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Activity of native hydrolytic enzymes and their association with the cell wall of three ectomycorrhizal fungi.

Mycorrhiza 23, 185-197 (2013)
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The ecological and biogeochemical relevance of hydrolytic enzymes associated with the fungal cell wall has been poorly studied in ectomycorrhizal (ECM) fungi. We used a modified sequential extraction procedure to investigate the activity of various hydrolytic enzymes (β-glucosidase, acid-phosphatase, leucine-aminopeptidase, chitinase, xylanase and glucuronidase) and their association with the cell wall of three ECM fungi (Rhizopogon roseolus, Paxillus involutus and Piloderma croceum). Fungi were grown on C-rich solid medium under three different P concentrations (3.7, 0.37 and 0.037 mM). The sequential extraction procedure classifies enzymes as: (a) cytosolic, (b) loosely bound, (c) hydrophobically bound, (d) ionically bound and (e) covalently bound. Results showed that for the same fungus absolute enzymatic activity was affected by P concentration, whilst enzymatic compartmentalization among the cytosol and the cell wall fractions was not. The association of enzymes with the cell wall was fungus- and enzyme-specific. Our data indicate also that enzymes best known for being either extracellular or cytosolic or both, do act in muro as well. The ecological implications of cell wall-bound enzymes and the potential applications and limitations of sequential extractions are further discussed.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Cell wall-bound enzymes; Paxillus involutus; Piloderma croceum; Rhizopogon roseolus; Sequential extraction; Multivariate analysis; General linear model; Bound Phosphatase-activity ; Paxillus-involutus ; Candida-albicans ; Phanerochaete-chrysosporium ; Beta-glucosidases ; Acid-phosphatase ; Soil ; Proteins ; Nutrients ; Cloning
ISSN (print) / ISBN 0940-6360
e-ISSN 1432-1890
Zeitschrift Mycorrhiza
Quellenangaben Band: 23, Heft: 3, Seiten: 185-197 Artikelnummer: , Supplement: ,
Verlag Springer
Begutachtungsstatus