Bioactive compounds from date fruit and seed as potential nutraceutical and functional food ingredients

Date palm is an important fruit bearing tree grown widely in the arid and semi-arid regions of the world. The date fruit and its by-products, such as seeds, have both nutritional and medicinal value. However, date fruit and seeds have not been fully considered as potential functional food ingredients to develop foods with promising health benefits. Based on the available information in the literature, fruit and seed of date palm are rich in phytochemicals, such as phenolics, anthocyanin, carotenoids, tocopherols, tocotrienols, phytosterols and dietary fiber. In addition, they were reported to possess several beneficial health properties explored under in-vitro and in-vivo conditions. Further research in this area would provide valuable information for the potential utilization of date fruit and seed as functional food ingredients. This review presents a comprehensive information about the bioactive compounds and nutraceutical properties of different varieties of date fruit and seed, as well as the potential for using them as functional food ingredients

Traditional Fermented Dairy Products in Southern Mediterranean Countries: From Tradition to Innovation

Fermented dairy products have been essential elements in the diet of Southern Mediterranean countries for centuries. This review aims to provide an overview of the traditional fermented products in Southern Mediterranean countries, with a focus on fermented dairy products, and to discuss innovative strategies to make improved versions of these traditional products. A large variety of fermented dairy products were reviewed, showing high diversity, depending on the used raw materials, starter cultures, and preparation procedures. Traditionally, dairy products were fermented using spontaneous fermentation, back-slopping, and/or the addition of rennet. Compared with commercial products, traditional products are characterized by peculiar organoleptic features owing to the indigenous microflora. The main limitation of traditional products is preservation as most products were consumed fresh. In addition to drying, brine or oil was used to extend the product shelf life but resulted in high salt/fat products. Several studies suggested alternative ingredients/processing to make revised products with new flavors, improved nutritional quality, and a longer shelf life. There is still plenty of room for more research to obtain a better understanding of the indigenous microflora and on quality improvement and standardization to reach a wider market

Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel milk protein hydrolysates

Nine novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (FLQY, FQLGASPY, ILDKEGIDY, ILELA, LLQLEAIR, LPVP, LQALHQGQIV, MPVQA and SPVVPF) were identified in camel milk proteins hydrolysed with trypsin. This was achieved using a sequential approach combining liquid chromatography tandem mass spectrometry (LC-MS/MS), qualitative/quantitative structure activity relationship (QSAR) and confirmatory studies with synthetic peptides. The most potent camel milk protein-derived DPP-IV inhibitory peptides, LPVP and MPVQA, had DPP-IV half maximal inhibitory concentrations (IC50) of 87.0 ± 3.2 and 93.3 ± 8.0 µM, respectively. DPP-IV inhibitory peptide sequences identified within camel and bovine milk protein hydrolysates generated under the same hydrolysis conditions differ. This was linked to differences in enzyme selectivity for peptide bond cleavage of camel and bovine milk proteins as well as dissimilarities in their amino acid sequences. Camel milk proteins contain novel DPP-IV inhibitory peptides which may play a role in the regulation of glycaemia in humans

Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel milk protein hydrolysates generated with trypsin

Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel milk proteins. Camel milk was hydrolysed with trypsin using a design of experiments (DOE, temperature (40–60 C), enzyme to substrate (E:S) ratio (0.50–2.00% (w/w)) and time (60–240 min)). Fifteen hydrolysates (H1–H15) having DPP-IV half maximal inhibitory concentration (IC50) values between 0.52 ± 0.06 (H9) and 1.26 ± 0.13 (H1) mg mL 1 were produced. Camel and bovine milk proteins hydrolysed at 40 C, 1.8% E:S and 218 min had DPP-IV IC50 values of 0.68 ± 0.08 and 0.85 ± 0.10 mg mL 1 (p < 0.05), respectively. Potent and unique DPP-IV inhibitory peptides (Leu-Pro-Val-Pro-Gln and Trp-Lys) were identified in camel milk protein hydrolysates, which were not present in bovine milk protein hydrolysates. The DPP-IV inhibitory properties of camel milk peptides were reported for the first time in this study. Camel milk is an interesting substrate to further investigate for its antidiabetic potential