Maintained particulate integrity of soy protein nanoparticles during gastrointestinal digestion via genipin crosslinking enhancing stability and bioavailability of curcumin.

Poor stability during gastrointestinal digestion is a major challenge for the applications of protein-based nanoparticles as oral delivery systems. In this work, genipin was used to crosslink the partially enzymatic hydrolyzed soy protein nanoparticles, aiming to improve their performance in gastrointestinal tract as delivery carrier. Results showed that the obtained genipin-crosslinked soy protein nanoparticles (GSPNPs) were still spherically monodisperse with a diameter around 60 nm. Encapsulation with GSPNPs significantly improved the solubility of curcumin (Cur) and its stability against UV light as well as long-term storage. Compared to those un-crosslinked nanoparticles, particles crosslinked by genipin had a more compact structure less sensitive to ionic effect and digestive enzymes, showing enhanced digestion stability. The well-maintained nanoparticulate structure of GSPNPs further contributed to the enhanced bioaccessibility and facilitated absorption by epithelial cells. Furthermore, in vivo experiment on rats showed that Cur encapsulated in GSPNPs exhibited a slowed down and sustained absorption manner with an 8.11-fold improvement in its bioavailability. These suggested that GSPNPs could be a promising nanocarrier to enhance the bioavailability of functional factors.

Effects of heat treatment at different moisture of mung bean flour on the structural, gelation and in vitro digestive properties of starch.

Effects of heat treatment (100 °C) at different moisture content (13-70 %) on the structural, gelation and digestive properties of starch in real mung bean flour (MBF) systems are investigated. The results showed that the structural destruction of the starch, the starch-lipid complexion and starch-protein interaction were promoted with increasing moisture content. The starch-protein interaction was mainly driven by hydrophobic interaction forces, leading the increase of total phase transition enthalpy. Even though starch retained ordered structure after heating at 50 %-70 % moisture, the typical pasting curve almost disappeared. The less leached amylose to construct the continuous phase, and more flexible amylopectin swollen granules dispersed in the matrix may weakened the viscoelasticity of the gels. As a result, two distinct gel textures were presented: soft solids with good water-binding capacity (below 30 %) and pasty fluids (above 40 %). Starch-lipid/protein interactions were demonstrated to retard the digestion rate of starch during MBS gelatinization according to the two-stage first-order kinetic and LOS (logarithm of the slope) models.

Characteristics of insoluble soybean fiber (ISF) concentrated emulsions: Effects of pretreatment on ISF and freeze-thaw stability of emulsions.

The properties of emulsions could be affected by the interactions between the components and network stabilization effect, which are commonly adjusted by changes in pH, ionic strength and temperature. In this work, insoluble soybean fiber (ISF) obtained via homogenization after alkaline treatment was pretreated firstly and then resultant emulsions were freeze-thawed. Heating pretreatment reduced droplet size, enhanced viscosity and viscoelasticity as well as subsequent stability of ISF concentrated emulsions, while both acidic pretreatment and salinized pretreatment decreased the viscosity and weakened the stability. Furthermore, ISF emulsions exhibited a good freeze-thaw performance which was further improved by secondary emulsification. Heating promoted the swelling of ISF and strengthened the gel-like structure of emulsions while salinization and acidization weakened the electrostatic interactions and caused the destabilization. These results indicated that pretreatment of ISF significantly influenced the concentrated emulsion properties, providing guidance for the fabrication of concentrated emulsions and related food with designed characteristics.

The intracellular fate and transport mechanism of shape, size and rigidity varied nanocarriers for understanding their oral delivery efficiency.

