Purification and Characterization of Soluble and Cell Wall-bound Acid .ALPHA.-Glucosidases of Ripe Yellow Banana Pulp.

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  • Konishi Yotaro
    Department of Food Science and Nutrition, Faculty of Human Life Science, Osaka City University
  • Harada Mia
    Department of Food Science and Nutrition, Faculty of Human Life Science, Osaka City University
  • Nakasuji Mie
    Department of Food Science and Nutrition, Faculty of Human Life Science, Osaka City University
  • D'Innocenzo Marisa
    Faculdade de Ciencias Farmaceuticas, Universidade de Sao Paulo
  • Lajolo Franco M.
    Faculdade de Ciencias Farmaceuticas, Universidade de Sao Paulo

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Other Title
  • バナナ果肉の可溶性および細胞壁結合型酸性α-グルコシダーゼの精製と性質
  • Purification and Characterization of Soluble and Cell Wall-bound Acid α-Glucosidases of Ripe Yellow Banana Pulp
  • Purification and Characterization of Soluble and Cell Wall bound Acid アルファ Glucosidases of Ripe Yellow Banana Pulp

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Abstract

Banana pulp, irrespective of the degree of ripening, contained soluble and cell wall-bound forms of acid α-glucosidases (SAAG and BAAG). BAAG was released with a neutral buffer containing 0.2-2 M NaCI after extracting of SAAG with a salt-free buffer. From the same bunch of ripe yellow bananas, SAAG and BAAG were purified at 732-fold and 264-fold, respectively, using ConASepharose and Sephadex G-150 gel column chromatographies. The molecular weights of SAAG and BAAG were 70, 000 and 90, 000, respectively, by gel filtration. These enzymes were typical maltases that required maltose (G2) and malto-oligosaccharides (G3-G7) as substrates, but not isomaltose, treharose, sucrose, pullulan, glycogen, or soluble starch. The Vmax/Km ratios (apparent hydrolytic efficiencies) of SAAG and BAAG toward G5-G7 were 89-112 and 14-52%, respectively, with the ratio toward maltose being 100%. As for ripe yellow banana where cell wall or amy loplastic membrane has not been maintained, it is speculated that BAAG could access starch and its hydrolytic products and would share in starch degradation in collaboration with amylases and SAAG.

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