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Cervone F, De Lorenzo G, Degrà L, et al. Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers. Plant Physiol. 1987;85(3):626-30doi: 10.1104/pp.85.3.626.
Cervone, F., De Lorenzo, G., Degrà, L., & Salvi, G. (1987). Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers. Plant physiology, 85(3), 626-30. https://doi.org/10.1104/pp.85.3.626
Cervone, F, et al. "Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers." Plant physiology vol. 85,3 (1987): 626-30. doi: https://doi.org/10.1104/pp.85.3.626
Cervone F, De Lorenzo G, Degrà L, Salvi G. Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers. Plant Physiol. 1987 Nov;85(3):626-30. doi: 10.1104/pp.85.3.626. PMID: 16665750; PMCID: PMC1054312.
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Plant Physiol. 1987 Nov;85(3):626-30. doi: 10.1104/pp.85.3.626.

Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by alpha-d-Galacturonate Oligomers.

Plant physiology

F Cervone, G De Lorenzo, L Degrà, G Salvi

Affiliations

  1. Dipartimento di Biologia vegetale, Università di Roma "La Sapienza," Piazzale A. Moro 00100, Rome, Italy.

PMID: 16665750 PMCID: PMC1054312 DOI: 10.1104/pp.85.3.626

Abstract

Endo-polygalacturonase (PG) was purified from a commercial preparation of Aspergillus niger pectinase by means of carboxymethylcellulose chromatography, preparative isoelectric focusing, and gel permeation through Sephadex G-50. The enzyme was electrophoretically homogeneous and consisted of a single polypeptide chain with a molecular weight of 33,500. The enzyme exhibited a specific activity significantly higher than those of purified polygalacturonases from phytopathogenic fungi. Galacturonate oligomers with a degree of polymerization higher than four appeared quickly as products of the enzymic hydrolysis of Napolygalacturonate. The oligomers were later degraded to di- and monogalacturonate. The homogeneous enzyme and growing mycelium of Aspergillus niger separately elicited a necrotic response in cowpea (Vigna unguiculata Walp.) pods. Heat-inactivated PG and PG inactivated with specific antibodies did not elicit necrosis, suggesting that the catalytic activity of the enzyme is necessary for its function as an elicitor. The PG-released oligosaccharides from Vigna cell wall and the galacturonides with a degree of polymerization greater than four separately elicited necrosis, whereas di- and monogalacturonate did not.

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