Purification of peroxidase from the medicinal herb Andrographis paniculata causing fungal hyphal distortion

• Autorzy: Ghosh M.

Warianty tytułu

PL

Oczyszczanie peroksydazy z leczniczej rośliny Andrographis paniculata, powodującej zniekształcenia strzępek grzybni

• Języki publikacji: EN

Abstrakty

EN

Peroxidases are ubiquitous in plants and their pattern of expression depends on tissue, development stage and environmental stimuli. They are involved in numerous physiological functions, including defense against pathogens and insect pests. The present study was conducted to isolate and purify a constitutive leaf peroxidase from the medicinal herb, Andrographis paniculata. The enzyme was purified through a series of purification steps and a 35kDa peroxidase was purified to homogeneity with pI value of 6.0. In vitro hyphal extension inhibition assay against the forest pathogen Trichosporium vesiculosum revealed significant morphological distortion of the protein treated hyphae.

PL

Peroksydazy są wszechobecne w roślinach. Forma ich ekspresji zależy od tkanki, stadium rozwojowego i wpływu środowiska. Są one związane z licznymi funkcjami fizjologicznymi, w tym z obroną przed patogenami i szkodnikami. Celem przedstawionej pracy było wyizolowanie i oczyszczenie peroksydazy z liści rośliny leczniczej Andrographis paniculata. Enzym był oczyszczany wieloetapowo i peroksydaza 35 kDa była oczyszczona jako jednorodna przy pI=6,0. W doświadczeniach prowadzonych in vitro metodą zahamowania wzrostu grzybni Trichosporium vesiculosum (patogen leśny) wykazano istotne zniekształcenia białek badanej grzybni.

• Wydawca: -
• Czasopismo: Herba Polonica
• Rocznik: 2010
• Tom: 56
• Numer: 2
• Opis fizyczny: p.69-78,fig.,ref.

Twórcy

autor

Ghosh M.

• Division of Plant Biotechnology, Institute of Forest Genetics and Tree Breeding, Forest Campus, R.S.Puram, Coimbatore - 641 002, India

Bibliografia

• 1. Moerschbacher BM. Plant peroxidases: involvement in response to pathogens. In: Penel C, Gaspar T, Greppin H eds. Plant Peroxidases 1980–1990, Topics and Detailed Literature on Molecular, Biochemical and Physiological Aspects. Universite´ de Gene`ve, Geneva, Switzerland, 1992: 91–99.
• 2. Kristensen BK, Bloch H, Rasmussen SK. Barley coleoptile peroxidases. Purification, molecular cloning and induction by pathogens. Plant Physiol 1999; 120:501-12.
• 3. Yang Y, Anderson EJ. Antimicrobial activity of a porcine myeloperoxidase against plant pathogenicbacteria and fungi. J Appl Microbiol 1999; 86:211-20.
• 4. Joseph LM, Koo TT, Man WS. Antifungal effects of hydrogen peroxide and peroxidase on spore germination and mycelial growth of Pseudocercospora species. Can J Bot 1998; 76: 2119 –24.
• 5. Caruso C, Chilosi G, Leonardi L, Bertini L, Margo P, Buonocore V, Caporale C. A basic peroxidase from wheat kernel with antifungal activity. Phytochemistry 2001; 58:743-50.
• 6. Ye XY, Ng TB. Isolation of novel peroxidase from french bean legumes and first demonstration of antifungal activity of a non-milk peroxidase. Life Sci 2002; 71:1667-80.
• 7. Ghosh M. Antifungal Properties of Haem Peroxidase from Acorus calamus. Ann Bot 2006; 98:1145-53.
• 8. Bradford MM. A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Analytical Biochem 1976; 72:248-54.
• 9. Imberty A, Goldberg R, Catesson AM. Tetramethyl benzidine and p-phenylenediamine pyrocatechol for peroxidase histochemistry and biochemistry: two new, non-carcinogenic chromogens for investigating lignification process. Plant Sci Lett 1984; 35:103-8.
• 10. Lamb C, Dixon RA. The oxidative burst in plant disease resistance. Annu Rev Plant Physiol Plant Mol Biol 1997; 48:251-75.
• 11. Maksimov IV, Cherepanova EA, Khairullin RM. Chitin-Specific peroxidases in plants. Biochemistry 2003; 68:111-15.
• 12. Maksimov IV, Cherepanova EA, Iarullina LG, Akhmetova IE. Isolation of chitin-specific wheat oxidoreductases. Prikl Biokhim Mikrobiol 2005; 41:616-20.
• 13. Akhunov AA, Golubenko Z, Beresneva YV, Khashimova NA, Ibragimov FA, Abdurashidova NA, Mustakimova EC, Stipanovic RD. Participation of Chitin Specific Isoforms of Peroxidase in Protective Reaction of Plants Infected by Pathogens. In: Proceedings of the 3rd Moscow International Congress onBiotechnology: State of the Art and Prospects of Development; Moscow. 2005a: 225.
• 14. Akhunov AA, Golubenko Z, Abdurashidova NA, Ibragimov FA, Beresneva YV, Khashimova NR, Mustakimova EC, Akbarova GO, Bokov AF, Stipanovic RD. Role of Peroxidase in Resistance of Malvaceae to Verticillium Dahliae. In : Proceedings of the 6th International Symposium on the Chemistry of Natural Compounds; Ankara, Turkey. 2005b:154.
• 15. Martinez C, Montillet JL, Bresson E, Agnel JP, Dai GH, Daniel JF, Geiger JP, Nicole M. Apoplastic peroxidase generates superoxide anions in cells of cotton cotyledons undergoing the hypersensitive reaction to Xanthomonas campestris pv. malvacearum Race 18. Mol Plant Microbe Int 1998; 11:1038-47.
• 16. Bestwick CS, Brown IR, Mansfield JW. Localized changes in peroxidase activity accompany hydrogen peroxide generation during the development of a nonhost hypersensitive Reaction in Lettuce. Plant Physiol 1998; 118:1067-78.
• 17. Fossdal CG, Sharma P, Lonneborg A. Isolation of the first putative peroxidase cDNA from a conifer and the local and systemic accumulation of related proteins upon pathogen infection. Plant Mol Biol 2001; 47:423-35.
• 18. Zou J, Rodriguez-Zas S, Aldea M, Li M, Zhu J, Gonzalez DO, Vodkin LO, DeLucia E, Clough SJ. Expression profiling soybean response to Pseudomonas syringae reveals new defense-related genes and rapid HRspecific down regulation of Photosynthesis. Mol Plant Microbe Int 2005; 18: 1161-74.

Uwagi

rekord w opracowaniu