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Updated: Apr 24, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
Dry heat stress stability evaluation of casein peptide mixture
Matthias D'Hondt1, Wim Demaré1, Sylvia Van Dorpe1
1Drug Quality and Registration (DruQuaR) Group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.
Abstract:
During food processing, peptide-containing products often experience thermal stress, which can be voluntary heat treatments to prolong expiration date, or unwanted side-effects, e.g. local heating during powder compaction or milling. No information is currently available on the primary structure stability of peptides when heated in the dry state. Therefore, the short-term dry heat stress stability of casein hydrolysate was evaluated by exposure to temperatures of 100, 140 and 180°C during 1, 3 and 5min time intervals. Moreover, the impact of oxidising and reducing agents, as well as photolytic stability were assessed. Contrary to the general belief that peptides are heat-labile, based on degradation results in solution, all peptides remained stable up to 3min at 180°C. The influence of a reducing environment was found to be minimal, while the impact of an oxidising environment was significant. Our findings open perspectives for thermal peptide processing techniques.
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