Please use this identifier to cite or link to this item: http://www.repositorio.ufc.br/handle/riufc/59036
Title in Portuguese: A novel peroxidase purified from Marsdenia megalantha latex inhibits phytopathogenic fungi mediated by cell membrane permeabilization
Author: Oliveira, Henrique P.
Silva, Rodolpho G. G
Oliveira, Jose T. A.
Sousa, Daniele O. B.
Pereira, Mirella L.
Souza, Pedro F. N.
Soares, Arlete A.
Gomes, Valdirene M.
Monteiro-Moreira, Ana C. O.
Moreno, Frederico B. M. B.
Vasconcelos, Ilka M.
Keywords: Marsdenia megalantha
Latex
Peroxidase
Antifungal protein
Fusarium
Protein defense
Issue Date: 2017
Citation: OLIVEIRA, Henrique P. et al. A novel peroxidase purified from Marsdenia megalantha latex inhibits phytopathogenic fungi mediated by cell membrane permeabilization. International Journal of Biological Macromolecules, [s.l.], v. 96, p. 743-753, 2017.
Abstract: An antifungal class III peroxidase was purified from Marsdenia megalantha latex (named Mo-POX) using DEAE-cellulose and gel filtration chromatography on a Superose 12 HR 10/30 column. Mm-POX has an apparent molecular mass of 67.0 kDa and a pI of 5.2, shares identity with other peroxidases, and fol lows Michaelis-Menten kinetics. It has a high affinity for guaiacol and hydrogen peroxide. The pH and temperature optima for Mm-POX were 5.0–7.0 and 60 ◦C, respectively. The catalytic activity of Mm-POX was decreased in the presence of classic peroxidase inhibitors including azide, dithiothreitol, ethylene diamine tetraacetic acid, and sodium metabisulfite and high concentrations of Na+, Mn+, and salicylic acid. In contrast, Ca+ and Mg+, even at low concentrations, enhanced the Mm-POX enzymatic activity. This protein inhibited the germination of the conidia of the phytopathogenic fungi Fusarium oxysporum and Fusarium solani by acting through a membrane permeabilization mechanism. Mm-POX also induced oxidative stress in F. solani. Mm-POX is the first enzyme to be isolated from the M. megalantha species and it has potential use in the control of plant disease caused by important phytopathogenic fungi. This adds biotechnological value to this enzyme.
URI: http://www.repositorio.ufc.br/handle/riufc/59036
metadata.dc.type: Artigo de Periódico
ISSN: 0141-8130
Appears in Collections:DBIO - Artigos publicados em revista científica

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