Polygalacturonase Isozymes in the Cyanolichen Peltigera canina

Rı́os, Asunción de los; Ramírez, Rosalía; Estévez, Pilar

doi:10.1016/s0176-1617(11)81471-9

Cited by 2 publications

(1 citation statement)

References 11 publications

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“…This is also the case with the polygalacturonase off! canina (de los Rios et al 1996). The presence of multiple cellulases is common to cellulase-secreting organisms (Eriksson and Pettersson 1988, Kollar 1994, Willick and Seligy 1985, Yague and Estevez 1989b).…”

Section: Discussionmentioning

confidence: 99%

Production of several isoforms of β‐1,4‐glucanase by the cyanolichen Peltigera canina

Rı́os

Ramírez

Estévez

1997

Physiologia Plantarum

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Lichen cellulase may participate in the degradation of the external substrata and/or modification of the photobiont cell wall. To promote a better understanding of the roles of cellulases in lichens, a cyanolichen was chosen because of the absence of cellulose in its symbionts. Freshly‐collected thalli of Peltigera canina (L.) Wild, produce β‐1,4‐glucanase (EC 3.2.1.4, β‐1,4‐D‐glucanohydrolase). This enzyme's activity was detected in the soluble and cell wall fractions and it was found to be secreted to the incubation medium when thalli were floated on water or on cellobiose. Several forms of the enzyme were detected by isoelectrofocusing. In preparative isoelectrofocusing, a single peak was obtained in each fraction, characterized by pls of 5.05, 5.25 and 4.75 in the soluble, cell wall and medium fractions, respectively. These differences were in agreement with the different pattern of bands obtained in slab‐isoelectrofocusing, where the most acidic band (pl of 4.45) was present only in the soluble fraction and the band with higher pl (6.17) was more intense in the cell wall fraction. Since both symbionts in a cyanolichen lack cellulose, cellulases cannot participate in the modification of their cell wall; the presence of cellulase in Peltigera canina must therefore be related to the degradation of the tissues of the moss substratum.

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Section: Discussionmentioning

confidence: 99%

Production of several isoforms of β‐1,4‐glucanase by the cyanolichen Peltigera canina

Rı́os

Ramírez

Estévez

1997

Physiologia Plantarum

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Cellulase Activity in Isolates of Verticillium dahliae Differing in Aggressiveness

et al. 2006

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Ten Verticillium dahliae isolates from different Galician locations were classified by degree of aggressiveness. High variability exists independent of locality of origin. Two isolates differing in aggressiveness were evaluated for cellulase production on several carbon sources. V. dahliae is able to degrade crystalline cellulose (Avicel) and, therefore, has the three enzymes necessary for its hydrolysis. The two isolates behaved similarly in the presence of soluble cellulose, but the most aggressive isolate had greater β-1,4-glucosidase (EC. 3.2.1.21) and endo-β-1,4-glucanase (EC. 3.2.1.4) activity. The less aggressive isolate needed more time to degrade crystalline cellulose. Cellulases may not be the determining factor for aggressiveness and symptom expression; however, they may play a role in penetration.

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Polygalacturonase Isozymes in the Cyanolichen Peltigera canina

Cited by 2 publications

References 11 publications

Production of several isoforms of β‐1,4‐glucanase by the cyanolichen Peltigera canina

Production of several isoforms of β‐1,4‐glucanase by the cyanolichen Peltigera canina

Cellulase Activity in Isolates of Verticillium dahliae Differing in Aggressiveness

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