Purification and characterization of alpha-galactosidase from sunflower seeds
2003
Kim, W.D. | Kaneko, S. | Park, G.G. | Tanaka, H. | Kusakabe, I. | Kobayashi, H.
From 100 g sunflower seeds, 1.2 mg purified alpha-galactosidase was obtained with an overall yield of 51%. The alpha-galactosidase acted on both terminal alpha-galactosyl residues and side-chain alpha-galactosyl residues of the galactomanno-oligosaccharides and galactomannans. The cDNA coding for sunflower alpha-galactosidase was cloned and the deduced amino acid sequence revealed that the mature enzyme consisted of 363 amino acid residues with a molecular weight of 40 263. Seven cysteine residues were found but no putative N-glycosylation sites were present in the sequence. The deduced amino acid sequences of mature enzyme and a-galactosidases from coffee, guar and Mortierella vinacea a-galactosidase II showed over 81%, 77%, and 47% homology, respectively. These enzymes are classified into the third group in which the enzyme has no insertion sequence and a broad specificity on galactomanno-oligosaccharides compared to the other groups.
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