In this study, the effect of in vitro gastrointestinal digestion of phenolic compounds, the total phenolic content, and the antioxidant potential of stingless bee honey were investigated. Among the 33 phenolic compounds investigated, 25 were quantified, and only eight were not bioaccessible (p-aminobenzoic acid, sinapic acid, pinobanksin, isorhamnetin, quercetin-3-glucoside, syringaldehyde, coumarin, and coniferaldehyde). Benzoic acid was predominant in most undigested samples (21.3 to 2414 μg 100 g-1), but its bioaccessibility varied widely (2.5 to 534%). Rutin, a glycosylated flavonoid, was quantified in all samples and might have been deglycosylated during digestion, increasing the bioaccessibility of quercetin in a few samples. Overall, the concentration of phenolic compounds prior digestion and their bioaccessibility varied greatly among samples. Nevertheless, higher concentrations before digestion were not correlated to greater bioaccessibility. This study is the first to assess the in vitro bioaccessibility of phenolic compounds in SBH, providing novel insights into SBH research.

Nowadays, the development of suitable strategies for the management and valorization of agri-food products is one of the most important challenges worldwide. In this context, the current research study aimed to explore a valorization strategy for different varieties (Khalas, Jabri, Lulu, Booman, and Sayer) of low-grade date fruit by extracting polyphenolic compounds and investigating their health-promoting bioactive properties. The generated extracts were comparatively analyzed for their phenolic contents, antioxidant, anti-inflammatory, anti-hemolytic, and enzyme inhibitory activities upon in vitro simulated gastrointestinal digestion (SGID). The total phenolic contents (TPC) ranged from 217.3 to 1846.9 mg GAE/100 g fresh weight. After complete SGID, the TPC remarkably increased from 570.8 mg GAE/100 g fresh weight (undigested), reaching the highest value of 1606.3 mg GAE/100 g fresh weight with the Khalas cultivar. Overall, gastric and complete-SGID-treated extracts exhibited higher antioxidant activities, compared to the undigested extracts for the five selected date varieties. Similarly, the gastric and complete SGID promoted the release of bioactive components endowed with significantly higher inhibition levels towards digestive enzymes related to diabetes. Moreover, extracts from all varieties revealed an increase in the inhibition of lipidemic-related enzymatic markers and anti-inflammatory activities when subjected to the gastric digestion phase, which decreased after complete SGID. Principal component analysis (PCA) suggested that higher bioactive properties were influenced by the TPC present in the samples. Overall, low-quality dates could be considered as a potential source of bioactive polyphenols with interesting nutraceutical properties, released upon their transit through the gastrointestinal tract.

In this study, microcapsules of Lactobacillus plantarum CICC 20022 (L. plantarum CICC 20022) were prepared by extrusion technique using sodium alginate (SA), sodium alginate-sodium caseinate (SA-SC) and sodium alginate-whey protein isolate (SA-WPI) as wall materials, respectively. Results showed that the best encapsulation yield of L. plantarum CICC 20022 was SA-WPI. Morphology and texture analysis showed that the microcapsules prepared by the SA-WPI system presented a more compact internal structure and higher resistance to external pressure. Fourier-transform infrared spectroscopy and low field nuclear magnetic resonance analysis demonstrated that the hydrogen bonding ability and network structure of the SA were improved by the addition of WPI. The survivability of L. plantarum CICC 20022 entrapped with the SA-WPI system was improved during freeze-drying and simulated gastrointestinal digestion. Therefore, the SA-WPI system can potentially be used as the vector of L. plantarum CICC 20022 in food applications.
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The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.