Nanocarriers have become an effective strategy to overcome epithelial absorption barriers. During the absorption process, the endocytosis mechanisms, cell internalization pathways, and transport efficiency of nanocarriers are greatly impacted by their physical properties. To understand the relationship between physical properties of nanocarriers and their abilities overcoming multiple absorption barriers, nanocarriers with variable physical properties were prepared via self-assembly of hydrolyzed α-lactalbumin peptide fragments. The impacts of size, shape, and rigidity of nanocarriers on epithelial cells endocytosis mechanisms, internalization pathways, transport efficiency, and bioavailability were studied systematically. The results showed that nanospheres were mainly internalized via clathrin-mediated endocytosis, which was then locked in lysosomes and degraded enzymatically in cytoplasm. While macropinocytosis was the primary pathway of nanotubes and transported to the endoplasmic reticulum and Golgi apparatus, resulting in a high drug concentration and sustained release in cytoplasm. Besides, nanotubes can overcome the multi-drug resistance by inhibiting the P-glycoprotein efflux. Furthermore, nanotubes can open intercellular tight-junctions instantaneously and reversibly, which promotes transport into blood circulation. The aqueous solubility of hydrophobic bioactive mangiferin (Mgf) was improved by nanocarriers. Most importantly, the bioavailability of Mgf was the highest for cross-linked short nanotube (CSNT) which outperformed free Mgf and other formulations by in vivo pharmacokinetic studies. Finally, Mgf-loaded CSNT showed an excellent therapeutic efficiency in vivo for the intervention of streptozotocin-induced diabetes. These results indicate that cross-linked α-lactalbumin nanotubes could be an effective nanocarrier delivery system for improving the epithelium cellular absorption and bioavailability of hydrophobic bioactive compounds.

Formation of mucus-permeable nanoparticles from soy protein isolate by partial enzymatic hydrolysis coupled with thermal and pH-shifting treatment.

Modulating the size and surface charge of nanocarriers provides an efficacious strategy to enhance bioavailability of encapsulated cargos through increased mucus penetration. In this study, mucus-permHeable soy protein nanoparticles (SPNPs) were successfully fabricated via gastrointestinal proteolysis coupled with heating and pH-shifting treatment. Results showed that treatment at 65 °C and 75 °C after proteolysis induced the assembly of α, ά, and ß subunits, forming a relatively loose structure. This facilitated further assembly upon pH-shifting, forming smaller-sized and less electronegative nanoparticles, which showed enhanced mucus permeability. However, treatment at 85 °C and 95 °C promoted stronger hydrophobic interactions and induced disulfide bond cross-linking between B and ß subunits, forming compact macro-aggregates with high ß-sheet structure. These larger-sized aggregates were less influenced by pH-shifting treatment, demonstrating limited mucus diffusion. This study provides a potential alternative to fabricate mucus-permeable nanoparticles, and established a relationship between protein subunit assembly behavior and its mucus permeability.

In vitro and in silico analysis of potential antioxidant peptides obtained from chicken hydrolysate produced using Alcalase.

Chicken hydrolysates (CHs) have been reported to protect mice against alcoholic liver injury possibly through oxidative stress reduction. In this study, the antioxidant activity of CHs was studied. Results showed that CHs exhibited significant antioxidant activity (around 600 and 400 µM TEAC/g in ORAC and ABTS assay, respectively) and could resist simulated gastrointestinal digestion. A total of 22 peptides were identified after antioxidant activity-oriented isolation using size-exclusion chromatography and high-performance liquid chromatography. Further in silico analysis and the validation of antioxidant activity revealed that novel peptides (RWGG and YYCQ) exhibited strong antioxidant activity. The most active peptide YYCQ displayed a TEAC value of 3.54 and 4.28 µM TEAC/µM in ORAC and ABTS assay, respectively. These peptides could contribute to reduce oxidative stress and protect against alcohol-induced liver injury. However, further studies understanding the bioactivity of such peptides in vivo are necessary before further applying them as functional food ingredient.

pH-driven-assembled soy peptide nanoparticles as particulate emulsifier for oil-in-water Pickering emulsion and their potential for encapsulation of vitamin D3.

