RT Journal Article SR Electronic(1) A1 Yoshitake, Akifumi A1 Katayama, Yoshihiro A1 Nakamura, Masaya A1 Iimura, Yousuke A1 Kawai, Shinya A1 Morohoshi, NoriyukiYR 1993 T1 N-linked carbohydrate chains protect laccase III from proteolysis in Coriolus versicolor JF Microbiology, VO 139 IS 1 SP 179 OP 185 DO https://doi.org/10.1099/00221287-139-1-179 PB Microbiology Society, SN 1465-2080, AB The structure and function of the N-linked carbohydrate chains in laccase III, one of the ligninolytic glycoenzymes from the white-rot fungus Coriolus versicolor, have been partially characterized using endoglycosidases (Endo F and Endo H) and the N-asparagine-specific inhibitor, tunicamycin. In the presence of 10 μg tunicamycin ml−1 laccase and proteinase activities in culture filtrates of C. versicolor were measured over 3 weeks. Laccase activity was slightly decreased by the addition of tunicamycin, whereas proteinase activity was increased. The N-linked carbohydrate chains were not necessary for laccase secretion and activity. Endo-glycosidase digestion showed that laccase III contained at least four N-linked carbohydrate chains, of which two were high-mannose type or hybrid type and two were complex type. Judging from the differences in the resistance of the native and the carbohydrate-depleted laccase to proteolytic digestion and high temperature, the four N-linked carbohydrate chains have important protective functions against proteolytic attack and elevated temperature., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-139-1-179