Glycosidases induced in Aspergillus tamarii. Secreted alpha-D-galactosidase and beta-D-mannanase.
An alpha-D-galactosidase (EC 3.2.1.22) and a beta-D-mannanase (EC 3.2.1.78), which were secreted into the growth medium when Aspergillus tamarii was cultivated in the presence of galactomannan, were purified by a procedure including chromatography on hydroxyapatite and DEAE-cellulose columns. Each of these enzymes showed a single protein band, corresponding to their respective activities, on polyacrylamide-gel electrophoresis. Both enzymes were shown to be glycoproteins containing N-acetylglucosamine, mannose and galactose, with molar proportions of 1:6:1.5 for alpha-D-galactosidase and 1:13:8 for beta-D-mannanase. Mr values as determined by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate and by the electrophoretic method of Hedrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164] were 56000 and 53000 respectively. The alpha-D-galactosidase differed markedly from the mycelial forms I and II studied in the preceding paper [Civas, Eberhard, Le Dizet & Petek (1984) Biochem. J. 219, 849-855] with regard to both its kinetic and structural properties.
D001230:Aspergillus / Q000201:enzymology*; D002412:Cations / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000096:biosynthesis*; D008361:Mannosidases / Q000096:biosynthesis* / Q000097:blood* / Q000302:isolation & purification; D008970:Molecular Weight; D013379:Substrate Specificity; D000519:alpha-Galactosidase / Q000096:biosynthesis* / Q000302:isolation & purification; D044902:beta-Mannosidase
D002412:Cations; D005696:Galactosidases; D008361:Mannosidases; D000519:alpha-Galactosidase; D044902:beta-Mannosidase; C041867:endo-1,4-beta-D-mannanase