In dairy products, the added sodium hyaluronate may form complexes with proteins, thereby affecting product properties. In the present study, the interaction between whey protein isolate (WPI)/ whey protein hydrolysate (WPH) and sodium hyaluronate (SH) was characterized under thermal treatment at different temperatures (25 ℃, 65 ℃, 90 ℃ and 121 ℃) after studying effects of protein/SH ratio and pH on complex formation. The addition of SH reduced the particle size of WPI/WPH and increased potential value in the system, with greater variation with increasing treatment temperature. The structural properties of complexes were studied. The binding with SH decreased the contents of free amino group and free thiol group, as well as the fluorescence intensity and surface hydrophobicity. FTIR results and browning intensity measurement demonstrated the formation of Maillard reaction products. Moreover, the attachment of SH improved the thermal stability of WPI/WPH and decreased their antigenicity.

Whey protein was pretreated with multi-frequency ultrasound in mono-, dual-, and tri-frequency modes. The effect of multi-frequency ultrasound pretreatment on the hardness, chemical forces, and microstructure of acid-induced whey protein gel was investigated. Whey protein gels pretreated with dual- and tri-frequency ultrasound showed higher hardness (p < 0.05) and a denser network than mono-frequency ultrasound and control. Moreover, they had higher hydrophobic interaction and lower disulfide bonds than the control (p < 0.05). The effect of gel properties on digestion was evaluated using an in vitro static model. Whey protein gels pretreated with dual- and tri-frequency ultrasound had a higher proportion of large fragments in the oral boluses than in the control. Large fragments (>3.35 mm) in those samples were resistant to gastric digestion. Moreover, the tri-frequency ultrasound pretreatment of whey protein gel released the least free amino group during gastric digestion. In contrast, whey protein gel with the mono-frequency ultrasound pretreatment released the highest amount of free amino acid group during intestinal digestion. Findings from this study suggests that gel hardness and network density could modulate the digestion behaviors of protein gels.

Whey protein isolate (WPI) is mainly composed of β-lactoglobulin (β-LG), α-lactalbumin (α-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45°C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > α-LA > β-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, H2O2 assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.

Nisin is the first FDA-approved antimicrobial peptide and shows significant antimicrobial activity against Gram-positive bacteria, but only a weakly inhibitory effect on Gram-negative bacteria. The aim of this study was to prepare whey protein-based edible films with the incorporation of milk-derived antimicrobial peptides (αs2-casein151-181 and αs2-casein182-207) and compare their mechanical properties and potential application in cheese packaging with films containing nisin. These two antimicrobial peptides showed similar activity against B. subtilis and much higher activity against E. coli than bacteriocin nisin, representing that these milk-derived peptides had great potential to be applied as food preservatives. Antimicrobial peptides in whey protein films caused an increase in film opaqueness and water vapor barrier properties but decreased the tensile strength and elongation at break. Compared to other films, the whey protein film containing αs2-casein151-181 had good stability in salt or acidic solution, as evidenced by the results from scanning electron microscope and Fourier transform infrared spectroscopy. Whey protein film incorporated with αs2-casein151-181 could inhibit the growth of yeasts and molds, and control the growth of psychrotrophic bacteria present originally in the soft cheese at refrigerated temperature. It also exhibited significant inhibitory activity against the development of mixed culture (E. coli and B. subtilis) in the cheese due to superficial contamination during storage. Antimicrobial peptides immobilized in whey protein films showed a higher effectiveness than their direct application in solution. In addition, films containing αs2-casein151-181 could act as a hurdle inhibiting the development of postprocessing contamination on the cheese surface during the 28 days of storage. The films in this study exhibited the characteristics desired for active packaging materials.

The instability and discoloration of (-)-epigallocatechin-3-gallate (EGCG) constrain its application in functional dairy products. Concurrently, challenges persist in the separation and utilization of whey in the dairy industry. By harnessing the interactions between polyphenols and whey proteins or their hydrolysates, this study proposed a method that involved limited enzymatic hydrolysis followed by the addition of EGCG and pH adjustment around the isoelectric point to obtain whey protein hydrolysates (WPH)-EGCG. Over 92 % of protein-EGCG complexes recovered from whey while ensuring the preservation of α-lactalbumin. The combination between EGCG and WPH depended on hydrogen bonding and hydrophobic interactions, significantly enhanced the thermal stability and storage stability of EGCG. Besides, the intestinal phase retention rate of EGCG in WPH-EGCG complex was significantly increased by 23.67 % compared to free EGCG. This work represents an exploratory endeavor in the improvement of EGCG stability and expanding the utilization approaches of whey.

