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Caron J.,Lille University of Science and Technology | Domenger D.,Lille University of Science and Technology | Belguesmia Y.,Lille University of Science and Technology | Kouach M.,CUMA | And 5 more authors.
Food Research International | Year: 2015

The aim of the present study is to investigate how peptides released by gastrointestinal (GI) digestion of one dietary protein can interact with regulating processes of food intake. An in vitro GI digestion of bovine haemoglobin was carried out and the bioactivity of the digests on CCK and GLP-1 secretion and dipeptidyl peptidase IV (DPP-IV) activity was measured. Intestinal digests exhibited the most potent action on gut hormone release and DPP-IV activity inhibition. They also had the ability to promote hormone gene expression. As a conclusion, two fractions from final intestinal digest led to the greatest GLP-1 secretion increase and DPP-IV activity inhibition. These findings could be very useful in obesity and T2D management research. © 2015 Elsevier Ltd.


PubMed | CNRS Regional Laboratory of Agri-Food and Biotechnology Research: The Charles VIOLLETTE Institute, French Institute of Health and Medical Research and CUMA
Type: Journal Article | Journal: Electrophoresis | Year: 2016

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.

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