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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/25193


    Title: Purification and properties of an insecticidal metalloprotease produced by Photorhabdus luminescens strain 0805-P5G, the entomopathogenic nematode symbiont
    Authors: 張佑慈;Chang, Yu-Tzu;張竣維;Hebron, C.Chang
    Contributors: 生物科技學系
    Date: 2013
    Issue Date: 2013-07-11 13:55:08 (UTC+8)
    Abstract: A total of 13 Photorhabdus luminescens strains were screened for proteolytic activity. The P. luminescens strain 0805-P5G had the highest activity on both skim milk and gelatin plates. The protease was purified to electrophoretical homogeneity by using a two-step column chromatographic procedure. It had a molecular weight of 51.8 kDa, as determined by MALDI-TOF mass spectrometry. The optimum pH, temperature, as well as pH and thermal stabilities were 8, 60 °C, 5-10, and 14-60 °C, respectively. It was completely inhibited by EDTA and 1,10-phenanthroline. Bioassay of the purified protease against Galleria mellonella by injection showed high insecticidal activity. The protease also showed high oral toxicity to the diamondback moth (Plutella xylostella) of a Taiwan field-collected strain, but low toxicity to an American strain. To our knowledge, this is the first report to demonstrate that the purified protease of P. luminescens has direct toxicity to P. xylostella and biopesticide potentiality.
    Relation: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2013, 14(1):308-321
    Appears in Collections:[生物科技學系] 期刊論文

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