Recherches sur les chitinases II. — Purification de la chitinase d'un streptomycète, et séparation électrophorétique de principes chitinolytiques distincts

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Abstract
The purification and concentration of the chitinase of a streptomycete are described. The procedure consists essentially of a mass adsorption on colloidal chitin, followed by washing out and enzymic hydrolysis of the adsorbant, and of two consecutive fractionations by ammonium sulfate. The chitinolytic "activity has been concentrated 70 times, with a yield of 27%. The purified solution is homogeneous in the ultracentrifuge (molecular weight = 30,000) and also during the tests of solubility in ethanol or ammonium sulfate solution. By electrophoresis at pH 8.2 in agar-agar plates, it has been possible to isolate three different chitinases, besides a small fraction of non-chitinolytic protein (4.5%). These three chitinases show slightly different electrophoretic patterns; they have however the same specific activities, but, when they are recombined, a synergistic effect on chitin hydrolysis is observed.

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