Proteinase activity in mycorrhizal fungi: I. The effect of extracellular pH on the production and activity of proteinase by ericoid endophytes from soils of contrasted pH.

Abstract

The effect of pH on the production and specific activity of the extracellular proteinase enzymes of two ecologically distinct ericoid mycorrhizal fungi is described. The proteinase of Hymenoscyphus ericae (Read), Korf & Kernan, isolated from roots of Calluna vulgaris (L.) Hull growing in soil of pH 35, was compared with a similar enzyme from an endophyte of the calcicolous alpine shrub Rhodothamnus chamaecistus (L.) Reichenb. growing in soil of pH 6.5. The fungi were grown in liquid culture at pH values ranging from 3.0 to 8.0 with pure protein, bovine serum albumin, as sole source of N. Both fungi yielded an extracellular acid proteinase with pH optimum for activity between 20 and 30. The production and activity of these enzymes was strongly affected by pH of the culture medium. Maximum enzyme production during exponential growth occurred in both fungi at a culture pH of 4.0-5.0, whereas higher pH treatments severely inhibited enzyme production. The acid proteinase of H. ericae was tolerant of extreme acidity and retained near-optimal activity in solutions of pH 2.0. In contrast, the activity of the enzyme from the Rhodothamnus endophyte was almost completely inhibited at this pH. However, proteinase from the Rhodothamnus endophyte retained activity at much higher pH values than did the proteinase from H. ericae. Unlike H. ericae, the isolated endophyte of Rhodothamnus was able to grow and use protein as sole source of N at pH 7.0 and 8.0. The effects of pH on enzyme production and upon growth of the fungi are discussed in relation to the characteristics of the environments of their host plants.