Impact of acidic and basic pH on the interfacial shear rheology and foaming properties of transglutaminase cross-linked casein micelle: Structure-function relationship

This work investigated the pH effect (pH 3.5 to 9.0) on the interfacial behavior of native and transglutaminase cross-linked (TGase) caseins films at air-water interface using a rotational rheometer equipped with a BiCone geometry. Both caseins formed a viscous-like interfacial adsorbed layer within the range of frequency from 0.1 to 10 rad/s, with a maxima viscoelastic layer at alkaline pH (8.0 and 9.0). TGase caseins exhibited the highest interfacial shear surface moduli values, and the difference between them was pronouncedly, under acid pH conditions (3.5 to 5.5). The conformational studies revealed the pH and transglutaminase cross-linking effect on the protein structure. The foaming properties suggested a weakening and strengthening of foaming capacity and stability, respectively, by TGase in alkaline pH conditions. The combination of pH-shifting and transglutaminase treatment, especially, under alkaline pH conditions might be applied to improve the casein ability to stabilize the foams in several food applications.

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Publication Details

Journal
Food Chemistry
Published
2025-02-13
DOI
https://doi.org/10.1016/j.foodchem.2025.143384
Citations
3
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
3.49
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article

Impact of acidic and basic pH on the interfacial shear rheology and foaming properties of transglutaminase cross-linked casein micelle: Structure-function relationship

Gaoussou Karamoko, Christine Chèné, Romdhane Karoui
3 citations
Food Chemistry
Proteins in Food Systems
3.49
article

Impact of acidic and basic pH on the interfacial shear rheology and foaming properties of transglutaminase cross-linked casein micelle: Structure-function relationship

Gaoussou Karamoko, Christine Chèné, Romdhane Karoui
article en
3 citations

Abstract

This work investigated the pH effect (pH 3.5 to 9.0) on the interfacial behavior of native and transglutaminase cross-linked (TGase) caseins films at air-water interface using a rotational rheometer equipped with a BiCone geometry. Both caseins formed a viscous-like interfacial adsorbed layer within the range of frequency from 0.1 to 10 rad/s, with a maxima viscoelastic layer at alkaline pH (8.0 and 9.0). TGase caseins exhibited the highest interfacial shear surface moduli values, and the difference between them was pronouncedly, under acid pH conditions (3.5 to 5.5). The conformational studies revealed the pH and transglutaminase cross-linking effect on the protein structure. The foaming properties suggested a weakening and strengthening of foaming capacity and stability, respectively, by TGase in alkaline pH conditions. The combination of pH-shifting and transglutaminase treatment, especially, under alkaline pH conditions might be applied to improve the casein ability to stabilize the foams in several food applications.

Food ChemistryVol. 476
Université de Lille (FR), Institut Charles Viollette (FR), Adrianor (FR), Université d'Artois (FR)
Clean water and sanitation
Openalex Percentile: Top 10%
Proteins in Food Systems
3.49
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Impact of acidic and basic pH on the interfacial shear rheology and foaming properties of transglutaminase cross-linked casein micelle: Structure-function relationship — Gaoussou Karamoko, Christine Chèné, et al. · Food Chemistry (2025) | TGRS Research Map | TGRS