The aim of the work was a comparative study of substrate specificity of molecular forms (MF) of green alga peroxidase depending on their systematic position, ecological conditions, of place and period of vegetation. Peroxidase activity was determined after the electrophoretic separation of proteins in PAAG, using benzidine, pyrogallol, pyrocatechol and guaiacol as substrata. Plural MFs of peroxidase both with wide substrate specificity and with expressed affinity only to one substrata were found in green alga. The greater number of MFs with wide substrate specificity was detected in unicellular green alga than it was found in more evolutional advanced multicellular green alga. The number of MFs of peroxidase in the integral spectra of green macrophytes, as well as early studied red and brown alga, was lesser than in blue-green alga. It was concluded that substrate specificity of peroxidase in green alga as well as in blue-green and red alga is narrowed with complication of their organization. The data are evidenced of evolutional importance of enzymatic MFs diversity and allow to consider them as one of units in the biochemical mechanisms of adaptation.

Keywords: green alga, peroxidase, benzidine, pyrogallol, pyrocatechol, guaiacol, molecular forms

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