Purification and characterization of two basic Beta-1,3-glucanases induced in Colletotrichum lindemuthianum infected bean seedlings

Daugrois Jean-Heinrich, Lafitte C., Barthe J.P., Faucher C., Touzé A., Esquerre Tugaye M.T.. 1992. Purification and characterization of two basic Beta-1,3-glucanases induced in Colletotrichum lindemuthianum infected bean seedlings. Archives of Biochemistry and Biophysics, 292 (2) : 468-474.

Autre titre : Purification et caractérisation de deux Bêta-1,3-glucanases de base induites chez les plantules de haricot contaminé par Colletotrichum lindemuthianum

Résumé : Two Beta-1,3-glucanases which are rapidly induced in the incompatible interaction between bean (cv. Processor) and #Colletotrichum lindemuthianum# race Beta were purified to homogeneity. Characterization of the two enzymes, GE1 and GE2, showed that they both had a basic isolectric point and a similar molecular weight (36,500 for GE1 and 36,000 for GE2), but differed in their pH optimum, thermal stability, and specific activity. GE2 was present in higher amounts but was shown to be less active than GE1 against laminarin and fungal cell walls isolated from race Beta of the fungus. Both enzymes were specific for Beta-1,3 linkages and showed a strict endolytic mode of action. Further characterization of GE2 was achieved by amino acid sequence analysis of tryptic peptides; the degree of homology shared with other basic Beta-1,3-glucanases depended on the plant source. A time-course study showed that GE1 and GE2 were increased during infection. They were also induced by fungal elicitors, there by indicating that they originate from the host.

Mots-clés Agrovoc : bêta glucanase, Colletotrichum lindemuthianum, relation hôte pathogène, mécanisme de défense, réponse de la plante, plantule, Phaseolus vulgaris

Classification Agris : F60 - Physiologie et biochimie végétale

Auteurs et affiliations

• Daugrois Jean-Heinrich
• Lafitte C.
• Barthe J.P.
• Faucher C.
• Touzé A.
• Esquerre Tugaye M.T.

Source : Cirad - Agritrop (https://agritrop.cirad.fr/400828/)

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