Purification and physical properties of sweet-almond α-galactosidase

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Abstract
[alpha]-Galactosidase from sweet almonds was purified about 2000-fold through 8 steps. 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. A molecular weight of about 33000 was determined from the gel-filtration data. The ultraviolet-absorption spectrum and thermal inactivation of the enzyme are described. The purified enzyme hydrolyzed p-nitrophenyl [plus or minus]-[alpha]-galactoside at a much faster rate than melibiose. The pH optimum was at 5.5-5.7. Besides hydrolysis, it also catalyzed transfer of galactosyl residues, chain elongation of melibiose and the synthesis of oligosaccharides from galactose.