Plant-Based Protein-Phenolic Interactions: Effect on different matrices and in vitro gastrointestinal digestion

Decoding the Duality of Antinutrients: Assessing the Impact of Protein Extraction Methods on Plant-Based Protein Sources

“…As phenolic compounds interact with proteins, this forms a complex that decreases protein digestibility, due to hydrophobic regions that sterically interact and restrict the action of digestive enzymes (Figure ). Strauch and Lila, reported this phenomena on pea protein (pea protein isolate 80%) and cranberry pomace extract, resulting in a decrease of protein digestibility, slower gastric digestion (pepsin <25%) and slower intestinal digestion (pancreatin <35%) …”

“…Additionally, quinones can participate in condensation reactions, culminating in the synthesis of high molecular weight, brown-hued pigments, commonly referred to as tannins. Furthermore, it has been observed that protein-phenolic interactions result in modifications to secondary and tertiary conformations, thermal stability and techno-functional properties . Concurrently, some studies have found a decrease in protein solubility, while thermal stability may exhibit enhancement .…”

“…Furthermore, it has been observed that protein-phenolic interactions result in modifications to secondary and tertiary conformations, thermal stability and techno-functional properties . Concurrently, some studies have found a decrease in protein solubility, while thermal stability may exhibit enhancement . Furthermore, these interactions potentially lead to a decrease in certain amino acid concentrations and a decrement in protein digestibility .…”

“…Furthermore, these interactions potentially lead to a decrease in certain amino acid concentrations and a decrement in protein digestibility . Additionally, protein-phenolic interactions in protein isolates/concentrates can produce an astringent aftertaste, that can be unpleasant for the consumer. , Cosson et al reported that 29 phenolic compounds are related with bitterness and or astringency, in pea protein isolates.…”

Egg White Protein–Proanthocyanin Complexes Stabilized Emulsions: Investigation of Physical Stability, Digestion Kinetics, and Free Fatty Acid Release Dynamics

“…Obviously, the introduction of proanthocyanins could cause a decline in the content of α-helix and β-turn structure while concurrently leading to a rise in the quantity of β-sheet structure (Figure 1j). These variations suggested that interactions between egg white proteins and proanthocyanins could bring about structural changes in the protein, involving both deconstruction and unfolding [22]. Compared with non-covalent complexes, the covalent complexes demonstrated a marked reduction in the content of random coil, which illustrated the development of more organized secondary structures following the covalent binding.…”