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The optimum coincided Post Date: Fri, 1 Aug 2008 1:20:32 +0000
Thus Svanberg 62 records that yeast cultivated between 25 and 28 showed a higher sacoharase con- tent than cultures grown outside this optimum. At the optimum temperature the production of saccharase by a non- multiplying culture of yeast was found by von Euler and Svanberg to remain constant throughout the period of investigation. The optimum coincided with the optimum Lowry, and Schneider 60 record a somewhat wider optimum In the case of the mycelium of Penicittium glaucum grown at or below von Euler found that the largest amount of saccharase was produced on the fourth day after inocula- tion.
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In a species of Fusarium Post Date: Fri, 1 Aug 2008 1:03:20 +0000
It amounted to only one-tenth of that produced under optimum conditions by a bottom yeast or one-sixth of that of a top yeast. The conidia of the Penicittium species studied contained but one-third of the saccharase found in the mycelium. In a species of Fusarium investigated in 1887 by Wasserzug 66 copper-reducing carbohydrates were not observed in a saccharose solution acted upon by the fungus until the fifth day after inoculation.
Autor of the post: Undefined
This may have been due Post Date: Fri, 1 Aug 2008 0:45:06 +0000
Here, therefore, the production of saccharase had been even slower than in the case of Peni- cittium glaucum. A reduction in saccharase production was observed by Fermi and Montesano in the case of their test-organisms when grown beyond their optimum temperatures. This may have been due to a general lowering of the vitality of the organisms since the recovery of enzyme production did not take place for a number of generations.
Autor of the post: Undefined
This view became discredited, but Post Date: Fri, 1 Aug 2008 0:32:03 +0000
At von Euler and Svanberg were unable to detect sacoharase production by their yeast strain. The action of sacoharase was thought by Brown to lead in the first instance to a compound being formed between the enzyme and the hydrolyte, cane sugar. This view became discredited, but has recently been accepted as correct by Colin and Chaudun.
Autor of the post: Undefined
OSullivan and Thompsons investigations Post Date: Fri, 1 Aug 2008 0:12:06 +0000
It is also supported by Fermi and Montesanos observation that sacoharase shows greater resistance to high temperatures in the presence of cane sugar than in the absence of the carbohydrate. Accord- ing to and Armstrong sacoharase extends its influence over the whole of the saccharose molecule, and differs in this respect from other disaccharide hydrolysing enzymes such as maltase, which affects only one part of the hydrolyte. OSullivan and Thompsons investigations in 1890 to IngersolTs observations in 1926, the subject of the rate of hydrolysis of saccharose by its specific enzyme has received considerable attention.
Autor of the post: Undefined
The reason for this decrease Post Date: Thu, 31 Jul 2008 23:59:17 +0000
Under favourable conditions, and in solutions containing up to 5 per cent, of saccharose, the rate will increase proportionally to the amount of hydrolyte present. Beyond this the rate remains stationary until a 20 per cent, concentration of saccharose is reached (von Euler and Myrback ), when a decrease in rate sets in. The reason for this decrease has not been satisfactorily explained so far.
Autor of the post: Undefined
Perhaps the saccharose itself Post Date: Thu, 31 Jul 2008 23:45:55 +0000
Colin and Chaudun associate it with the greater viscosity of high concentrations, pointing out that glycerin, as was first observed by Michaelis and Pechstein and by Bourquelot, produces a similar inhibition. But increased viscosity apparently (Ingersoll ) is not an important factor. Perhaps the saccharose itself, as Ingersoll suggests, may be the factor governing the retardation.
Autor of the post: Undefined
For this reason the former Post Date: Thu, 31 Jul 2008 23:34:57 +0000
Another type of inhibition in the rate of hydrolysis is that caused by the two products of reaction, glucose and fructose, even at favourable concentrations of saccharose. It is usually observed that saccharase from yeast is iiihibited by fructose and that Aspergittus saocharase is similarly affected by the addition of glucose. For this reason the former enzyme has been regarded as different from the latter, possessing a specific affinity for the fructose half of the saccharose mole- cule as against the specificity of the Aspergillus saccharase for the glucose half of saccharose.
Autor of the post: Undefined
Contributions to this study Post Date: Thu, 31 Jul 2008 23:16:45 +0000
The terms fruoto- and gluco-saocharase respectively have sometimes been applied to the two enzymes (Kuhn and Munch 77 ). The study of the action of glucose, fructose, and methylglucoside on the rate of hydrolysis of saccharose is at present being actively pursued. Contributions to this study have been made by Nelson and Anderson, 78 Nelson and Post, 79 Josephson, 80 von Euler and Josephson, 81 and by Weidenhagen, 82 so far, however, without any definite conclusions being reached as to the significance of the various observations made.
Autor of the post: Undefined
In the case of propionic Post Date: Thu, 31 Jul 2008 23:01:09 +0000
An accelerating action of various acids on the activity of saccharase was observed by Bertrand and Rosenblatt. They found that the saccharase of Asprgillua niger usually was less markedly affeoted in its action by acids than yeast saocharase, though the effect differed with the nature of the acid. In the case of propionic acid the concentration inducing the most rapid acceleration of the reaction was found to be the same for both enzymes.
Autor of the post: Undefined
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