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Specificity of Heat-Stable Pseudomonal Proteases: Peptide Mapping by Reverse-Phase High Performance Liquid Chromatography¹

ConAgra Frozen Foods, 409 Vandiver Drive, Suite 102, Building 7, Columbia, MO 65202

R. T. Marshall

University of Missouri, Food Science and Nutrition, 122 Eckles Hall Columbia 65211

ABSTRACT

Extracellular heat-stable proteases from strains 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.

¹ Contribution from the Missouri Agricultural Experiment Station. Journal Series Number 10368.