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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.

International audience; The identification of phosphopeptides is currently a challenge when they are part of a complex matrix of peptides, such as a milk protein enzymatic hydrolysate. This challenge increases with both the number of phosphorylation sites on the phosphopeptides and their amino acid length. Here, this paper reports a four-phase strategy from an enzymatic casein hydrolysate before a mass spectrometry analysis in order to enhance the identification of phosphopeptides and phosphosites: (i) the control protein hydrolysate, (ii) a two-step enzymatic dephosphorylation of the latter, allowing for the almost total dephosphorylation of peptides, (iii) a one-step enzymatic dephosphorylation, allowing for the partial dephosphorylation of the peptides and (iv) an additional endoGluC enzymatic hydrolysis, allowing for the cleavage of long-size peptides into shorter ones. The reverse-phase high-pressure liquid chromatography–tandem mass spectrometry (RP-HPLC-MS/MS) analyses of hydrolysates that underwent this four-phase strategy allowed for the identification of 28 phosphorylation sites (90%) out of the 31 referenced in UniprotKB/Swiss-Prot (1 June 2021), compared to 17 sites (54%) without the latter. The alpha-S2 casein phosphosites, referenced by their similarity in the UniProt database, were experimentally identified, whereas pSer148, pThr166 and pSer187 from a multiphosphorylated long-size kappa-casein were not. Data are available via ProteomeXchange with identifier PXD027132.

International audience; Protein hydrolysates are, in general, mixtures of amino acids and small peptides able to supply the body with the constituent elements of proteins in a directly assimilable form. They are therefore characterised as products with high nutritional value. However, hydrolysed proteins display an unpleasant bitter taste and possible off-flavours which limit the field of their nutrition applications. The successful identification and characterisation of bitter protein hydrolysates and, more precisely, the peptides responsible for this unpleasant taste are essential for nutritional research. Due to the large number of peptides generated during hydrolysis, there is an urgent need to develop methods in order to rapidly characterise the bitterness of protein hydrolysates. In this article, two enzymatic hydrolysis kinetics of micellar milk caseins were performed for 9 h. For both kinetics, the optimal time to obtain a hydrolysate with appreciable organoleptic qualities is 5 h. Then, the influence of the presence or absence of peptides and their intensity over time compared to the different sensory characteristics of hydrolysates was studied using heat maps, random forests and regression trees. A total of 22 peptides formed during the enzymatic proteolysis of micellar caseins and influencing the bitterness the most were identified. These methods represent simple and efficient tools to identify the peptides susceptibly responsible for bitterness intensity and predict the main sensory feature of micellar casein enzymatic hydrolysates.

International audience; Enzymatic hydrolysis of food proteins generally changes the techno-functional, nutritional, and organoleptic properties of hydrolyzed proteins. As a result, protein hydrolysates have an important interest in the food industries. However, they tend to be characterized by a bitter taste and some off-flavors, which limit their use in the food industry. These tastes and aromas come from peptides, amino acids, and volatile compounds generated during hydrolysis. In this article, sixteen more or less bitter enzymatic hydrolysates produced from a milk protein liquid fraction enriched in micellar caseins using commercially available, food-grade proteases were subjected to a sensory analysis using a trained and validated sensory panel combined to a peptidomics approach based on the peptide characterization by reverse-phase high-performance liquid chromatography, high-resolution mass spectrometry, and bioinformatics software. The comparison between the sensory characteristics and the principal components of the principal component analysis (PCA) of mass spectrometry data reveals that peptidomics constitutes a convenient, valuable, fast, and economic intermediate method to evaluating the bitterness of enzymatic hydrolysates, as a trained sensory panel can do it.

Production of bioactive peptides (BAPs) by Lactobacillus species is a cost-effective approach compared to the use of purified enzymes. In this study, proteolytic Lactobacillus helveticus strains were used for milk fermentation to produce BAPs capable of inhibiting angiotensin converting enzyme (ACE). Fermented milks were produced in bioreactors using batch mode, and the resulting products showed significant ACE-inhibitory activities. However, the benefits of fermentation in terms of peptide composition and ACE-inhibitory activity were noticeably reduced when the samples (fermented milks and non-fermented controls) were subject to simulated gastrointestinal digestion (GID). Introducing an ultrafiltration step after fermentation allowed to prevent this effect of GID and restored the effect of fermentation. Furthermore, an integrated continuous process for peptide production was developed which led to a 3 fold increased peptide productivity compared to batch production. Using a membrane bioreactor allowed to generate and purify in a single step, an active ingredient for ACE inhibition.

In vitro nutritional characterization of milk proteins with different molecular arrangements. 6. International congress on food digestion

International audience

International audience; To compensate for their amino acid auxotrophy, lactobacilli have developed the ability to hydrolyze proteins present in their environment. This proteolytic activity not only generates the free amino acids needed by the bacteria, but also a large variety of peptides, some of which are endowed with biological activities. These so-called "bioactive peptides" (BAPs) are interesting from a nutrition and healthcare perspective. The use of lactic acid bacteria (LAB) such as lactobacilli is an effective strategy for production and valorization of new BAPs. The proteolytic activity of lactobacilli is exerted in a strain-and species-dependent manner: each species exhibits different proteinase content, leading to a large variety of proteolytic activities. This underlines the high potential of Lactobacillus strains to produce novel hydrolysates and BAPs of major interest. This review aims at discussing the potential of different Lactobacillus species to release BAPs from fermentation media and processes. Strategies used for peptide production are presented. Additionally, we propose a methodology to select the most promising Lactobacillus strains as sources of BAPs. This methodology combines conventional approaches and in silico analyses.