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the handbook of food engineering practice crc press chapter 10 ...

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semi-empirical kinetic/ma<strong>the</strong>matical model that effectively represents <strong>the</strong> experimental data.<br />

Preferably <strong>the</strong> model would still have <strong>the</strong> general form <strong>of</strong> <strong>the</strong> quality function <strong>of</strong> eq.(14),<br />

where Q(A) can obtain any form o<strong>the</strong>r than <strong>the</strong> typical ones <strong>of</strong> Table 1. The steps for<br />

building such a model are described by Saguy and Karel (1980). Multivariable linear<br />

models, polynomial equations or nonlinear models can be defined and <strong>the</strong>ir fit to <strong>the</strong> data<br />

can be tested with computer aided multiple linear, polynomial or nonlinear regressions.<br />

Empirical equations modeling <strong>the</strong> effect <strong>of</strong> different composition or process parameters can<br />

be derived from statistical experimental designs, like <strong>the</strong> surface response methods<br />

(Thompson, 1983).<br />

A special category <strong>of</strong> reactions, <strong>the</strong> enzymatic reactions, important in <strong>food</strong>s are<br />

usually modeled by <strong>the</strong> Michaelis-Menten equation. This is a reaction rate function based<br />

on <strong>the</strong> steady-state enzyme kinetics approach (Engel, 1981). For an enzymatic system,<br />

with no inhibition, <strong>the</strong> rate equation has <strong>the</strong> form:<br />

r A =<br />

k [A]<br />

K m + [A] (16)<br />

where A is <strong>the</strong> substrate, k=k o [e] is proportional to <strong>the</strong> enzyme (e) concentration (k is<br />

usually called v max in biochemical terminology) and K m is a constant (r A = 0.5 k for [A] =<br />

K m ). When [A]>>K m , <strong>the</strong> equation reduces to a zero order reaction, r A =k. This is <strong>of</strong>ten<br />

<strong>the</strong> case in <strong>food</strong>s with uniformly distributed substrate in excess and small amounts <strong>of</strong><br />

enzyme, e.g., lipolysis <strong>of</strong> milk fat. When K m >>[A], <strong>the</strong> equation reduces to first order,<br />

r A =(k/K m ) [A]. This occurs in <strong>food</strong>s where <strong>the</strong> enzymes are highly compartmentalized<br />

and have limited access to <strong>the</strong> substrate or where generally <strong>the</strong> substrate limits <strong>the</strong> reaction,<br />

e.g., browning <strong>of</strong> fruit and vegetable tissue due to polyphenolase activity. Thus, a large<br />

portion <strong>of</strong> enzymatic reactions in <strong>food</strong>s can be handled as zero or first order systems.<br />

16

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