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Characterization of the phosphatase activities of mosses in relation to their environment
Author(s) -
Turner B. L.,
Baxter R.,
Ellwood N. T. W.,
Whitton B. A.
Publication year - 2001
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1046/j.1365-3040.2001.00767.x
Subject(s) - phosphomonoesterase , bryophyte , subarctic climate , substrate (aquarium) , phosphate , botany , phosphorus , chemistry , acid phosphatase , nutrient , phosphatase , environmental chemistry , zoology , biology , ecology , enzyme , biochemistry , organic chemistry
Phosphatase activities and environmental features were characterized for 12 terrestrial and aquatic mosses in upland northern England, along with four species sampled from subarctic Sweden. Phosphomonoesterase (PMEase) and phosphodiesterase (PDEase) activities of shoot tips were measured using para ‐nitrophenyl phosphate ( p ‐NPP) and bis‐ p NPP. All species showed PMEase activity, but not all showed PDEase activity. The mean pH optimum was 5·0 for PMEase and 5·7 for PDEase. The kinetic parameters K m and V max were calculated from three linear transformations of the Michaelis–Menten equation. The mean K m values of the mosses ranged between 77 and 468 µ m for PMEase and 26 and 414 µ m for PDEase. The corresponding V max values were 0·6–205 µ mol p NP g −1 DW h −1 for PMEase and 1·4–110 µ mol pNP g −1 DW h −1 for PDEase. Mosses from Sweden displayed greater K m and smaller V max values than those from England. The aquatics Fontinalis antipyretica and Rhynchostegium riparioides displayed two‐phase kinetics for PMEase and PDEase, with K m and V max being dependent on substrate concentration. Staining suggested that PMEase activity was located in the cell wall of most mosses. Phosphatase assays provide a rapid method for screening environmental nutrient status and a standard procedure is recommended.