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Butyro-amidase

It is still to be noted that the butyro-amidase does not furnish the reaction ordinarily found when the experiment takes place in the presence of bacteria which secrete the enzyme. We succeed in the latter case, with the living ferment, in deamidizing up to 96 per cent of the total nitrogen contained in the products of the proteolysis. Now the enzymes isolated from their bacteria react solely on certain substances which form only about I of the total weight. Butyro-amidase reacts in two different ways on asparagin, according to the conditions of the medium. With water alone, as seen above, the action is limited to the amide grouping. On the contrary, in the presence of... [Pg.556]

The limited effect which we have just found with butyro-amidase acting on the products of hydrolysis of the nitrogenous materials, can be explained by the hypothesis that the bacterium secretes numerous specific enzymes, each acting on different substances. Butyro-amidase, thus isolated, would contain only certain enzymes, and not all those which are necessary for the evidently more exacting fermentation. Althou the amidases attack a series of substances of similar structure, they set ammonia free by different methods. We are, therefore, quite naturally led to believe that in this process several catalysts intervene, for it would be inadmissible that the same enzyme should be called upon to fill such varied functions. We will then conclude by saying that to each of the different chemical processes there corresponds a well-determined type of catalyst, whether the reaction be one of hydroly, or one of reduction. Unfortunately, in the present state of the question, this opinion cannot be confirmed by any experimental proof. [Pg.557]


See other pages where Butyro-amidase is mentioned: [Pg.555]    [Pg.555]    [Pg.557]    [Pg.558]    [Pg.555]    [Pg.555]    [Pg.557]    [Pg.558]   
See also in sourсe #XX -- [ Pg.4 , Pg.5 ]




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