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  • Title: Purification and some properties of alpha-galactosidase from Penicillium purpurogenum.
    Author: Shibuya H, Kobayashi H, Park GG, Komatsu Y, Sato T, Kaneko R, Nagasaki H, Yoshida S, Kasamo K, Kusakabe I.
    Journal: Biosci Biotechnol Biochem; 1995 Dec; 59(12):2333-5. PubMed ID: 8611759.
    Abstract:
    alpha-Galactosidase was purified by ion-exchange chromatographies on DEAE-cellulose and SE-cellulose columns from the culture filtrate of Penicillium purpurogenum No. 618. The final preparation was judged homogeneous by SDS-PAGE and its molecular mass and isoelectric point were estimated to be 67 kDa and 4.1, respectively. The N-terminal amino acid sequence of the enzyme was analyzed and aligned with those of other alpha-galactosidases. In addition, the enzyme acted on the stubbed alpha-galactosyl residue connected to the beta-1,4-manno-oligosaccharide chain, indicating that this specificity was quite different from that of Mortierella vinacea alpha-galactosidase.
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