Kinetics of trypsin-catalyzed hydrolysis determined by isothermal titration calorimetry

Application of ITC in foods: A powerful tool for understanding the gastrointestinal fate of lipophilic compounds

“…For example, ITC has been used to measure enthalpy changes associated with interactions in colloidal systems, such as dissociation of surfactant micelles [26][27][28], binding of surfactants to polymers [29][30][31], adsorption of surface-active molecules to colloidal particles [32][33][34], and partitioning of molecules in aqueous micellar solutions [35,36]. In addition, ITC has previously been used to monitor enzyme hydrolysis reactions [37][38][39], which may be useful for studying the digestion of food components (such as proteins, carbohydrates, and lipids) under simulated GIT conditions.…”

Simple ITC method for activity and inhibition studies on human salivary α-amylase

“…Though numerous papers have already been published on enzyme kinetic measurements using microcalorimetry, only a few very recent articles have dealt with inhibition studies 9,10 . In some cases, product or substrate inhibitions have been studied 5,11,12 , but ITC has scarcely been applied to determine half maximal inhibitory concentration (IC 50 ).…”

In vitro gastric digestion of protein-based structured food : An engineering approach

“…Second, pepsin is more efficient towards protein while less efficient towards smaller peptides when compared to the intestinal proteases. For example, Maximova and Trylska (2015) found very low k cat for trypsincatalyzed hydrolysis of casein (0.01 s −1 ) as the substrate, which is very low compared to our measurement of BSA catalyzed by pepsin in Chapter 5, even if considering that we corrected the k cat with the conversion factor of 'susceptible peptide bonds'. Other studies reported high k cat values for trypsin-catalyzed hydrolysis of certain syn- Stevens and Hume (2004) thetic peptides (Tsunematsu, Imamura, and Makisumi 1983;Sears and Clark 1993).…”