Effect of creatine and EDTA supplemented diets on European seabass (Dicentrarchus labrax) allergenicity, fish muscle quality and omics fingerprint.

The relatively easy access to fish worldwide, alongside the increase of aquaculture production contributes to increased fish consumption which result in higher prevalence of respective allergies. Allergies to fish constitute a significant concern worldwide. ß-parvalbumin is the main elicitor for IgE-mediated reactions. Creatine, involved in the muscle energy metabolism, and ethylenediamine tetraacetic acid (EDTA), a calcium chelator, are potential molecules to modulate parvalbumin. The purpose of this study was to test creatine (2, 5 and 8%) and EDTA (1.5, 3 and 4.5%) supplementation in fish diets to modulate ß-parvalbumin expression and structure and its allergenicity in farmed European seabass (Dicentrarchus labrax) while assessing its effects on the end-product quality. Fish welfare and muscle quality parameters were evaluated by plasma metabolites, rigor mortis, muscle pH and sensory and texture analysis. Proteomics was used to assess alterations in muscle proteome profile and metabolic fingerprinting by Fourier transform infrared spectroscopy was used to assess the liver metabolic profile. In addition, IgE-reactivity to parvalbumin was analysed using fish allergic patient sera. Metabolic fingerprinting of liver tissue revealed no major alterations in infrared spectra with creatine supplementation, while with EDTA, only absorption bands characteristic of lipids were altered. Comparative proteomics showed up regulation of (tropo) myosin and phosphoglycerate mutase 2 with Creatine supplementation. In the case of EDTA proteomics showed up regulation of proteins involved in cellular and ion homeostasis. Allergenicity seems not to be modulated with creatine or EDTA supplementation as no decreased expression levels were found and IgE-binding reactivity showed no quantitative differences.

Data on the in-vitro digestibility of acid gels prepared from brewers' spent grain protein isolates.

Brewers' Spent Grain (BSG) is the primary waste of the beer brewing process, which comprises a plethora of nutritionally appealing ingredients such as proteins, dietary fibres, essential lipids and micronutrients. In our previous study [1], the acid-induced gelation capacity of BSG protein isolate as influenced by the thermal pre-treatment severity was systematically investigated. In the present work, we aimed at providing a dataset outlining the gastrointestinal fate of the acid gels under simulating pre-absorptive digestion conditions adopting the INFOGEST static in-vitro digestion protocol. Protein hydrogel digestibility was assessed by quantification of the total soluble nitrogen content in the initial acid gels as well as the obtained gastric and small intestine chymes. The extent of proteolysis occurring in the oral, gastric and intestinal phases was investigated by SDS-PAGE and the molecular weight distribution of the proteins in the obtained gastric chymes and intestinal digesta was determined by image analysis. The dataset can be deployed to assist food scientists in the design and development of alternative protein-based food and food supplement products adopting the "waste-to-fork" concept.

Proteomic responses of carotenoid and retinol administration to Mongolian gerbils.

Various health benefits of carotenoids have been described. However, while human observational studies generally suggest positive health effects, supplementation with relatively high doses of individual carotenoids (supplements) have partly produced adverse effects. In the present study, we investigated the effect of several carotenoids on the proteomic response of male Mongolian gerbils (aged 6 weeks). Five groups of gerbils (n = 6 per group) received either retinol (vitamin A/53 mg per kg bw), all-trans ß-carotene (pro-vitamin A/100 mg kg-1), the non-pro vitamin A carotenoid lutein (100 mg kg-1), the acyclic carotenoid lycopene (100 mg kg-1) or vehicle (Cremophor EL), via oral single gavage. Gerbils were 12 h post-prandially sacrificed and blood plasma, liver, and white adipose tissue were collected. For liver and adipose tissue, a 2D-DIGE (difference gel electrophoresis) approach was conducted; for plasma, proteomic analyses were achieved by liquid chromatography-mass spectrometry. Compared to controls (vehicle), various proteins were showing significant abundance variations in plasma (66), liver (29) and adipose tissue (19), especially regarding structure (22), protein metabolism (15) and immune system/inflammation (19) functions, while proteins related to antioxidant effects were generally less abundant, suggesting no in vivo relevance. Surprisingly, a large overlap in protein regulation was found between lycopene and retinol exposure, while other carotenoids, including all-trans ß-carotene, did not show this overlap. Mainly retinoid acid receptor co-regulated proteins may mechanistically explain this overlapping regulation. This overlapping regulation may be related to common nuclear hormone receptor mediated signalling, though further studies using synthetic ligands of retinoid receptors targeting protein regulation are needed for confirmation.

