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Chicory, recognized as a functional food, is increasingly becoming the focus of research. This study aimed to investigate the in vitro impact of gastrointestinal digestion on the composition and bioactive properties of chicory decoction. Chicory flour, derived from the roots, was transformed into an aqueous decoction and was subjected to simulated in vitro human gastrointestinal digestion (SGID). For the first time, the influence of the digestive process on specific classes of bioactive molecules was tracked across different digestive compartments (oral, gastric, and intestinal) using a metabolomic approach. Concurrently, the antioxidant, anti-inflammatory, and intestinal hormone regulation effects were assessed before and after SGID. The findings revealed that specific transformations of chlorogenic acid (CGA) and sesquiterpene lactones (STL) during SGID enhanced antioxidant and anti-inflammatory properties post-digestion. Quantitative results demonstrated a significant increase in ROS scavenging capacity and metabolite activity., Competing Interests: Declaration of competing interest The authors affirm that they do not have any known financial conflicts of interest or personal relationships that could have potentially biased the findings presented in this work., (Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.)

Mass spectrometry has become the technique of choice for the assessment of a high variety of molecules in complex food matrices. It is best suited for monitoring the evolution of digestive processes in vivo and in vitro. However, considering the variety of equipment available in different laboratories and the diversity of sample preparation methods, instrumental settings for data acquisition, statistical evaluations, and interpretations of results, it is difficult to predict a priori the ideal parameters for optimal results. The present work addressed this uncertainty by executing an inter-laboratory study with samples collected during in vitro digestion and presenting an overview of the state-of-the-art mass spectrometry applications and analytical capabilities available for studying food digestion. Three representative high-protein foods - skim milk powder (SMP), cooked chicken breast and tofu - were digested according to the static INFOGEST protocol with sample collection at five different time points during gastric and intestinal digestion. Ten laboratories analysed all digesta with their in-house equipment and applying theirconventional workflow. The compiled results demonstrate in general, that soy proteins had a slower gastric digestion and the presence of longer peptide sequences in the intestinal phase compared to SMP or chicken proteins, suggesting a higher resistance to the digestion of soy proteins. Differences in results among the various laboratories were attributed more to the peptide selection criteria than to the individual analytical platforms. Overall, the combination of mass spectrometry techniques with suitable methodological and statistical approaches is adequate for contributing to the characterisation of the recently defined digestome., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

The gastrointestinal digestion of food proteins can generate peptides with a wide range of biological activities. In this study, we screened various potential bioactivities generated by plant-based proteins. Whey protein as an animal protein reference, five grades of pea protein, two grades of wheat protein, and potato, fava bean, and oat proteins were submitted to in vitro SGID. They were then tested in vitro for several bioactivities including measures on: (1) energy homeostasis through their ability to modulate intestinal hormone secretion, to inhibit DPP-IV activity, and to interact with opioid receptors; (2) anti-hypertensive properties through their ability to inhibit ACE activity; (3) anti-inflammatory properties in Caco-2 cells; (4) antioxidant properties through their ability to inhibit production of reactive oxygen species (ROS). Protein intestinal digestions were able to stimulate intestinal hormone secretion by enteroendocrine cells, to inhibit DPP-IV and ACE activities, to bind opioid receptors, and surprisingly, to decrease production of ROS. Neither pro- nor anti-inflammatory effects have been highlighted and some proteins lost their pro-inflammatory potential after digestion. The best candidates were pea, potato, and fava bean proteins.

Consumers and governments have become aware how the daily diet may affect the human health. All proteins from both plant and animal origins are potential sources of a wide range of bioactive peptides and the large majority of those display health-promoting effects. In the meat production food chain, the slaughterhouse blood is an inevitable co-product and, today, the blood proteins remain underexploited despite their bioactive potentiality. Through a comparative food peptidomics approach we illustrate the impact of resolving power, accuracy, sensitivity, and acquisition speed of low-resolution (LR)- and high-resolution (HR)-LC-ESI-MS/MS on the obtained peptide mappings and discuss the limitations of MS-based peptidomics. From in vitro gastrointestinal digestions of partially purified bovine hemoglobin, we have established the peptide maps of each hemoglobin chain. LR technique (normal bore C18 LC-LR-ESI-MS/MS) allows us to identify without ambiguity 75 unique peptides while the HR approach (nano bore C18 LC-HR-ESI-MS/MS) unambiguously identify more than 950 unique peptides (post-translational modifications included). Herein, the food peptidomics approach using the most performant separation methods and mass spectrometers with high-resolution capabilities appears as a promising source of information to assess the health potentiality of proteins., (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Like their owners, dogs and cats are more and more affected by overweight and obesity-related problems and interest in functional pet foods is growing sharply. Through numerous studies, fish protein hydrolysates have proved their worth to prevent and manage obesity-related comorbidities like diabetes. In this work, a human in vitro static simulated gastrointestinal digestion model was adapted to the dog which allowed us to demonstrate the promising effects of a tilapia byproduct hydrolysate on the regulation of food intake and glucose metabolism. Promising effects on intestinal hormones secretion and dipeptidyl peptidase IV (DPP-IV) inhibitory activity were evidenced. We identify new bioactive peptides able to stimulate cholecystokinin (CCK) and glucagon-like peptide 1 (GLP-1) secretions, and to inhibit the DPP-IV activity after a transport study through a Caco-2 cell monolayer. [ABSTRACT FROM AUTHOR]