Exploring the dipeptidyl peptidase IV inhibitory potential of probiotic-fermented milk: An in vitro and in silico comprehensive investigation into peptides from milk of different farm animals.

Bioactive peptides produced via enzymatic hydrolysis have been widely investigated for their dipeptidyl peptidase-IV (DPP-IV) inhibitory properties. However, deficit of studies on fermentation as a mean to produce DPP-IV inhibitory peptides prompted us to draw a comparative study on DPP-IV inhibitory peptides generated from cow, camel, goat, and sheep milk using probiotic fermentation. Further, peptide identification, in silico molecular interactions with DPP-IV, and ensemble docking were performed. Results obtained suggested that goat milk consistently exhibited higher hydrolysis than other milk types. Further, Pediococcus pentosaceus (PP-957) emerged as a potent probiotic, with significantly lower DPP-IV-IC50 values 0.17, 0.12, and 0.25 µg/mL protein equivalent in fermented cow, camel, and goat milk, respectively. Overall, peptides (RPPPPVAM, CHNLDELKDTR, and VLSLSQPK) exhibited strong binding affinity with binding energies of -9.31, -9.18 and -8.9 Kcal·mol-1, respectively, suggesting their potential role as DPP-IV inhibitors. Overall, this study, offers valuable information toward antidiabetic benefits of fermented milk products via inhibition of DPP-IV.

Molecular docking studies on α-amylase inhibitory peptides from milk of different farm animals.

Milk-derived peptides have emerged as a popular mean to manage various lifestyle disorders such as diabetes. Fermentation is being explored as one of the faster and efficient way of producing peptides with antidiabetic potential. Therefore, in this study, an attempt was made to comparatively investigate the pancreatic α-amylase (PAA) inhibitory properties of peptides derived from milk of different farm animals through probiotic fermentation. Peptide's identification was carried out using liquid chromatography-quadrupole time-of-flight mass spectrometry and inhibition mechanisms were characterized by molecular docking. Results obtained showed a PAA-IC50 value (the amount of protein equivalent needed to inhibit 50% of enzymes) between 2.39 and 36.1 µg protein equivalent for different fermented samples. Overall, Pediococcus pentosaceus MF000957-derived fermented milk from all animals indicated higher PAA inhibition than other probiotic derived fermented milk (PAA-IC50 values of 6.01, 3.53, 15.6, and 10.8 µg protein equivalent for bovine, camel, goat, and sheep fermented milk). Further, molecular docking analysis indicated that camel milk-derived peptide IMEQQQTEDEQQDK and goat milk-derived peptide DQHQKAMKPWTQPK were the most potent PAA inhibitory peptides. Overall, the study concluded that fermentation derived peptides may prove useful in for managing diabetes via inhibition of carbohydrate digesting enzyme PAA.

In vitro antidiabetic and antihypercholesterolemic activities of camel milk protein hydrolysates derived upon simulated gastrointestinal digestion of milk from different camel breeds.

Milk protein hydrolysates derived from 4 camel breeds (Pakistani, Saheli, Hozami, and Omani) were evaluated for in vitro inhibition of antidiabetic enzymatic markers (dipeptidyl peptidase IV and α-amylase) and antihypercholesterolemic enzymatic markers (pancreatic lipase and cholesterol esterase). Milk samples were subjected to in vitro simulated gastric (SGD) and gastrointestinal digestion (SGID) conditions. In comparison with intact milk proteins, the SGD-derived milk protein hydrolysates showed enhanced inhibition of α-amylase, dipeptidyl peptidase IV, pancreatic lipase, and cholesterol esterase as reflected by lower half-maximal inhibitory concentration values. Overall, milk protein hydrolysates derived from the milk of Hozami and Omani camel breeds displayed higher inhibition of different enzymatic markers compared with milk protein hydrolysates from Pakistani and Saheli breeds. In vitro SGD and SGID processes significantly increased the bioactive properties of milk from all camel breeds. Milk protein hydrolysates from different camel breeds showed significant variations for inhibition of antidiabetic and antihypercholesterolemic enzymatic markers, suggesting the importance of breed selection for production of bioactive peptides. However, further studies on identifying the peptides generated upon SGD and SGID of milk from different camel breeds are needed.

Novel insights on extraction and encapsulation techniques of elderberry bioactive compounds.

