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A peroxidase purified from cowpea roots possesses high thermal stability and displays antifungal activity against Colletotrichum gloeosporioides and Fusarium oxysporum.

Authors :
Silva, Fredy A.
Albuquerque, Louise M.
Martins, Thiago F.
de Freitas, Jonnanthan A.
Vasconcelos, Ilka M.
Queiroz de Freitas, David
Moreno, Frederico B.M.B.
Monteiro-Moreira, Ana C.O.
Oliveira, Jose T.A.
Source :
Biocatalysis & Agricultural Biotechnology; Jul2022, Vol. 42, pN.PAG-N.PAG, 1p
Publication Year :
2022

Abstract

Plants encode specific class III peroxidases (POX) as large multigene families that are involved in lignification, cell elongation, stress defense, and seed germination. However, many functions associated with these plant enzymes are not fully understood. Here, a class III peroxidase (Vu-RPOX) was purified from cowpea (Vigna unguiculata) roots with 0–90% ammonium sulfate precipitation, chitin column and Resource Q anion-exchange chromatography. Vu-RPOX is a glycoprotein composed by a 58 kDa polypeptide chain and pI of 3.79. Two peptide sequences of Vu-RPOX (RGLDVVNDIKT and RCSTFINRL) generated by Nano ESI-Q-TOF MS/MS analysis showed variable identity with seed coat peroxidase of Glycine max , peroxidase E5 of Vigna radiata , hypothetical peroxidase of Phaseolus vulgaris , and peroxidase E5-like of Vigna unguiculata. Vu-RPOX follows the Michaelis-Menten kinetics, optimal activity at pH 6.0, and was high thermo-stable when incubated up to 75 °C for 90 min. The catalytic activity of Vu-RPOX decreased in the presence of the classic peroxidase inhibitors, but was not inhibited by MgCl 2 , NH 4 Cl, MnCl 2 , CaCl 2 , and NaCl. Vu-RPOX delay the vegetative growth of the phytopathogenic fungi Colletrotrichum gloeosporioides and Fusarium oxysporum. Based on its properties Vu-RPOX is a potentially useful molecule for application in biomedical, biotechnological, industrial, and agricultural areas particularly because it showed high stability when exposed to a wide range of temperatures and performance at pH 4–7 and impairment of mycelial growth of C. gloeosporioides and F. oxysporum. • A peroxidase (Vu-RPOX) was purified using chitin and Ion exchange column. • The enzyme is a glycoprotein with 58 kDa and pI 3.75. • Vu-RPOX has Km 0.120–33.44 mM and Vmax 0.15–0.93 AU/min for different substrates. • The peroxidase showed high thermo and chemical stability under several conditions. • Vu-RPOX has inhibitory activity on phytopathogenic fungi. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
18788181
Volume :
42
Database :
Supplemental Index
Journal :
Biocatalysis & Agricultural Biotechnology
Publication Type :
Academic Journal
Accession number :
157548130
Full Text :
https://doi.org/10.1016/j.bcab.2022.102322