Journal
FOOD CHEMISTRY
Volume 239, Issue -, Pages 268-275Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.06.115
Keywords
pH-stat; Titrimetry; Pepsin; Aspartic proteases; Proteolysis; Hydrolysis; Whey proteins; In vitro digestion
Funding
- French National Research Agency under the Investissements d'Avenir program [ANR-11-IDEX-0003-02]
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This study intends to demonstrate that acid titration at low pH is very well adapted to the monitoring of pepsin activity. After a description of the underlying principles, this approach was used during in vitro gastric digestions of a model of complex food containing 15 wt% of whey proteins, according to both static (2 h at pH = 3, Infogest protocol) and dynamic pH conditions (from pH 6.3 down to 2 in 1 h). Pepsin activity was quantitatively assessed in all experiments through the calculation of degrees of hydrolysis (DH). Final values of 3.7 and 3.0% were obtained in static and dynamic pH conditions, respectively, and validated using an independent method. Results also show that about 92% of the peptides were detected at pH = 3, and 100% for pH <= 2.5. Overall, the proposed approach proved to be very worthy to study protein hydrolysis during in vitro gastric digestions. (C) 2017 Elsevier Ltd. All rights reserved.
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