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Specificity of heat stable pseudomonal proteases peptide mapping by reverse phase high performance liquid chromatography


, : Specificity of heat stable pseudomonal proteases peptide mapping by reverse phase high performance liquid chromatography. Journal of Dairy Science 72(4): 875-882

Extracellular heat-stable proteases from strain P26, 32A, P1, and 27 of Pseudomonas fluorescens were partially purified by molecular exclusion chromatography. Peptides generated from the hydrolysis of oxidized ribonuclease A by proteases of known substrate specificity (trypsin, chymotrypsin, Staphylococcus aureus protease) and the pseudomonal proteases were separated by reverse-phase HPLC. The proteases of known specificity generated a low number of peptides in relatively high concentrations. Proteases of strains P26, 32A, P1 and P27 produced more peptides, and most of these peptides were in low concentrations. Thus, the pseudomonal proteases exhibited a comparatively wide substrate specificity. Among the heat-stable proteases, those of strains P26 and 32A hydrolyzed a wider range of peptide bonds than did proteases of strains P1 and P27.

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