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Control and possible applications of a novel carrot-spoilage basidiomycete, Fibulorhizoctonia psychrophila.

de Vries RP, de Lange ES, Wösten HA, Stalpers JA - Antonie Van Leeuwenhoek (2008)

Bottom Line: Growth of this fungus was observed between 0 and 20 degrees C with an optimum at 9-12 degrees C, while incubation of mycelium grown at 15-32 degrees C resulted in absence of growth even after the fungus was transferred back to 15 degrees C.Growth was inhibited in the presence of the antifungals sorbic acid or natamycin, in particular when the fungus was incubated at 18 degrees C.F. psychrophila produces polysaccharide degrading enzymes that, when compared to enzymes from the ascomycete fungus Aspergillus niger, retain a larger proportion of their activity at lower temperatures.

View Article: PubMed Central - PubMed

Affiliation: Department of Microbiology, Utrecht University, Utrecht, The Netherlands. r.p.devries@uu.nl

ABSTRACT
A novel cold-tolerant fungus, Fibulorhizoctonia psychrophila, was isolated from a refrigerated carrot storage facility and identified as an anamorph of Athelia, often classified in Rhizoctonia s.l. Growth of this fungus was observed between 0 and 20 degrees C with an optimum at 9-12 degrees C, while incubation of mycelium grown at 15-32 degrees C resulted in absence of growth even after the fungus was transferred back to 15 degrees C. Growth was inhibited in the presence of the antifungals sorbic acid or natamycin, in particular when the fungus was incubated at 18 degrees C. F. psychrophila produces polysaccharide degrading enzymes that, when compared to enzymes from the ascomycete fungus Aspergillus niger, retain a larger proportion of their activity at lower temperatures. This indicates that F. psychrophila could be used as a source for novel industrial enzymes that are active at 4-15 degrees C.

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Relative hydrolase activities in culture filtrate of Fibulorhizoctonia psychrophila and Aspergillus at different temperatures. (a) A. niger culture filtrate; (b) F. psychrophila culture filtrate. AGL = α-galactosidase, LAC = β-galactosidase, BGL = β-glucosidase, BXL = β-xylosidase. Activity at 30° is set at 100%
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Fig4: Relative hydrolase activities in culture filtrate of Fibulorhizoctonia psychrophila and Aspergillus at different temperatures. (a) A. niger culture filtrate; (b) F. psychrophila culture filtrate. AGL = α-galactosidase, LAC = β-galactosidase, BGL = β-glucosidase, BXL = β-xylosidase. Activity at 30° is set at 100%

Mentions: For A. niger, enzyme activities dropped to 30–50% when incubation at 15°C was compared to 30°C (Fig. 4a). At 4°C, only 10–20% of the 30°C-activity was observed. For F. psychrophila only a 5–35% drop was detected when comparing 30°C to 15°C and 30–60% of the activity at 30°C was still observed at 4°C (Fig. 4b). The strongest difference was observed for α-galactosidase and β-glucosidase, where more than 90% of the activity was still detected at 15°C for F. psychrophila, while for A. niger only 35–45% of the activity was detected at this temperature.Fig. 4


Control and possible applications of a novel carrot-spoilage basidiomycete, Fibulorhizoctonia psychrophila.

de Vries RP, de Lange ES, Wösten HA, Stalpers JA - Antonie Van Leeuwenhoek (2008)

Relative hydrolase activities in culture filtrate of Fibulorhizoctonia psychrophila and Aspergillus at different temperatures. (a) A. niger culture filtrate; (b) F. psychrophila culture filtrate. AGL = α-galactosidase, LAC = β-galactosidase, BGL = β-glucosidase, BXL = β-xylosidase. Activity at 30° is set at 100%
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2268727&req=5

Fig4: Relative hydrolase activities in culture filtrate of Fibulorhizoctonia psychrophila and Aspergillus at different temperatures. (a) A. niger culture filtrate; (b) F. psychrophila culture filtrate. AGL = α-galactosidase, LAC = β-galactosidase, BGL = β-glucosidase, BXL = β-xylosidase. Activity at 30° is set at 100%
Mentions: For A. niger, enzyme activities dropped to 30–50% when incubation at 15°C was compared to 30°C (Fig. 4a). At 4°C, only 10–20% of the 30°C-activity was observed. For F. psychrophila only a 5–35% drop was detected when comparing 30°C to 15°C and 30–60% of the activity at 30°C was still observed at 4°C (Fig. 4b). The strongest difference was observed for α-galactosidase and β-glucosidase, where more than 90% of the activity was still detected at 15°C for F. psychrophila, while for A. niger only 35–45% of the activity was detected at this temperature.Fig. 4

Bottom Line: Growth of this fungus was observed between 0 and 20 degrees C with an optimum at 9-12 degrees C, while incubation of mycelium grown at 15-32 degrees C resulted in absence of growth even after the fungus was transferred back to 15 degrees C.Growth was inhibited in the presence of the antifungals sorbic acid or natamycin, in particular when the fungus was incubated at 18 degrees C.F. psychrophila produces polysaccharide degrading enzymes that, when compared to enzymes from the ascomycete fungus Aspergillus niger, retain a larger proportion of their activity at lower temperatures.

View Article: PubMed Central - PubMed

Affiliation: Department of Microbiology, Utrecht University, Utrecht, The Netherlands. r.p.devries@uu.nl

ABSTRACT
A novel cold-tolerant fungus, Fibulorhizoctonia psychrophila, was isolated from a refrigerated carrot storage facility and identified as an anamorph of Athelia, often classified in Rhizoctonia s.l. Growth of this fungus was observed between 0 and 20 degrees C with an optimum at 9-12 degrees C, while incubation of mycelium grown at 15-32 degrees C resulted in absence of growth even after the fungus was transferred back to 15 degrees C. Growth was inhibited in the presence of the antifungals sorbic acid or natamycin, in particular when the fungus was incubated at 18 degrees C. F. psychrophila produces polysaccharide degrading enzymes that, when compared to enzymes from the ascomycete fungus Aspergillus niger, retain a larger proportion of their activity at lower temperatures. This indicates that F. psychrophila could be used as a source for novel industrial enzymes that are active at 4-15 degrees C.

Show MeSH
Related in: MedlinePlus