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EXTRACELLULAR ENZYMES OF THE MICROCYSTIS AERUGINOSA PCC 7813 STRAIN ARE INHIBITED IN THE PRESENCE OF HYDROQUINONE AND PYROGALLOL, ALLELOCHEMICALS PRODUCED BY AQUATIC PLANTS 1
Author(s) -
Dziga Dariusz,
Goral Tomasz,
Bialczyk Jan,
Lechowski Zbigniew
Publication year - 2009
Publication title -
journal of phycology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.85
H-Index - 127
eISSN - 1529-8817
pISSN - 0022-3646
DOI - 10.1111/j.1529-8817.2009.00742.x
Subject(s) - microcystis aeruginosa , biology , extracellular , enzyme , pyrogallol , biochemistry , aminopeptidase , hydroquinone , allelopathy , strain (injury) , enzyme assay , leucine , botany , cyanobacteria , bacteria , amino acid , germination , genetics , anatomy
Several cyanobacterial species have a high potential to dominate in marine environments and freshwater reservoirs, and the ecological and physiological reasons for this phenomenon are not understood comprehensively. In this study, the ability of a Microcystis aeruginosa Kütz. strain to produce free dissolved enzymes was documented. We have observed that this highly toxic strain releases alkaline phosphatase, leucine aminopeptidase, and β‐glucosidase into the ambient environment. Additionally, the inhibitory activity of selected phenols produced by aquatic plants on the activity of these enzymes was analyzed. The investigated compounds, pyrogallol and, to a lesser degree, hydroquinone, decreased the activity of extracellular enzymes produced by M. aeruginosa, with leucine aminopeptidase being the most sensitive to the inhibitors. The noncompetitive character of enzymatic inhibition suggests that the polyphenols produced by aquatic plants are able to influence the activity of different extracellular or membrane‐bound enzymes.