Unlike many other kinetic volumes available, this book opens the door to the many untapped research opportunities in the food science realm where mathematical modeling can be applied.
Kinetic Modeling of Reactions In Foods - CRC Press Book
Well done and timely. Congratulations to the author. It is wonderful to have a comprehensive collection of kinetic models, lucid analyses and data in both tabulated and graphical forms, all in one volume! Importantly, the book is quite well-referenced, making relatively easy to find supplemental material when desired. We provide complimentary e-inspection copies of primary textbooks to instructors considering our books for course adoption. Most VitalSource eBooks are available in a reflowable EPUB format which allows you to resize text to suit you and enables other accessibility features.
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Kinetic Modeling of Reactions In Foods (Food Science and Technology)
Summary The level of quality that food maintains as it travels down the production-to-consumption path is largely determined by the chemical, biochemical, physical, and microbiological changes that take place during its processing and storage. Illustrating how kinetic modeling can predict and control food quality from farm to fork, this authoritative resource: Applies kinetic models using general chemical, physical, and biochemical principles Introduces Bayesian statistics in kinetic modeling, virtually unchartered territory in the food science field Integrates food science, kinetics, and statistics to predict and control food quality attributes using computer models Uses real-world examples rather than hypothetical data to illustrate concepts This essential reference is an indispensable guide to understanding all aspects of kinetic food modeling.
Reviews "The book is a spectacular accomplishment and a result of monumental work. Request an e-inspection copy. Share this Title. Recommend to Librarian. Related Titles. Equation 4. The rate of the hydrolysis process 42 is shown as:. Equation 5. Then, the Equations for the mechanisms of the substrate and the product inhibition are 46 :. Equation 6. Equation 7. Equation 8.
Qi and He 46 proposed that the inactivation of the protease mechanism is:. Equation 9. Equation From the definition of the equilibrium constant of the dissociation of ES, it is possible to find an expression for the concentration of ES:. Substituting Equation 15 into Equation 13 shows:. Substituting Equation 18 into Equation 16 forms an exponential expression of [ ES ] that can be obtained when replaced in Equation 5 to provide a model to estimate the change in the ratio of the DH as function of the same DH. The comparison of this expression with the Equation 19 , which has been used to adjust curves for this type of protein enzymatic hydrolysis 46 , 48 , provides a method to obtain the overall expressions to estimate the kinetic parameters a and b using the Equation 20 and Equation 21 :.
Figure 1 shows an opposite effect of the substrate concentration on the DH, indicating possible substrate inhibition without product inhibition. From a kinetic point of view, this effect means that the complex SES is obtained and therefore the equilibrium constant dissociation value K s should be close to zero. Under this assumption, there is no product inhibition. The compound EP tends to dissociate, and for this reason, equilibrium constant K P value of the compound should be high.
Based on the above, the final Equations for a and b with substrate inhibition are:.
Kinetic Modeling of Reactions In Foods
K s was calculated through the division of the intercept by the slope, which was determined from this plot. Then, it is possible to obtain the K d value by dividing the K 2 value by the intercept of the line as shown in Figure 3. To estimate K 3 it is necessary to know the values of Michaelis-Menten constants K M and r max using the double reciprocal approach of Hannes-Woolf shown in the Equation 24 32 :.
Using the last Equation, it is possible to obtain a straight line, which is shown in Figure 3 , and determine the slope and intercept of the line. This determination makes it possible to calculate the K 3 and K M values because the K d value is also known. The correlation coefficient value of the straight line in Figure 3 is close to 1, which indicates that the linearization process was acceptable.
The values of the ratios of the initial substrate concentration to the reaction rate corresponding to the initial concentrations of substrate were evaluated in each test. The reaction rates were obtained from the initial section in each curve in Figure 2. The K M value is shown below with a correlation factor R 2 of 0. The K M value and the graphic behavior shown in Figure 3 supports the substrate inhibition hypothesis proposed for the reacting system 49 , which has been documented by different authors with other substrates but with the same enzyme One explanation for the substrate inhibition is found in the presence of fat in RTV, which can interact with the proteins to produce a lipid-protein complex and reduce the accessibility of the enzyme to the protein On the other hand, there is the possibility of a hydrophobic interaction between proteins and substrates that reduces the accessibility of the enzyme 41 , The Kinetic constant values for hydrolysis of RTV-alcalase 2.
Replacing the kinetic constant values in the Equation 22 and Equation 23 and substituting these expressions into the Equation 19 , provides:. The use of the Equation 25 at the different operating conditions provides the predicted values shown in the Figures 1 and 2 , which is within the range of acceptability verified by the low average relative-error value Under experimental conditions, it was possible to obtain high DH and hydrolysis rates, which are directly dependent on the enzyme concentration and inversely dependent on the substrate concentration.
The kinetics of the hydrolysis reaction followed a substrate inhibition mechanism, which was adjusted through a typical exponential Equation that involves two parameters a and b associated with the kinetic constants Ks, K 2 , and K d under the assumption that there is no product inhibition. The Michaelis-Menten constants in the hydrolysis reaction were determined using the double reciprocal approach of Hanes-Woolf.
Food and Agriculture Organization of the United Nations. Fisheries and Aquaculture topics. Waste management of fish and fish products. Topics Fact Sheets. Shahidi F, Ambigaipalan P. Curr Opin Food Sci. Arvanitoyannis IS. Waste Management for the Food Industries.
Amsterdam: Academic Press. Oxidative stability of mahi mahi red muscle dipped in tilapia protein hydrolysates. Food Chem. Recent advances in food biopeptides: Production, biological functionalities and therapeutic applications. Biotechnol Adv. Protein hydrolysates from animal processing by-products as a source of bioactive molecules with interest in animal feeding.
Food Res Int. Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications. Deraz SF. J Aquat Food Prod T.
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