Claim · model-written summary
Pectic substrates at pH 6.5 and above induced pectin lyases in aquatic hyphomycetes.
- Taxon
- aquatic hyphomycetese1
- Treatment
- pectic substrates at pH 6.5 and abovee0
- Outcome
- pectin lyases were inducede0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingDirectionValueQualifier
Verbatim
e0“the pectin lyases were induced on pectic substrates at pH 6.5 and above.”
e1“All seven species of aquatic hyphomycetes tested produced both polygalacturonases and pectin lyases.”
Title
Pectinases in Leaf Degradation by Aquatic Hyphomycetes: the Enzymes and Leaf Maceration
A.-C. Chamier; P. A. Dixon Microbiology 1982. doi:10.1099/00221287-128-10-2469
Other claims from this paper (13)
- Observation All seven tested aquatic hyphomycetes produced polygalacturonases and pectin lyases.
- Observation Aquatic hyphomycete polygalacturonases were constitutive.
- Observation Some aquatic hyphomycetes grew on pectic substrates at pH 5 and pH 7.
- Observation Other aquatic hyphomycetes grew on pectic substrates only at pH 7.
- Intervention effect Tricladium splendens grew equally well on polypectate and glucose.
- Observation Tricladium splendens produced three endo-polygalacturonase isoenzymes.
- Observation Articulospora tetracladia produced three endo-polygalacturonase isoenzymes.
- Observation Tetrachaetum elegans secreted a presumed exo-pectin lyase and a pectin esterase.
- Observation Mycocentrospora angulata secreted an endo-pectin lyase and a pectin esterase.
- Observation The four fungal species completely macerated alder leaf strips within 9 to 12 days at stream pH 7.
- Mechanism Pectin lyases and pectin esterases were the predominant enzymes used in alder leaf maceration.
- Mechanism Ca2+ stimulates these enzymes and may explain rapid plant decay in calcium-rich streams at pH 6.5 and above.
- Association Fungal occurrence on experimental stream leaf packs did not appear related to pectolytic capability.