Evidence for formation of the veratryl alcohol cation radical by lignin peroxidase

Biochemistry ◽  
1995 ◽  
Vol 34 (18) ◽  
pp. 6020-6025 ◽  
Author(s):  
Aditya Khindaria ◽  
Thomas A. Grover ◽  
Steven D. Aust
Keyword(s):  
Lignin Peroxidase ◽  
Cation Radical ◽  
Veratryl Alcohol

scholarly journals Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant

2018 ◽  
Vol 293 (13) ◽  
pp. 4702-4712 ◽  
Author(s):  
Carl J. Houtman ◽  
Eranda Maligaspe ◽  
Christopher G. Hunt ◽  
Elena Fernández-Fueyo ◽  
Angel T. Martínez ◽  
...  
Keyword(s):  
Lignin Peroxidase ◽  
Cation Radical ◽  
Veratryl Alcohol

Stabilization of the Veratryl Alcohol Cation Radical by Lignin Peroxidase†

Biochemistry ◽  
1996 ◽  
Vol 35 (20) ◽  
pp. 6418-6424 ◽  
Author(s):  
Aditya Khindaria ◽  
Isao Yamazaki ◽  
Steven D. Aust
Keyword(s):  
Lignin Peroxidase ◽  
Cation Radical ◽  
Veratryl Alcohol

Detection and Characterization of the Lignin Peroxidase Compound II−Veratryl Alcohol Cation Radical Complex†

Biochemistry ◽  
1997 ◽  
Vol 36 (46) ◽  
pp. 14181-14185 ◽  
Author(s):  
Aditya Khindaria ◽  
Guojun Nie ◽  
Steven D. Aust
Keyword(s):  
Lignin Peroxidase ◽  
Cation Radical ◽  
Veratryl Alcohol ◽  
Radical Complex ◽  
Compound Ii

Kinetic and Thermodynamic Characterization of Lignin Peroxidase Isolated from Agaricus bitorqus A66

2012 ◽  
Vol 10 (1) ◽  
Author(s):  
Ismat Bibi ◽  
Haq Nawaz Bhatti
Keyword(s):  
Lignin Peroxidase ◽  
Thermal Inactivation ◽  
Specific Activity ◽  
Gel Filtration ◽  
Veratryl Alcohol ◽  
Exchange Chromatography ◽  
Different Temperatures ◽  
Scale Experiment ◽  
Menten Kinetic

This study deals with purification and characterization of lignin peroxidase (LiP) isolated from Agaricus bitorqus A66 during decolorization of NOVASOL Direct Black dye. A laboratory scale experiment was conducted for maximum LiP production under optimal conditions. Purification & fractionation of LiP was performed on DEAE-Sepharose ion exchange chromatography followed by Sephadex G-50 gel filtration. The purified LiP has a specific activity of 519 U/mg with 6.73% activity recover. The optimum pH and temperature of purified LiP for the oxidation of veratryl alcohol were 6.8 and 45 °C, respectively. Michaelis-Menten kinetic constants (Vmax and Km) were determined using different concentrations of veratryl alcohol (1-35 mM). The Km and Vmax were 16.67 mM and 179.2 U/mL respectively, for veratryl alcohol oxidation as determined from the Lineweaver-Burk plot. Thermal inactivation studies were carried out at different temperatures to check the thermal stability of the enzyme. Enthalpy of activation decreased where Free energy of activation for thermal denaturation increased at higher temperatures. A possible explanation for the thermal inactivation of LiP at higher temperatures is also discussed.

scholarly journals Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta

2021 ◽  
Vol 7 (9) ◽  
pp. 762
Author(s):  
Jina Baik ◽  
Anwesha Purkayastha ◽  
Kyung Hye Park ◽  
Taek Jin Kang
Keyword(s):  
Lignin Peroxidase ◽  
Functional Characterization ◽  
Veratryl Alcohol ◽  
Storage Conditions ◽  
Versatile Peroxidase ◽  
Bjerkandera Adusta ◽  
Cellular Mechanisms ◽  
Melanin Pigmentation ◽  
Crude Enzyme Preparation

Melanin pigmentation in the human skin results from complicated cellular mechanisms that remain to be entirely understood. Uneven melanin pigmentation has been counteracted by inhibiting synthesis or transfer of melanin in the skin. Recently, an enzymatic approach has been proposed, wherein the melanin in the skin is decolorized using lignin peroxidase. However, not many enzymes are available for decolorizing melanin; the most studied one is lignin peroxidase derived from a lignin degrading fungus, Phanerochaete chrysosporium. Our current study reveals that versatile peroxidase from Bjerkandera adusta can decolorize synthetic melanin. Melanin decolorization was found to be dependent on veratryl alcohol and hydrogen peroxide, but not on Mn2+. The degree of decolorization reached over 40% in 10 min at 37 °C and a pH of 4.5. Optimized storage conditions were slightly different from those for the reaction; crude enzyme preparation was the most stable at 25 °C at pH 5.5. Since the enzyme rapidly lost its activity at 50 °C, stabilizers were screened. As a result, glycerol, a major component in several cosmetic formulations, was found to be a promising excipient. Our results suggest that B. adusta versatile peroxidase can be considered for future cosmetic applications aimed at melanin decolorization.

scholarly journals Veratryl alcohol-mediated oxidation of isoeugenyl acetate by lignin peroxidase

2001 ◽  
Vol 265 (3) ◽  
pp. 1008-1014 ◽  
Author(s):  
Rimko Ten Have ◽  
Robbert G. De Thouars ◽  
Henk J. Swarts ◽  
Jim A. Field
Keyword(s):  
Lignin Peroxidase ◽  
Veratryl Alcohol ◽  
Mediated Oxidation
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