-Acetylglucosaminidase was induced by either -acetylglucosamine or -acetylmannosamine in several strains of Enzyme activity was not induced in a -acetylglucosamine non-utilizing mutant which is unable to express the first three steps in the -acetylglucosamine catabolic pathway. The enzyme, purified 500-fold, had a specific activity of 36.8 units (mg protein) and catalysed the hydrolysis of -nitrophenyl-β--acetylglucosamine, -diacetylchitobiose and -triacetylchitotriose. No activity was observed toward colloidal chitin, hyaluronic acid or mucin. The cellular distribution of -acetylglucosaminidase was determined by measuring enzyme activity before and after acid treatment of intact cells. -Acetylglucosaminidase (80-88% of the total cellular activity) was rapidly secreted to the periplasm when the enzyme was induced either during yeast growth at 28 °C or germ-tube formation at 37 °C. Export of the enzyme from the periplasm into the medium was fourfold greater during germ-tube formation, and after 6 h incubation the amount of enzyme released into the medium represented 70% of cell-associated enzyme activity.


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