Publications Repository - Gdańsk University of Technology

We investigated the resistance of individual constituent casein epitopes (αS1-, αS2-, β- and κ-CN) in food-grademilk protein sodium caseinate (NaCN) to simulated human gastro-duodenal digestion. The influence of NaCNadsorption to the surface of oil-in-water emulsion droplets and the effect of crosslinking of the protein withenzyme transglutaminase (TG) on the proteolysis were studied by indirect ELISA. TG crosslinking renderedfragments of casein molecules significantly resistant to digestion. However, it depended on the type of casein andwhether NaCN was presented in solution or emulsion. The crosslinking was found to considerably hinder thedigestion of several amino acid regions in one of the major caseins of NaCN, β-CN. For αS1- and αS2-CN, onlylimited resistance to digestive enzymes was observed after NaCN had been crosslinked in solution but not (or to alimited extent) in emulsion. κ-CN proved to be the least resistant to the enzymatic hydrolysis regardless of the TGtreatment. Our work shows for the first time how the digestibility of individual components of important food-grade protein ingredients can differ in a complex, colloidal food system. It also shows an example of how thedigestibility can be modulated by chemical and physical structuring.

Authors

• Böttger Franziska,
• Dupont Didier,
• Dorota Dulko link open in new tab ,
• Bajka Balazs,
• Alan Mackie,
• dr hab. inż. Adam Macierzanka link open in new tab