) as templates at pH = 4.3 and T ~ 25 °C was investigated in a systematic way. In this cascade reaction mixture, the oxidation of aniline is catalyzed by HRPC with H2O2 that is formed in situ as byproduct of the GOD-catalyzed oxidation of d-glucose with O2. Under the elaborated experimental conditions which we considered ideal, the formation of PANI-ES products is evident, as judged by UV/Vis/NIR and EPR measurements. Comparison was made with a reference reaction, which was run under similar conditions with added H2O2 instead of GOD and d-glucose. Although the reference reaction was found to be superior, with the cascade reaction, PANI-ES products can still be obtained with high aniline conversion (> 90%) within 24 h as stable dark green PANI-ES/AOT vesicle dispersion. Our results show that the in situ formation of H2O2 does not prevent the inactivation of HRPC known to occur in the reference reaction. Moreover, the GOD used in the cascade reaction is inactivated as well by polymerization intermediates.

Preparation of aqueous polyaniline-vesicle suspensions with class III peroxidases. Comparison between horseradish peroxidase isoenzyme C and soybean peroxidase

2013 ◽  
Vol 67 (8) ◽  
Author(s):  
Katja Junker ◽  
Ivan Gitsov ◽  
Nick Quade ◽  
Peter Walde
Keyword(s):  
Horseradish Peroxidase ◽  
Enzyme Stability ◽  
Class Iii ◽  
Salt Form ◽  
Reaction Conditions ◽  
Soybean Peroxidase ◽  
Peroxidase Isoenzyme ◽  
Complete Inactivation ◽  
Class Iii Peroxidases ◽  
Optimal Reaction

AbstractAniline was polymerised enzymatically in aqueous solution at pH = 4.3 and 25°C in the presence of submicrometer-sized vesicles formed from sodium bis(2-ethylhexyl)sulphosuccinate (AOT). H2O2 served as oxidant and the enzyme used was either horseradish peroxidase isoenzyme C (HRPC) or soybean peroxidase (SBP), both being class III peroxidases. From previous studies with HRPC, it is known that stable vesicle suspensions containing the emeraldine salt form of polyaniline (PANI-ES) can be obtained within 1–2 days with a 90–95 % yield, provided that optimal reaction conditions are applied. Unfortunately, HRPC becomes inactivated during polymerisation. In the present study, a linear dendritic block copolymer was added to HRPC, resulting in higher operational enzyme stability; the stabilising effect, however, was too small to afford a substantial decrease in the required amount of enzyme. Moreover, replacing HRPC with SBP was of no advantage, although SBP is known to be more stable towards inactivation by H2O2 than HRPC. By contrast, SBP was found to be much slower in oxidising aniline, and complete inactivation of SBP occurred before all the aniline monomers were oxidised, leading to low yields and the formation of over-oxidised products. The same was observed for HRP isoenzyme A2. Reactions without vesicles indicated that peroxidase inactivation was probably caused by PANI-ES.

The inactivation of horseradish peroxidase isoenzyme AZ by hydrogen peroxide: an example of partial resistance due to the formation of a stable enzyme intermediate

2001 ◽  
Vol 6 (5-6) ◽  
pp. 504-516 ◽  
Author(s):  
Alexander N. P. Hiner ◽  
Josefa Hernández-Ruiz ◽  
José Neptuno Rodríguez-López ◽  
Marino B. Arnao ◽  
Ramón Varón ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Partial Resistance ◽  
Peroxidase Isoenzyme ◽  
Enzyme Intermediate

scholarly journals Monitoring the heme iron state in horseradish peroxidase to detect ultratrace amounts of hydrogen peroxide in alcohols

RSC Advances ◽  
2021 ◽  
Vol 11 (17) ◽  
pp. 9901-9910
Author(s):  
Raheleh Ravanfar ◽  
Alireza Abbaspourrad
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Oxidative Damage ◽  
Heme Iron ◽  
Aqueous Systems ◽  
Iron State ◽  
Low Concentrations

Despite the importance of hydrogen peroxide (H2O2) in initiating oxidative damage and its connection to various diseases, the detection of low concentrations of H2O2 (<10 μM) is still limited using current methods, particularly in non-aqueous systems.

scholarly journals The Reaction of Ferrous Horseradish Peroxidase with Hydrogen Peroxide

1970 ◽  
Vol 245 (9) ◽  
pp. 2409-2413
Author(s):  
Robert W. Noble ◽  
Quentin H. Gibson
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase

scholarly journals Fluorescent Derivatization of Aromatic Carboxylic Acids with Horseradish Peroxidase in the Presence of Excess Hydrogen Peroxide

2015 ◽  
Vol 31 (1) ◽  
pp. 37-44
Author(s):  
Junichi ODO ◽  
Masahiko INOGUCHI ◽  
Hiroyuki AOKI ◽  
Yuto SOGAWA ◽  
Masahiro NISHIMURA
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Carboxylic Acids ◽  
Aromatic Carboxylic Acids ◽  
Excess Hydrogen

scholarly journals Detection of a Tryptophan Radical as an Intermediate Species in the Reaction of Horseradish Peroxidase Mutant (Phe-221 → Trp) and Hydrogen Peroxide

1998 ◽  
Vol 273 (24) ◽  
pp. 14753-14760 ◽  
Author(s):  
Atsushi Morimoto ◽  
Motomasa Tanaka ◽  
Satoshi Takahashi ◽  
Koichiro Ishimori ◽  
Hiroshi Hori ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Intermediate Species
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