The structure and function of the -linked carbohydrate chains in laccase III, one of the ligninolytic glycoenzymes from the white-rot fungus , have been partially characterized using endoglycosidases (Endo F and Endo H) and the -asparagine-specific inhibitor, tunicamycin. In the presence of 10 μg tunicamycin ml laccase and proteinase activities in culture filtrates of were measured over 3 weeks. Laccase activity was slightly decreased by the addition of tunicamycin, whereas proteinase activity was increased. The -linked carbohydrate chains were not necessary for laccase secretion and activity. Endo-glycosidase digestion showed that laccase III contained at least four -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 -linked carbohydrate chains have important protective functions against proteolytic attack and elevated temperature.


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