As glycosylations are difficult to analyze, their roles and effects are poorly understood. Glycosylations in human milk (HM) differ across lactation. Glycosylations can be involved in antimicrobial activities and may serve as food for beneficial microorganisms. This study aimed to identify and analyze O-linked glycans in HM by high-throughput mass spectrometry. 184 longitudinal HM samples from 66 donors from day 3 and months 1, 2, and 3 postpartum were subjected to a post-translational modification specific enrichment-based strategy using TiO2 and ZrO2 beads for O-linked glycopeptide enrichment. β-CN was found to be a major O-linked glycoprotein, additionally, αS1-CN, κ-CN, lactotransferrin, and albumin also contained O-linked glycans. As glycosyltransferases and glycosidases are involved in assembling the glycans including O-linked glycosylations, these were further investigated. Some glycosyltransferases and glycosidases were found to be significantly decreasing through lactation, including two O-linked glycan initiator enzymes (GLNT1 and GLNT2). Despite their decrease, the overall level of O-linked glycans remained stable in HM over lactation. Three different motifs for O-linked glycosylation were enriched in HM proteins: Gly-Xxx-Xxx-Gly-Ser/Thr, Arg-Ser/Thr and Lys-Ser/Thr. Further O-linked glycan motifs on β-CN were observed to differ between intact proteins and endogenous peptides in HM.

UNASSIGNED: To develop Antarctic krill oil emulsions with casein and whey protein concentrate (WPC) and study their physicochemical properties and storage stability.
UNASSIGNED: Emulsions were prepared by homogenisation and ultrasonication. The properties of the emulsions were investigated via ultraviolet ray spectroscopy, dynamic light scattering, confocal laser scanning microscope, sodium dodecyl sulphate-polyacrylamide gel electrophoresis, Fourier transform infra-red spectrometer, and fluorescence spectrum. Shelf life was predicted by the Arrhenius model.
UNASSIGNED: Casein- and WPC-krill oil emulsions were well formed; the mean particle diameters were less than 128.19 ± 0.64 nm and 158 ± 1.56 nm, the polymer dispersity indices were less than 0.26 ± 0.01 and 0.27 ± 0.01, and the zeta potential were around -46.88 ± 5.02 mV and -33.51 ± 2.68 mV, respectively. Shelf life was predicted to be 32.67 ± 1.55 days and 29.62 ± 0.65 days (40 °C), 27.69 ± 1.15 days and 23.58 ± 0.14 days (50 °C), 24.02 ± 0.15 days and 20.1 ± 0.08 days (60 °C).
UNASSIGNED: The prepared krill oil emulsions have great potential to become a new krill oil supplement.

Gut microbiota has been implicated in the initiation and progression of various diseases; however, the underlying mechanisms remain elusive and effective therapeutic strategies are scarce. In this study, we investigated the role and mechanisms of gut microbiota in TNBS-induced colitis and its associated kidney injury while evaluating the potential of dietary protein as a therapeutic intervention. The intrarectal administration of TNBS induced colitis in mice, concurrently with kidney damage. Interestingly, this effect was absent when TNBS was administered intraperitoneally, indicating a potential role of gut microbiota. Depletion of gut bacteria with antibiotics significantly attenuated the severity of TNBS-induced inflammation, oxidative damage, and tissue injury in the colon and kidneys. Mechanistic investigations using cultured colon epithelial cells and bone-marrow macrophages unveiled that TNBS induced cell oxidation, inflammation and injury, which was amplified by the bacterial component LPS and mitigated by thiol antioxidants. Importantly, in vivo administration of thiol-rich whey protein entirely prevented TNBS-induced colonic and kidney injury. Our findings suggest that gut bacteria significantly contribute to the initiation and progression of colitis and associated kidney injury, potentially through mechanisms involving LPS-induced exaggeration of oxidative cellular damage. Furthermore, our research highlights the potential of dietary thiol antioxidants as preventive and therapeutic interventions.

Buffalo colostrum is the initial mammary secretion after parturition, consisting of nutritional and bioactive components. In this study, we conducted a proteomic analysis of buffalo colostrum whey to identify bioactive proteins and peptides. A total of 107 differentially expressed proteins (DEPs) were identified in buffalo colostrum whey compared to those in mature milk. Gene Ontology analysis revealed that DEPs were primarily associated with immune response and tissue development. KEGG pathway enrichment suggested that colostrum actively enhances nascent immunity involved in interleukin and interferon signaling pathways. Furthermore, candidate antimicrobial peptides (AMPs) of whey protein hydrolysates from buffalo colostrum were characterized, which exhibits broad-spectrum activity against gram-positive and gram-negative pathogens. Overall, this study improves our understanding of protein variations in buffalo lactation, and contributes to the development of AMPs from buffalo colostrum.

In this study, a new fermented food was developed using pineapple by-products and whey protein (2.6%) as raw materials through the co-fermentation of autochthonous lactic acid bacteria and yeast. To better understand the fermentation mechanism and the impact of microorganisms on the entire fermentation system, we tracked the changes in carbohydrate and amino acid profiles, organoleptic quality and microbial community during the fermentation process. Compared with unfermented samples, dietary fiber and free amino acids increased significantly as fermentation proceeded. The fermented samples were significantly lower in astringency and bitterness and significantly higher in sourness, umami and richness. The fermented products were richer in volatile compounds with floral, cheesy, fruity and other flavors. Relevant analyses showed that the core microbial community was highly correlated with the quality attributes of the fermented products. Microorganisms such as Lactococcus, Weissella, Hanseniaspora, Saccharomyces and Lachancea contributed significantly to the fermented products.