[Isolation and properties of N-acetyl-beta-D-hexosaminidase from the fungus Hohenbuechelia serotina].

N-Acetyl-beta-D-hexosaminidase (EC 3.2.1.52) isolated from the fruit bodies of Hohenbuechelia serotina (Fr.) splits N-acyl-p-nitrophenyl-beta-D-glucosaminides acylated at the amino group of the aminosugar by fatty acids, substituted benzoic acids and some amino acids and peptides. The enzyme was purified about 210-fold by chromatography on CM-Sephadex C-50 and DEAE--Sephadex A-50 and by gel filtration of Sephadex G-200 with a yield of 4%. The enzyme had pI 6,6. Some properties of the enzyme, pH-optimum, thermal stability and substrate specificity were studied. The Michaelis constants for some p-nitrophenyl-beta-D-glucosaminides were were calculated. p-Nitrophenyl N-acetyl-beta-D-glucosaminides were calculated. p-Nitrophenyl N-acetyl-beta-D-glucosaminide and D-galactosaminide at concentrations more than 0,3 mM inhibited the enzyme.