1887

Abstract

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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/content/journal/micro/10.1099/00221287-139-1-179
1993-01-01
2019-11-17
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-139-1-179
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