Mechanistic studies on the effect of veratryl alcohol on the lignin peroxidase catalyzed oxidation of pyrogallol red in reversed micelles

Lan, Jing; Huang, Xirong; Hu, Ming; Liu, Weifeng; Li, Yuezhong; Qu, Yinbo; Gao, Pin

doi:10.2478/s11532-007-0032-x

Cited by 5 publications

(1 citation statement)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As reported in case of peroxidases there is requirement of H 2 O 2 during catalysis (Lan et al 2007;Vyas and Molitoris 1995). Fungal Mn peroxidases have been reported to require a Mn dependent oxidation to produce hydrogen peroxide required as co-substrate during catalysis (Francisco et al 1999).…”

Section: Enzyme Assaysmentioning

confidence: 85%

Coordinate action of exiguobacterial oxidoreductive enzymes in biodegradation of reactive yellow 84A dye

et al. 2008

View full text Add to dashboard Cite

A novel bacterial species identified as Exiguobacterium sp. RD3 degraded the diazo dye reactive yellow 84A (50 mg l(-1)) within 48 h at static condition, at 30 degrees C and pH 7. Lower salinity conditions were found to be favorable for growth and decolorization. Enzymatic activities of an H(2)O(2) independent oxidase along with laccase and an azoreductase suggest their prominent role during the decolorization of reactive yellow 84A. Presence of an H(2)O(2) independent oxidase in Exiguobacterium sp. RD3 was confirmed and hydrogen peroxide produced was detected by a coupled iodometric assay. Azoreductase activity was prominent in presence of cofactors NADH and NADP in mineral salt medium. Considerable depletion of COD of the dye solution during degradation of dye was indicative of conversion of complex dye into simple oxidizable products. Products of degradation were analyzed by HPLC, FTIR and GCMS. A possible product of the degradation was identified by GCMS. Degradation of dye resulted with significant reduction of phytotoxicity, confirming the environmentally safe nature of the degradation metabolites.

show abstract

Section: Enzyme Assaysmentioning

confidence: 85%

Coordinate action of exiguobacterial oxidoreductive enzymes in biodegradation of reactive yellow 84A dye

et al. 2008

View full text Add to dashboard Cite

show abstract

Kinetic Study of Peroxidase‐Catalyzed Coupling of Benzene‐1,4‐diamine and N‐(2‐Aminoethyl)naphthalen‐1‐amine: Development of Micromolar Hydrogen Peroxide Reaction System

Shivakumar

Nagaraja

Aradhana

et al. 2010

Helvetica Chimica Acta

View full text Add to dashboard Cite

A novel chromogenic method to measure the peroxidase activity using para-phenylenediamine dihydrochloride (¼ benzene-1,4-diamine hydrochloride; PPDD) and N-(1-naphthyl)ethylenediamine dihydrochloride (¼ N-(2-aminoethyl)naphthalen-1-amine; NEDA) is presented. The PPDD entraps the free radical and gets oxidized to electrophilic diimine, which couples with NEDA to give an intense redcolored chromogenic species with maximum absorbance at 490 nm. This assay was adopted for the quantification of H 2 O 2 between 20 and 160 mm. Catalytic efficiency and catalytic power of the commercial peroxidase were found to be 4.47 Â 10 4 m À1 min À1 and 3.38 Â 10 À4 min À1, respectively. The catalytic constant (k cat ) and specificity constant (k cat /K m ) at saturated concentration of the co-substrates were 0.0245 Â 10 3 min À1 and 0.0445 mm À1 min À1, respectively. The chromogenic coupling reaction has a minimum interference from the reducing substances such as ascorbic acid, l-cystein, citric acid, and oxalic acid. The method being simple, rapid, precise, and sensitive, its applicability has been tested in the crude vegetable extracts that showed peroxidase activity.

show abstract

Ligninase-mediated transformation of 4,4′-dibromodiphenyl ether (BDE 15)

Feng

Mao

Chen

et al. 2013

Environ Sci Pollut Res

View full text Add to dashboard Cite

The structurally related hydroxylated polybrominated diphenyl ether (PBDE) like hydroxylated 4,4'-dibromodiphenyl ether widely occur in precipitation, surface water, and biotic media. The origins of hydroxylated PBDEs (OH-PBDEs) are of particular interest due to their greater toxic potencies than the corresponding PBDEs. We studied the transformation behavior and products of 4,4'-dibromodiphenyl ether (BDE 15) mediated by lignin peroxidase (LiP), an extracellular enzyme that is produced by certain white rot fungus and is widely present in the natural environment. We found that BDE 15 can be effectively transformed through the reaction mediated by LiP, and two different mono-OH-dibromodiphenyl ethers were identified by using gas chromatography-mass spectrometry (GC-MS) and GC-MS/MS. In particular, we compared the reaction behavior for systems variously containing natural organic matter (NOM) and/or veratryl alcohol (VA), a metabolite that certain fungus produces along with LiP in nature. It was found that the VA's enhancement effect on LiP performance was impaired by the presence of NOM. The findings in this study provide useful information for better understanding the origins of OH-PBDEs found in the environment.

show abstract

Mechanistic studies on the effect of veratryl alcohol on the lignin peroxidase catalyzed oxidation of pyrogallol red in reversed micelles

Cited by 5 publications

References 28 publications

Coordinate action of exiguobacterial oxidoreductive enzymes in biodegradation of reactive yellow 84A dye

Coordinate action of exiguobacterial oxidoreductive enzymes in biodegradation of reactive yellow 84A dye

Kinetic Study of Peroxidase‐Catalyzed Coupling of Benzene‐1,4‐diamine and N‐(2‐Aminoethyl)naphthalen‐1‐amine: Development of Micromolar Hydrogen Peroxide Reaction System

Ligninase-mediated transformation of 4,4′-dibromodiphenyl ether (BDE 15)

Contact Info

Product

Resources

About