Purification and Some Properties of Pectate Lyase from Alkaliphilic Nocardiopsis sp. TOA-1.

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  • Mitsuiki Shinji
    Department of Industrial Chemistry, Faculty of Engineering, Kyushu Sangyo University Division of Bioresource and Bioenvironmental Sciences,Department of Bioscience and Biotechnology, Kyushu University
  • Eguchi Hiroyoshi
    Department of Industrial Chemistry, Faculty of Engineering, Kyushu Sangyo University
  • Hara Yoko
    Department of Industrial Chemistry, Faculty of Engineering, Kyushu Sangyo University
  • Sakai Masashi
    Department of Industrial Chemistry, Faculty of Engineering, Kyushu Sangyo University
  • Moriyama Yasushi
    Fundamental Research Center, TOTO Ltd.
  • Goto Masatoshi
    Division of Bioresource and Bioenvironmental Sciences,Department of Bioscience and Biotechnology, Kyushu University
  • Furukawa Kensuke
    Division of Bioresource and Bioenvironmental Sciences,Department of Bioscience and Biotechnology, Kyushu University

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Other Title
  • 好アルカリ性Nocardiopsis　sp.TOA-1株の生産するペクチン酸リアーゼの精製と諸性質

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Abstract

An extracellular pectate lyase of alkaliphilic Nocardiopsis sp. TOA-l, designated NPLase, was purified to homogeneity. The molecular mass of NPLase was estimated to be 54 kDa. Highest ac-tivity of this enzyme was obtained at pH 10.0 and 40°C and the isoelectric point (p1) was 4.7. NPLase was an endo type pectate lyase which degrades polygalacturonic acid in a random manner.

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