Influence of bile salts on the gastrointestinal digestion of agar-casein hybrid systems and the nanoassembly of their digestion products.

This manuscript reports on the effect of different bile salts concentration on the gastrointestinal digestion of casein and casein-agar hybrid systems and evaluates the effect on the nanostructural assembly of the digestion products through the application of advanced small angle X-ray scattering analysis (SAXS). The results showed that bile salts promote the hydrolysis of micellar casein upon in vitro gastrointestinal digestions. It is noteworthy that in the presence of agar, bile salts interact with the polysaccharide, leading to a reduction in their proteolytic activity.

Current advances for protein digestibility.

Protein is an essential macronutrient in our diet, source of nitrogen and essential amino acids, but the biological utilization of dietary protein depends on its digestibility and the absorption of amino acids and peptides in the gastrointestinal tract. The methods to define the amount and the quality of protein to meet human nutritional needs, such as the Digestible Indispensable Amino Acid Score (DIAAS), require the use of animal models or human studies. These methods are the reference in protein quality evaluation, but they are expensive and long-lasting procedures with significant ethical restrictions.

In vitro digestibility of proteins from red seaweeds: Impact of cell wall structure and processing methods.

This study aimed to assess the nutritional quality and digestibility of proteins in two red seaweed species, Gelidium corneum and Gracilaropsis longissima, through the application of in vitro gastrointestinal digestions, and evaluate the impact of two consecutive processing steps, extrusion and compression moulding, to produce food snacks. The protein content in both seaweeds was approximately 16 %, being primarily located within the cell walls. Both species exhibited similar amino acid profiles, with aspartic and glutamic acid being most abundant.

CCK and GLP-1 response on enteroendocrine cells of semi-dynamic digests of hydrolyzed and intact casein.

A semi-dynamic gastrointestinal device was employed to explore the link between protein structure and metabolic response upon digestion for two different substrates, a casein hydrolysate and the precursor micellar casein. As expected, casein formed a firm coagulum that remained until the end of the gastric phase while the hydrolysate did not develop any visible aggregate. Each gastric emptying point was subjected to a static intestinal phase where the peptide and amino acid composition changed drastically from that found during the gastric phase.