Demethoxylation of Milled Wood Lignin and Lignin Related Compounds by Laccase from White-rot Fungus, Cerrena unicolor

  • Leonowicz, A. (Department of Biochemistry, Maria Curie-Sklodowska University) ;
  • Rogalski, J. (Department of Biochemistry, Maria Curie-Sklodowska University) ;
  • Malarczyk, E. (Department of Biochemistry, Maria Curie-Sklodowska University) ;
  • Grzywnowicz, K. (Department of Biochemistry, Maria Curie-Sklodowska University) ;
  • Ginalska, G. (Department of Biochemistry, Maria Curie-Sklodowska University) ;
  • Lobarzewski, J. (Department of Biochemistry, Maria Curie-Sklodowska University) ;
  • Ohga, S. (Department of Forest Resources Sciences, College of Agriculture, Kyushu University) ;
  • Pashenova, N. (Institute of Forest, Russian Academy of Science) ;
  • Lee, S.S. (Department of Biological Education, Korea National University of Education) ;
  • Cho, Nam-Seok (School of Forest Resources, Chungbuk National University)
  • 투고 : 2000.10.04
  • 심사 : 2000.12.11
  • 발행 : 2000.12.30

초록

Highly purified Cerrena unicolor laccase (benzenediol:oxygen oxidoreductase, EC 1.10.3.2) caused the demethoxylation of milled wood lignin and several lignin related substances. The constitutive form of the enzyme produced extracellularly by C. unicolor fermenter culture was isolated and purified by ion-exchange chromatography on the DEAE-Toyopearl column and by affinity chromatography on a ConA-Sepharose and Syringyl-AH-Sepharose 4B columns. The enzyme was further immobilized on functionalized porous glass (CPG) and keratin coated CPG. The demethylating activity was monitored both by estimation of released methanol and by detection of the level of methoxyl groups (also in some water miscible solvents) after incubation of lignin materials with laccase preparations (free and immobilized). The effects of the incubation time and temperature on the demethoxylating activity of immobilized laccase preparations were also studied.

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