Analysis of the Ectomycorrhizal Enzymatic Functional Diversity of Fagus mexicana
In forest ecosystems, ectomycorrhizal symbiosis is able to produce a large range of extracellular and cell wall-bound enzymes which hydrolyze compounds contained in soil organic matter. Enzymatic activity profiles of individual ectomycorrhiza have value of functional traits to characterize the diver...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences, India. Section B: Biological sciences India. Section B: Biological sciences, 2018-12, Vol.88 (4), p.1377-1387 |
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Sprache: | eng |
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Zusammenfassung: | In forest ecosystems, ectomycorrhizal symbiosis is able to produce a large range of extracellular and cell wall-bound enzymes which hydrolyze compounds contained in soil organic matter. Enzymatic activity profiles of individual ectomycorrhiza have value of functional traits to characterize the diversity of ectomycorrhizal (ECM) communities.
Fagus mexicana
is an endemic and only species that has restricted distribution to cloud forest of Sierra Madre Oriental in México and there are few works focused to the relationship between this forest species and ectomycorrhizal, which enhance its growth and development. This work analyzes the enzyme functional diversity of ectomycorrhizal fungi associated to
F. mexicana
trees of different ages. In this study, the ECM species:
Cantharellus cibarius
Fr.,
Laccaria amethystina
Cook,
Lactarius subdulcis
(Pers.) gray and
Xathoconium separans
(Peck) Halling & Both, were founded near these trees and the influence of the niche on the mean catabolic activity of ectomycorrhizal community, varied according to the dominant substrate; where
L. amethystina
and
X. separans
presented the highest β-glucosidase and acid phosphatase activities in
F. mexicana
tips. The enzymatic profiles demonstrated a functional plasticity of the ectomycorrhizal species associated to the age of trees tested and also could be a trait of their capability of adaptation to the cloud forest ecosystem. |
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ISSN: | 0369-8211 2250-1746 |
DOI: | 10.1007/s40011-017-0876-6 |