Purification and some properties of alpha-L-fucosidase isolated from Streptococcus sanguis.
alpha-L-Fucosidase acting on naturally occurring substrates was highly purified from the growth culture of Streptococcus sanguis ATCC 10557. The molecular weight of the enzyme was approximately 120,000 and the optimal pH was at 5.5. The purified enzyme showed specificity toward the linkage of alpha-(1 leads to 2) fucosides in oligosaccharides and glycoproteins. The enzyme released L-fucose from glycoprotein in human parotid saliva.
D002849:Chromatography, Gas; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004589:Electrophoresis, Disc; D006023:Glycoproteins / Q000378:metabolism; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009844:Oligosaccharides / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000378:metabolism; D013298:Streptococcus sanguis / Q000201:enzymology*; D013379:Substrate Specificity; D005644:alpha-L-Fucosidase / Q000302:isolation & purification* / Q000378:metabolism
D006023:Glycoproteins; D009844:Oligosaccharides; D012471:Salivary Proteins and Peptides; D005644:alpha-L-Fucosidase