Mediator role of veratryl alcohol in the lignin peroxidase-catalyzed oxidative decolorization of Remazol Brilliant Blue R

• Published in: Enzyme and microbial technology Vol. 36; no. 2; pp. 327 - 332
• Main Authors: Christian, Viral, Shrivastava, Rohit, Shukla, Dharmendra, Modi, Hasmukh, Vyas, Bharatkumar Rajiv Manuel
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01.02.2005; Elsevier Science
• Subjects: Biological and medical sciences; Biotechnology; Decolorization; Fundamental and applied biological sciences. Psychology; Trametes versicolor; Veratryl alcohol; Decolorization; Veratryl alcohol; Trametes versicolor; Fungi; Discoloration; Peroxidases; Enzyme; Coriolus versicolor; Basidiomycetes; Oxidoreductases; Thallophyta; Diarylpropane peroxidase
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/j.enzmictec.2004.09.006

Lignin peroxidase (LiP) produced by Trametes versicolor decolorizes Remazol Brilliant Blue R (RBBR) in the presence as well as in the absence of veratryl alcohol (VA). VA enhances and stabilizes the RBBR-decolorization rates by lignin peroxidase. RBBR has better substrate reactivity than VA for LiP. RBBR is also decolorized directly by LiP and competitively inhibits VA oxidation by LiP. In the presence of higher concentrations of RBBR (i) RBBR decolorization rates improve, (ii) veratryl aldehyde appears after a lag and (iii) VA oxidation rates decrease. The lag is due to consumption of VA cation radical (VA +) generated upon LiP-catalyzed VA oxidation, during RBBR oxidation. That may result in the formation of compound III in the absence of VA + and contributes to the inhibitory influence of RBBR on LiP activity.