Enzymatic catalysis of 2,6-dimethoxyphenol by laccases and products characterization in organic solutions

• 来源期刊: 中国科学B辑（英文版）
• 年，卷（期）: 2008,（7）
• 页码范围: 669-676
• 页数: 8页
• 语种: 英文
• DOI: 10.1007/s11426-008-0071-y

摘要

2,6-Dimethoxyphenol (DMP) as a substrate was widely used in determination of laccase activity. It is surprising, however, that its catalyzed oxidation products have not been completely determined until now. Studies were thus conducted on Rhus laccase (RL) and immobilized Rhus laccase (IRL)-catalyzed oxidation reactions of 2,6-dimethoxyphenol in water-organic solvent systems. These reactions pro-ceeded well in water-(im)miscible organic solvent systems pre-saturated with water. Only one product, 3,3',5,5'-tetramethoxy-1,1'biphenyl-4,4'-diol (TMBP), was produced by RL catalysis, and it was thor-oughly characterized by FT-IR, NMR, GC-MS, etc. A simple enzymatic mechanism of this reaction is proposed.