BACKGROUND: Elderberry (Sambucus nigra L.) has been used in traditional medicine and as a supplement in many beverages and meals. Elderberry is a good source of bioactive flavonoids like quercetin, kaempferol, and rutin, as well as other phenolic compounds. Extraction techniques significantly influence the efficiency of extraction of bioactive compounds. Green chemistry elements such as safety, environmental friendliness, run-down or at least minimal contaminants, efficiency, and economic criteria should all be addressed by an effective bioactive extraction process. Furthermore, micro/nanoencapsulation technologies are particularly effective for increasing bioavailability and bioactive component stability. SCOPE AND APPROACH: This review article comprehensively describes new developments in elderberry extraction and encapsulation. Elderberry is largely employed in the food and pharmaceutical industries due to its health-promoting and sensory characteristics. Elderberry has traditionally been used as a diaphoretic, antipyretic, diuretic, antidepressant, and antitumor agent in folk medicine. KEY FINDINGS AND CONCLUSIONS: Conventional extraction methods (e.g. maceration and Soxhelt extraction) as well as advanced green techniques (e.g. supercritical fluids, pulsed electric field, emulsion liquid extraction, microwave, and ultrasonic extraction) have been used to extract bioactives from elderberry. Over the other protective measures, encapsulation techniques are particularly recommended to protect the bioactive components found in elderberry. Microencapsulation (spray drying, freeze drying, extrusion, emulsion systems) and nanoencapsulation (nanoemulsions, solid lipid nanoparticles and nanodispersions, nanohydrogels, electrospinning, nano spray drying) approaches for elderberry bioactives have been examined in this regard.

Lactobacillus reuteri-fortified camel milk infant formula: Effects of encapsulation, in vitro digestion, and storage conditions on probiotic cell viability and physicochemical characteristics of infant formula.

Lactobacillus reuteri fortified camel milk infant formula (CMIF) was produced. The effect of encapsulation in different matrices (sodium alginate and galacto-oligosaccharides) via spray drying, simulated infant gastrointestinal digestion (SIGID), and storage conditions (temperature and humidity) on the viability of L. reuteri in CMIF and the physicochemical properties of CMIF were evaluated. Compared with free cells, probiotic cell viability was significantly enhanced against SIGID conditions upon encapsulation. However, L. reuteri viability in CMIF decreased after 60 d of storage, predominantly at higher storage humidity and temperature levels. At the end of the storage period, significant changes in the color values were observed in all CMIF, with a reduction in their greenness, an increase in yellowness, and a wide variation in their whiteness. Moreover, pH values and caking behavior of all CMIF stored at higher temperature (40°C) and humidity [water activity (aw) = 0.52] levels were found to be significantly higher than the samples stored under other conditions. Over 30 d of storage at lower humidity conditions (aw = 0.11 and 0.33) and room temperature (25°C), no significant increase in CMIF lipid oxidation rates was noted. Fourier-transform infrared spectroscopy analysis showed that, compared with the other storage conditions, CMIF experienced fewer changes in functional groups when stored at aw = 0.11. Microscopic images showed typical morphological characteristics of milk powder, with round to spherical-shaped particles. Overall, camel milk fortified with encapsulated L. reuteri can be suggested as a promising alternative in infant formula industries, potentially able to maintain its physicochemical characteristics as well as viability of probiotic cells when stored at low humidity levels (aw = 0.11) and temperature (25°C), over 60 d of storage.

Cow and camel milk-derived whey and casein protein hydrolysates demonstrated effective antifungal properties against selected Candida species.

Bioactive peptides derived from milk proteins are widely known to possess antibacterial activities. Even though the antibacterial effects of milk-derived peptides are widely characterized, not much focus is given to their antifungal characterization. Therefore, in this study, we investigated the antifungal properties of camel and cow whey and casein hydrolysates against various species of pathogenic Candida. The hydrolysates were produced using 2 enzymes (alcalase and protease) at differing hydrolysis durations (2, 4, and 6 h) and tested for their antifungal properties. The results showed that intact cow whey and casein proteins did not display any anti-Candida albicans properties, whereas the alcalase-derived 2 h camel casein hydrolysate (CA-C-A2) displayed a higher percentage of inhibition against Candida albicans (93.69 ± 0.26%) followed by the cow casein hydrolysate generated by protease-6 h (Co-C-P6; 81.66 ± 0.99%), which were significantly higher than that of fluconazole, a conventional antifungal agent (76.92 ± 4.72%). Interestingly, when tested again Candida krusei, camel casein alcalase 2 and 4 h (CA-C-A2 and CA-C-A4), and cow whey alcalase-6 h (CO-W-A6) hydrolysates showed higher antifungal potency than fluconazole. However, for Candida parapsilosis only camel casein alcalase-4 h (Ca-C-A4) and cow casein protease-6 h (Co-C-P6) hydrolysates were able to inhibit the growth of C. parapsilosis by 19.31 ± 0.84% and 23.82 ± 4.14%, respectively, which was lower than that shown by fluconazole (29.86 ± 1.11%). Overall, hydrolysis of milk proteins from both cow and camel enhanced their antifungal properties. Camel milk protein hydrolysates were more potent in inhibiting pathogenic Candida species as compared with cow milk protein hydrolysates. This is the first study that highlights the antifungal properties of camel milk protein hydrolysates.