@article{mbs:/content/journal/micro/10.1099/00221287-139-1-179, author = "Yoshitake, Akifumi and Katayama, Yoshihiro and Nakamura, Masaya and Iimura, Yousuke and Kawai, Shinya and Morohoshi, Noriyuki", title = "N-linked carbohydrate chains protect laccase III from proteolysis in Coriolus versicolor", journal= "Microbiology", year = "1993", volume = "139", number = "1", pages = "179-185", doi = "https://doi.org/10.1099/00221287-139-1-179", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-139-1-179", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "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.", }