Purification and Biochemical Characterization of Cell Wall-bound Trehalase from Pericarp Tissues of Actinidia deliciosa

DOI NDL Digital Collections Web Site Web Site 27 References
  • Li Xing-Jun
    Graduate School of Biosphere Sciences, Hiroshima University
  • Nakagawa Naoki
    Graduate School of Biosphere Sciences, Hiroshima University
  • Sakurai Naoki
    Graduate School of Biosphere Sciences, Hiroshima University

Bibliographic Information

Other Title
  • キウイ（<i>Actinidia deliciosa</i>）果肉細胞壁に結合しているトレハラーゼの精製と生化学的性質

Search this article

Description

A trehalase (EC 3.2.1.28) was purified from the cell walls of Actinidia deliciosa fruit. The purified trehalase had optimal pH of around 5, Km of 0.25 mM and Vmax of 5667 pkat/mg protein, and was relatively heat stable. The enzyme showed highly specific activity to trehalose and weak activity to maltose and maltotriose, but did not hydrolyze any other disaccharides. Trehalase activity was unaffected by Ca2+, Na+, K+, Li+, Mn2+, Co2+, and Mg2+ ions and EDTA, but markedly inhibited by Hg2+ and Fe3+ ions, iodoacetic acid, tris(hydroxymethyl)aminomethane (Tris), p-chloromercuribenzoate (PCMB), glucose and glucosamine. This cell wall-bound enzyme seems to degrade apoplastic trehalose. Another possibility is that this trehalase has additional functions such as defence against insects.<br>

Journal

References(27)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top