The proteolytic enzymes of proteus vulgaris.
Bensusan, Howard Bernard
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Two variations of the formol titration were developed to determine proteolytic activity. The first used phenolphthalein as an end-point indicator while the second was a potentiometric titration with an end point of pH 7.8. The standard error of the mean for the two methods were -+ 0.3 and -+ 0.13 microeqs. respectively. The substrate used was a 3% gelatin solution with a tris (hydroxymethyl) aminomethane buffer at pH 7.4, the optimum pH of enzyme activity. [TRUNCATED] The production and purification of the proteolytic enzymes of Proteus vulgaris are discussed. Kaolin was used as an adsorbent in the purification. Subsequent elution yielded a preparation containing two proteolytic enzymes and an inactive traction. The active traction consists of a relatively heat-stable enzyme and a heat-labile enzyme. The kinetics of these two enzymes was, studied to determine the Michaelis-Menten constants, effects of substrate, effect of end products, the molar energy of activation, and the inactivation by heat. A unit of activity based on reaction rates is proposed.
Thesis (Ph.D.)--Boston University
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