Purification, Characterization, and Overexpression of Thermophilic Pectate Lyase of<i>Bacillus</i>sp. RN1 Isolated from a Hot Spring in Thailand

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  • SUKHUMSIIRCHART Wasana
    Department of Biochemistry, Faculty of Medicine, Srinakharinwirot University
  • KAWANISHI Sakiko
    Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University
  • DEESUKON Warin
    Department of Biochemistry, Faculty of Medicine, Srinakharinwirot University
  • CHANSIRI Kosum
    Department of Biochemistry, Faculty of Medicine, Srinakharinwirot University
  • KAWASAKI Haruhiko
    Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University
  • SAKAMOTO Tatsuji
    Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University

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  • Purification, Characterization, and Overexpression of Thermophilic Pectate Lyase of Bacillus sp. RN1 Isolated from a Hot Spring in Thailand

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A thermophilic pectate lyase, Pel SWU, was isolated from a culture filtrate of Bacillus sp. RN1 isolated from a hot spring in Ranong Province, Thailand. The enzyme was purified to homogeneity using cation-exchange and hydrophobic column chromatographies. The molecular mass of Pel SWU was estimated to be 33 kDa. The specific substrate was demethylated galacturonic acid. The enzyme was stable at pH 4.0–10.0 and at temperatures up to 70 °C in the presence of calcium and polygalacturonic acid (PGA). The optimum pH and temperature were 10.0 and 90 °C. The pel gene encoding Pel SWU was 1,023 bp, which corresponds to 341 amino acids. The properties of the recombinant enzyme was similar to those of Bacillus Pel SWU. Unsaturated di- and trigalacturonic acids were formed mainly as the final products of degradation by Pel SWU, as revealed by high-performance anion-exchange chromatography (HPAEC) and electrospray ionization mass spectrometry (ESI-MS) analyses. This thermophilic pectate lyase should be useful in the degradation of pectin networks at high temperature.

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