Aminopeptidase Profiles of Four Species of Phytophthora†

AUTOR(ES)

Huber, D. M.

RESUMO

Phytophthora palmivora, P. cinnamomi, P. drechsleri, and P. cactorum were readily separated on the basis of the aminopeptidase substrate specificities of their mycelial suspensions. Variability among isolates of the same species was not significant with most substrates and isolates tested, regardless of source. Both qualitative and quantitative differences in enzyme activity were useful for species identification. Differentiation of these four species was possible with comparative reactions of l-alanyl-, l-arginyl-, l-benzoylarginyl, l-gamma-glutamyl-, l-glycyl-, l-hydroxyprolyl-, l-leucyl-, l-lysyl-, 4-methoxyleucyl-, l-prolyl-, and 4-methoxyalanyl-beta-naphthylamides. Variation in peptidase activity was usually detectable after 4 h of incubation, with increased activity sometimes manifest after 24 h of incubation. P. palmivora exhibited the lowest, and P. drechsleri exhibited the highest, overall peptidase activity. This fluorescent aminopeptidase profile procedure provides a relatively rapid method to supplement other taxonomic criteria for identification of these species of Phytophthora.

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