Ectomycorrhizal fungal communities and enzymatic activities vary across an ecotone between a forest and field

Megan A. Rúa, Becky Moore, Nicole Hergott, Lily Van, Colin R. Jackson, Jason D. Hoeksema

Research output: Contribution to journalArticlepeer-review

Abstract

Extracellular enzymes degrade macromolecules into soluble substrates and are important for nutrient cycling in soils, where microorganisms, such as ectomycorrhizal (ECM) fungi, produce these enzymes to obtain nutrients. Ecotones between forests and fields represent intriguing arenas for examining the effect of the environment on ECM community structure and enzyme activity because tree maturity, ECM composition, and environmental variables may all be changing simultaneously. We studied the composition and enzymatic activity of ECM associated with loblolly pine (Pinus taeda) across an ecotone between a forest where P. taeda is established and an old field where P. taeda saplings had been growing for <5 years. ECM community and environmental characteristics influenced enzyme activity in the field, indicating that controls on enzyme activity may be intricately linked to the ECM community, but this was not true in the forest. Members of the Russulaceae were associated with increased phenol oxidase activity and decreased peroxidase activity in the field. Members of the Atheliaceae were particularly susceptible to changes in their abiotic environment, but this did not mediate differences in enzyme activity. These results emphasize the complex nature of factors that dictate the distribution of ECM and activity of their enzymes across a habitat boundary.
Original languageEnglish
Pages (from-to)185-210
Number of pages26
JournalJournal of Fungi
Volume1
Issue number2
DOIs
StatePublished - Sep 2015
Externally publishedYes

ASJC Scopus Subject Areas

  • Ecology, Evolution, Behavior and Systematics
  • Plant Science
  • Microbiology (medical)

Keywords

  • Carbon
  • Nitrogen
  • Peroxidase
  • Phenol oxidase
  • Phosphatase
  • Pinus taeda
  • Soil texture
  • β-glucosidase

Cite this