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- Title
Effect of Commercially Utilized Thermal Treatments on Interactions Between Casein and β-lactoglobulin and Their Digestion in Simulated Gastrointestinal Environment.
- Authors
Long, Yingzi; Ruan, Chengcheng; Hu, Bing; Wu, Juqing; Li, Chunbao; Nian, Yingqun
- Abstract
The objective of present study is to investigate and compare the effects of different commercially utilized thermal treatments of 65 ℃ for 30 min, 80 ℃ for 15 s, 95 ℃ for 5 min and 137 ℃ for 5 s on the interactions between casein and β-lactoglobulin (β-LG) and the consequent digestion profile in simulating gastrointestinal (GI) environments. It was demonstrated, by the measurements of turbidity, polyacrylamide gel electrophoresis, and molecular affinity between β-LG and casein, that high temperature (95 ℃ and 137 ℃) or long heating time (30 min) significantly increased the turbidity of β-LG and casein mixture, promoted the self-aggregates of β-LG, and enhanced the complexation of β-LG and κ-casein, as a result of the intermolecular thiol and disulfide interchange, as well as the strong affinity between β-LG and casein. Comparatively, the pasteurization of about 80 ℃ for 15 s decreased the turbidity of the model mixture of β-LG and casein, and did not lead to β-LG and κ-casein aggregates cross-linked with disulfide. In addition, the affinity of the heated casein and β-LG with the thermal treatment of 80 ℃ for 15 s was the lowest compared with the ones shown in the other three treatments. In the simulated gastric condition, the model mixture of β-LG and casein heated at 80 ℃ for 15 s appeared to be digested faster compared with the one treated at 137 ℃ for 5 s. However, this phenomenon could not be observed obviously in the simulated intestinal condition. Therefore, the formation of disulfide between the reactive thiols in denatured β-LG and κ-casein accounts mainly for the β-LG self-aggregates and the β-LG-casein complexes in the commercially utilized thermal treatments. In terms of interactions between β-LG and casein, pasteurization may be considered as an ideal thermal treatment of milk for heating processing, without significant impact on product properties.
- Subjects
LACTOGLOBULINS; CASEINS; HEAT treatment of milk; POLYACRYLAMIDE gel electrophoresis; DAIRY processing; DIGESTION
- Publication
Food Biophysics, 2023, Vol 18, Issue 3, p353
- ISSN
1557-1858
- Publication type
Article
- DOI
10.1007/s11483-023-09776-9