Abstract
From 100 g sunflower seeds, 1.2 mg purified α-galactosidase was obtained with an overall yield of 51%. The α-galactosidase acted on both terminal α-galactosyl residues and side-chain α-galactosyl residues of the galactomanno-oligosaccharides and galactomannans. The cDNA coding for sunflower α-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 α-galactosidases from coffee, guar and Mortierella vinacea α-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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Kim, WD., Kaneko, S., Park, GG. et al. Purification and characterization of α-galactosidase from sunflower seeds. Biotechnology Letters 25, 353–358 (2003). https://doi.org/10.1023/A:1022337012865
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DOI: https://doi.org/10.1023/A:1022337012865