| Abstract: | The velocity constant k of protein changes is commonly determined by heating as abruptly as possible to a given temperature for various periods. Its dependence on temperature or activation heat is deduced from the k value determinations at different temperatures, using the ARRHENIUS diagram. In contrast to this, the authors determined the k and E values in a temperature field for a constant reaction time. This is done directly in the foodstuff which is introduced (in ball form) into a bath of constant temperature. In case of foodstuffs with mere heat conduction, there are in the interior innumerable spherical shells subjected to the same thermal stress which increases from within towards the exterior. Thermal protein changes (such as the thermal coagulation of egg white and muscle proteins and the formation of metmyochromogen) which can be visualized directly or, in case of enzymatic denaturation, indirectly by colour reactions, using the presence-absence method, may be observed if the ball is cut in half. This procedure (termed "change-over method" by the authors) permits to calculate the unknown k and E values from the radius of the visible inner circle. (This applied also to cylindrical forms.) Since this method allows to estimate approximately these reaction kinetic constants directly in the foodstuff under conditions encountered in practice, it is in many cases better suited for simulating, calculating, or optimizing desirable or undesirable protein changes occurring during thermal processing than the mere model experiment with abrupt heating which does not reproduce the changes in the reaction medium occuring during the slow increase or decrease in temperature. |
