Glycoprotein nature of tannase in Aspergillus niger.
1. Tannase (tannin acyl-hydrolase, EC 3.1.1.20) was isolated from the culture medium of Aspergillus niger and purified about 200-fold. On polyacrylamide-gel electrophoresis it gave a single band. 2. The molecular weight of the enzyme was of the order of 55 000 as determined by gel filtration. The enzyme contains 21.5% of carbohydrates (mannose and glucose). 3. Treatment of tannase with alkaline borohydride decreased the content of threonine, serine and mannose, suggesting that the carbohydrate-peptide linkage is of the O-glycoside type, involving mannose linked to threonine and serine.
D001230:Aspergillus / Q000201:enzymology*; D001234:Aspergillus niger / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000032:analysis* / Q000302:isolation & purification; D002854:Chromatography, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis*; D008358:Mannose / Q000032:analysis; D008970:Molecular Weight; D013634:Tannins
D005656:Fungal Proteins; D006023:Glycoproteins; D013634:Tannins; D002265:Carboxylic Ester Hydrolases; C022711:tannase; D008358:Mannose