Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
권호 표지

Hydrogen Peroxide, Its Measurement and Effect During Enzymatic Decoloring of Congo Red

  • Woo, Sung-Whan (Department of Biological Engineering, Inha University) ;
  • Cho, Jeung-Suk (Department of Biological Engineering, Inha University) ;
  • Hur, Byung-Ki (Department of Biological Engineering, Inha University) ;
  • Shin, Dong-Hoon (Graduate School of Biotechnology, Korea University) ;
  • Ryu, Keun-Gap (Chemical Engineering School, Ulsan University) ;
  • Kim, Eun-Ki (Department of Biological Engineering, Inha University)
  • Published : 2003.10.01
Download PDF
⟨ Previous Next ⟩

Abstract

The color of Congo red hinders the spectrometric measurements of a concentration of hydrogen peroxide and enzyme activity (Horseradish peroxidase; HRP) during enzymatic decoloring of Congo red. In this study, a method was developed to measure peroxidase activity and hydrogen peroxide concentration in the presence of Congo red. The oxidation product of HRP/hydrogen peroxide and ABTS(2,2'-azino-bis-(3-ethylbenzotriazoline-6-sulfonic acid)) formed a dark green color. The spectrum of this product showed absorption bands at 420 nm and 734 nm. When compared with the Congo red spectrum, the absorption at 734 nm of this product did not overlap with Congo red, thus making the hydrogen peroxide measurement possible even in the presence of Congo red. Kinetic study of decoloring of Congo red performed by this method showed that the decoloring reaction followed the Michaelis-Menten kinetics. Pulse feeding of hydrogen peroxide, upon depletion, significantly increased the decoloring of Congo red. This result shows that this newly developed technique can monitor, predict, and improve the enzymatic decoloring process.

Keywords

References

  1. Int. Chem. Kinet. v.30 Reaction of 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) derived radicals with hydroperoxides. Kinetics and mechanism Aliaga,C.;E.A.Lissi https://doi.org/10.1002/(SICI)1097-4601(1998)30:8<565::AID-KIN5>3.0.CO;2-Q
  2. Ecotoxicol. Environ. Safe v.3 Ecotoxicology of dyestuffs - a joint effort by industry Anliker,R. https://doi.org/10.1016/0147-6513(79)90060-5
  3. BioEssays v.6 Biodegradation of environmental pollutants by the white rot fungus Phanerochaete chrysosporium: involvement of the lignin degrading system Bumpus,J.A.;S.D.Aust
  4. Appl. Environ. Microbiol. v.56 Biodegradation of azo and heterocyclic dyes by Phanerochaete chrysosporium Cripps,C.;J.A.Bumpus;S.D.Aust
  5. Anal. Chim. Acta v.309 Flow-injection stopped-flow spectrofluorimetric kinetic determination of total ascorbic acid based on an enzyme-linked coupled reaction Huang,H.;R.Cai;Y.Du;Y.Zeng https://doi.org/10.1016/0003-2670(95)00056-6
  6. Anal. Sci. v.13 Catalytic determination of hydrogen peroxide by using the molybdenum-porphyrin complex as a mimetic enzyme of peroxidase Huang,X.M.;M.Zhu;L.Y.Mao;H.X.Shen
  7. Anal. Sci. v.15 Spectrophotometric determination of hydrogen peroxide using β-CD-hemin as a mimetic enzyme of peroxidase Huang,Y.;R.Cai;L.Mao;Z.Liu;H.Huang https://doi.org/10.2116/analsci.15.889
  8. Biotech. Biopro. Eng. v.8 Response of bioluminescent bacteria to sixteen azo dyes Lee,H.;S.Choi;M.Gu https://doi.org/10.1007/BF02940264
  9. Anal. Chim. Acta v.340 Comparative study of some synthesized and commercial fluorogenic substrates for horseradish peroxidase and its mimetic enzyme hemin by a flow injection method Li,Y.Z.;A.Townshend https://doi.org/10.1016/S0003-2670(96)00548-X
  10. Appl. Microbiol. Biotechnol. v.51 Oxidation of aromatic alcohols by laccase from Trametes versicolor mediated by the 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) cation radical and dication Majcherczyk,A.;C.Johannes;A.Huttermann https://doi.org/10.1007/s002530051392
  11. Environ. Chem. v.4 Sorption and toxicity of azo and triphenylmethane dyes to aquatic microbial populations Michaels,G.B.;D.L.Lewis https://doi.org/10.1897/1552-8618(1985)4[45:SATOAA]2.0.CO;2
  12. Environ. Toxicol. Chem. v.5 Microbial transformation rates of azo and triphenylmethane dyes Michaels,G.B.;D.L.Lewis https://doi.org/10.1897/1552-8618(1986)5[161:MTROAA]2.0.CO;2
  13. Anal. Sci. v.7 Application of peroxidase-like activity of anion-exchange resins modified with manganese(III)-tetrakis(sulfophenyl)porphine to determination of glucose, cholesterol and triglyceride Mifune,M.;J.Odo;N.Motohashi;Y.Saito;A.Iwado;Y.Tanaka;M.Chikuma;H.Tanaka
  14. Anal. Sci. v.14 Flow analysis of hydrogen peroxide with a dye-formation reaction catalyzed by an ion-exchange resin modified with $Mn^ {3+}$-tetrakis(sulfophenyl) porphine Mifune,M.;T.Mukuno;M.Tani;A.Iwado;J.Odo;N.Motohashi;Y.Saito https://doi.org/10.2116/analsci.14.519
  15. Chemosphere v.15 The degradation of dyestuffs in aerobic biodegradation tests Pagga,U.;D.Brown https://doi.org/10.1016/0045-6535(86)90542-4
  16. J. Microbiol. Biotechnol. v.2 Decolorization of azo dyes by Aspergillus sojae B-10 Ryu,B.H.;Y.D.Weon
  17. J. Microbiol. Biotechnol. v.11 Isolation and characterization of antibiotic and heavy metal-resistant Pseudomonas aeruginosa from different polluted waters in Sohag district, Egypt Soltan,El-Sayed.M.
  18. Anal. Chim. Acta v.370 Spectrophotometric determination of hydrogen peroxide in rainwater Tanner,P.A.;A.Y.S.Wong https://doi.org/10.1016/S0003-2670(98)00273-6
  19. J. Microbiol. Biotechnol. v.12 Biotechnological potential of marine cyanobacteria in wastewater treatment: Disinfection of raw sewage by Oscillatoria willei BDU130511 Uma,L.;K.Selvaraj;R.Manjula;G.Subramanian;S.Nagarkar
  20. J. Microbiol. Biotechnol. v.12 Effects of polyurethane as support material for the methanogenic digester of a two-stage anaerobic wastewater digestion system Woo,K.;H.Yang;W.Lim
  21. Eur. J. Biochem. v.129 Properties of purified orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46 Zimmerman,T.;H.G.Kulla;T.Leisinger https://doi.org/10.1111/j.1432-1033.1982.tb07040.x