Exlxacellular proteases from strains P26, 32A, P1, and 1)27 of Pseudomonas fluorescens were produced using a dialysis membrane method. The proteases were partially purified by gel filtration (molecular weight cutoff = 60,000) and selected biochemical characteristics were determined. Proteases of all strains were heat-stable (62.5C, 30 rain), neutral (>84% of total activity between pH 6 and 8) metalloenzymes (inhibited by 10 mM EDTA). Optimal temperature for activity was about 37C, but all proteases were active at 5C. Activation energies on azocasein ranged from 4.5 (P1) to 14.0 (32A) kcal-mol -I. All extracellular proteases had strong endopeptidase activity, but no exopeptidase (aminopeptidase) activity was detected.
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Mitchell et al. (1989) studied this question.
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