Proteomic response of inflammatory stimulated intestinal epithelial cells to in vitro digested plums and cabbages rich in carotenoids and polyphenols.

Due to their anti-oxidant and anti-inflammatory potential, polyphenol and carotenoid-rich plant foods have been suggested as promising phytochemicals in the prevention of or as adjuvants regarding inflammatory bowel diseases (IBD). In the present study, we investigated whether plum (Italian Plum, Prunus cocomilla), or cabbage (Kale, Brassica oleracea var. sabellica), selected for their high phytochemical content, are able to reduce inflammation in cellular models of the intestinal epithelium, employing proteomic methods. For this purpose, plum/cabbage (carotenoid content: 1.9 mg per 100 g resp. 13 mg per 100 g; polyphenol content: 83 mg per 100 g resp. 27 mg per 100 g) were gastro-intestinally digested, and aliquots exposed (18 h) to either a monoculture (Caco-2) or a triple culture (Caco-2/HT-29-MTX (90 : 10, v/v) with THP-1 like macrophages), stimulated (with LPS, TNF-α, and IL-1ß) to induce inflammation. Cells (Caco-2, Caco-2/HT-29-MTX, and THP-1) were then harvested separately, and proteomic analyses of total cell extracts were carried out by 2D-DIGE. In the monoculture, 68 protein-spots were significantly (p < 0.05, expression ratio >1.5) differentially regulated due to the Kale and Italian plum digesta, and in the co-culture 206 protein-spots, compared to digesta without plum/cabbage. These belonged to 27 (monoculture) and 76 (coculture) uniquely identified proteins, suggesting the coculture to be a more sensitive model. Proteins included antioxidant enzymes such as catalase, superoxide dismutase and glutathione-S-transferases. Only 3 proteins were differentially regulated in the THP-1 cells, perhaps as these were only indirectly exposed. The results show promise regarding some aspects related to IBD complications, however, employing phytochemical-rich food items should be further investigated in in vivo trials.

Proteomic evaluation of wound-healing processes in potato (Solanum tuberosum L.) tuber tissue.

Proteins from potato (Solanum tuberosum L.) tuber slices, related to the wound-healing process, were separated by 2-DE and identified by an MS analysis in MS and MS/MS mode. Slicing triggered differentiation processes that lead to changes in metabolism, activation of defence and cell-wall reinforcement. Proteins related to storage, cell growth and division, cell structure, signal transduction, energy production, disease/defence mechanisms and secondary metabolism were detected. Image analysis of the 2-DE gels revealed a time-dependent change in the complexity of the polypeptide patterns. By microscopic observation the polyalyphatic domain of suberin was clearly visible by D4, indicating that a closing layer (primary suberisation) was formed by then. A PCA of the six sampling dates revealed two time phases, D0-D2 and D4-D8, with a border position between D2 and D4. Moreover, a PCA of differentially expressed proteins indicated the existence of a succession of proteomic events leading to wound-periderm reconstruction. Some late-expressed proteins (D6-D8), including a suberisation-associated anionic peroxidase, have also been identified in the native periderm. Despite this, protein patterns of D8 slices and native periderm were still different, suggesting that the processes of wound-periderm formation are extended in time and not fully equivalent. The information presented in this study gives clues for further work on wound healing-periderm formation processes.