Purification and physical properties of sweet-almond alpha-galactosidase.
1. alpha-Galactosidase from sweet almonds was purified about 2000-fold through eight steps. 2. The enzyme preparation was free from other related enzymes known to occur in sweet almonds, and behaved as a homogeneous protein on filtration through Sephadex G-75. 3. A molecular weight of about 33000 was determined from the gel-filtration data. 4. The ultraviolet-absorption spectrum and thermal inactivation of the enzyme are described. 5. The purified enzyme hydrolysed p-nitrophenyl alpha-d-galactoside at a much faster rate than melibiose. 6. The pH optimum was at 5.5-5.7. 7. Besides hydrolysis, it also catalysed transfer of galactosyl residues, chain elongation of melibiose and the synthesis of oligosaccharides from galactose.
D002021:Buffers; D002498:Centrifugation; D011232:Chemical Precipitation; D002845:Chromatography; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D004187:Disaccharides / Q000032:analysis; D005690:Galactose; D005696:Galactosidases / Q000032:analysis*; D005947:Glucose; D006027:Glycosides / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009754:Nuts; D009844:Oligosaccharides / Q000096:biosynthesis; D010783:Photometry; D012995:Solubility; D013053:Spectrophotometry; D013696:Temperature
D002021:Buffers; D004187:Disaccharides; D006027:Glycosides; D009844:Oligosaccharides; D005696:Galactosidases; D005947:Glucose; D005690:Galactose