Association of pectolytic and cellulolytic enzymes with bacterial slow wilt of Carnation caused by Erwinia chrysanthemi Burkh., McFad. et Dim

The Carnation strain of Erwinia chrysanthemi Burkh., McFadden et Dimock (isolate 307) produced polygalacturonic acid trans-eliminase (PGTE) and cellulase (Cx) in culture as well as in infected Carnation plants. The PGTE exhibited a pH optimum near 9.6 with sodium polypectate or polygalacturonic acid...

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Veröffentlicht in:Phytopathologia mediterranea 1970-12, Vol.9 (2/3), p.136-144
Hauptverfasser: Garibaldi, Angelo, Bateman, Durward F.
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Sprache:eng
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Zusammenfassung:The Carnation strain of Erwinia chrysanthemi Burkh., McFadden et Dimock (isolate 307) produced polygalacturonic acid trans-eliminase (PGTE) and cellulase (Cx) in culture as well as in infected Carnation plants. The PGTE exhibited a pH optimum near 9.6 with sodium polypectate or polygalacturonic acid as the substrate. This enzyme system was shown to consist of two components with isoelectric points of pI 9.1 and pI 7.9. The former component (pI 9.1) attacked its substrate in a more random manner (endo) than did the component with a pI of 7.9. The molecular weigts of both PGTE components were similar and ranged between 30,000 and 32,400. The Cx of E. chrysanthemi appeared to consist of one component and it exhibited a pH optimum of 6.5-7 on carboxymethylcellulose (CMC). This enzyme had a pI of 5.5. The PGTE activity found in infected plants was limited to the lower 5 cm of infected stem tissues. No significant activity could be demonstrated in the upper portions of diseased stems before or after development of severe symptoms of slow wilt or stunt. Cx activity was maximum in the lower 5 cm of infected stems but it could also be easily demonstrated in the upper stem portions. Both pectolytic and cellulolytic enzymes, are associated with pathogenesis by E. chrysanthemi, but the specific role these enzymes play in the development of slow wilt or stunt of Carnation remains to be elucidated. Il ceppo di Erwinia chrysanthemi Burkh., McFad. et Dim. (isolamento 307) che causa l'avvizzimento o nanismo del Garofano, produce in coltura e nelle piante infette una transeliminasi dell'acido poligalatturonico (PGTE) e una cellulasi (Cx). La PGTE presenta una attività ottimale ad un pH di circa 9,6 usando come substrato sia il polipectato di sodio sia l'acido poligalatturonico. Sottoposto a purificazione questo enzima si è rivelato essere costituito da due componenti con punto isoelettrico (pI) rispettivamente di 9,1 e di 7,9. Il primo (pI 9,1) attacca il substrato in punti più casuali (endo) di quanto non faceia il componente pI 7,9, che attacca maggiormente la parte terminale delia catena poligalatturonica. I pesi molecolari di entrambi i componenti sono simili e variano tra 30.000 e 32.400. La cellulasi (Cx) prodotta da questo batterio è apparsa costituita da un solo componente presentante una attività ottimale ad un pH di 6,5-7 su carbossimetilcellulosa e un punto isoelettrico di 5,5. La PGTE è stata rinvenuta solo nella parte basale (5 cm) dei fusti infetti di Garofano
ISSN:0031-9465
1593-2095