Eis

Figure 3. General equilibrium model for reversible enzyme inhibition. Source: Ref. 1, p. 38.

The measured rate at each point is v,. A plot is made of X/Vi versus X (Fig. 6b). From the y-axis intercept calculate the uninhibited rate; that is, 1/intercept equals the true rate due to enzyme concentration [c]. This method is useful for comparing enzyme amounts from different sources, and during enzyme purification until the inhibitor has been removed.

of the wide range of ingenious methods that have been reported for following the rate of product formation by food-related enzymes. In most cases factors such as pH, temperature, activating ions, time of reaction, and detection methods may be adjusted to fit the specific needs of the project in hand. Thus, these should be considered as starting points for designing assays to meet particular requirements, not the only way to measure the enzyme activity under investigation.

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