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Patterns of activities of root phosphomonoesterase and phosphodiesterase in wetland plants as a function of macrophyte species and ambient phosphorus regime
Author(s) -
Rejmánková Eliška,
Sirová Dagmara,
Carlson Emily
Publication year - 2011
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.2011.03652.x
Subject(s) - macrophyte , phosphomonoesterase , wetland , phosphorus , enzyme , chemistry , botany , phosphodiesterase , phosphate , environmental chemistry , phosphatase , biology , ecology , biochemistry , organic chemistry
Summary• Phosphorus (P)‐limited plants produce higher amounts of root phosphatases, but research has mostly focused on phosphomonoesterases (PMEs). Because phosphate diesters can form a significant proportion of organic P in wetlands, we aimed to determine whether wetland plants produce both root PMEs and root phosphodiesterases (PDEs), and, if so, what factors influence activities of these enzymes. • We measured the activities of root PMEs and PDEs colorimetrically in a wide range of macrophytes from natural and P‐enriched wetlands. Hydrolyzable P in sediments was analyzed using commercially available PMEs and PDEs. • In all species, both root PMEs and PDEs were always present, and their activities were closely correlated. Sedges and broadleaved emergents had the highest activity of both enzymes, while those of floating‐leaved plants were the lowest. Redundancy analysis revealed close association between root enzymes and the proportion of monoesterase‐ and diesterase‐hydrolyzable dissolved unreactive P. Both enzymes were positively correlated with root tissue N : P ratio. • Both plant and sediment traits were important when explaining differences in enzyme activities. Although the activities are related to ambient P regime, the relationship was not close enough to use root enzymes as reliable predictors of dissolved unreactive P that is hydrolyzed by sediment phosphomono‐ and diesterases.

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