Pickering emulsions prepared by food-grade particles have gained growing attention due to their promising application in functional food and pharmaceutical industries. In this study, we successfully fabricated soy peptide-based nanoparticles (SPN) through pH-driven process. Obtained particles with small particle size were surface active and shared intermediate wettability, and they could be well applied as an efficient particulate emulsifier for stabilizing oil-in-water Pickering emulsions at SPN concentration above 0.25 wt%. Furthermore, formed emulsions stabilized with SPN exhibited good protection towards Vitamin D3 against UV irradiation and oxidative deterioration, where controlled release of Vitamin D3in vitro could also be well achieved by modulating particle concentration. The whole process can contribute to a sustainable development of low-value peptide byproducts as functional food ingredients.

pH-Driven formation of soy peptide nanoparticles from insoluble peptide aggregates and their application for hydrophobic active cargo delivery.

The insoluble soy peptide aggregates formed upon proteolysis are generally considered as "ready to be discarded", which placed additional burden on related industries. In this study, with the aim of promoting sustainable utilization of these large aggregates, novel soy peptide-based nanoparticles (SPN) were successfully fabricated from these aggregates via a controlled pH-shifting method, and the obtained SPN exhibited good storage stability and antioxidant activity. Furthermore, the pH-shifting process also provided a driven force for loading and delivering curcumin, which significantly improved its water solubility (up to 105 folds), storage and simulated gastric-intestinal digestive stability, as well as in vitro bioavailability and antioxidant activity. These results indicated that controlled pH-shifting could be an effective and facile method to trigger the assembly of insoluble aggregates into functional peptide nanoparticles for the delivery of bioactive cargoes, which provided a new strategy for the sustainable and high-value application of these low-value peptide byproducts.

Whipping properties and stability of whipping cream: The impact of fatty acid composition and crystallization properties.

In this study, five fats (hydrogenated palm kernel oil, HPKO-A and HPKO-B; refined vegetable oils, RVO-A and RVO-B; transesterification oil, TO) were used to prepare whipping creams. HPKO-A and RVO-A which rich in lauric and myristic acids facilitated the formation of small crystals and dense crystal network, while higher stearic acid content of HPKO-B formed large spherical crystals. The richness in palmitic acid (RVO-B and TO) and oleic acid (TO) led to the formation of weak crystal network. Higher partial coalescence was correlated to higher collision frequency of fat globules and crystal connection, therefore, the overruns, firmness and stability of creams prepared by HPKO-A and RVO-A were higher than those of HPKO-B and RVO-B. The least stability of cream prepared by TO was related to the weak crystal networks. In summary, higher lauric and myristic acids content resulted in dense crystal networks, promoting partial coalescence and improving the cream quality.

Effect of cooking and in vitro digestion on the peptide profile of chicken breast muscle and antioxidant and alcohol dehydrogenase stabilization activity.

The present study aimed to investigate the effect of cooking and simulated gastrointestinal digestion on the antioxidant and alcohol dehydrogenase (ADH) stabilization activity of peptides extracted from chicken breast muscle. Results showed that cooking would not affect peptide bioactivity, whereas further digestion using gastrointestinal enzymes could lead to significant changes, producing an increase in ORAC (112.5 to 682.0 uM TE/g) and ABTS radical scavenging activities (164.0 to 848.9 uM TE/g), whereas a decrease in DPPH radical scavenging (from 36.1% to 4.4%), ferric-reducing power (OD 700 from 0.50 to 0.15) and ADH stabilization activities (from 44.1% to 20.5%) was observed. The peptidomic analysis resulted in the identification and relative quantitation of 777 peptides from 76 different parent proteins and evidenced that peptides derived from titin and collagen were mainly responsible for the differences detected in the peptide profile. The decrease of DPPH radical scavenging, ferric reducing power, and ADH stabilization activity may result from the release of inactive peptides containing oxidized residues, mainly from collagen, leading to the loss of efficacy of active sequences. The results confirmed the importance of collagen derived peptides on the antioxidant and ADH stabilization activity observed in chicken breast as well as the negative impact of oxidation on the bioactivity of generated peptides after simulated gastrointestinal digestion. Nevertheless, further work would be needed to confirm the peptide sequences responsible for the observed bioactivity.

Chicken breast-derived alcohol dehydrogenase-activating peptides in response to physicochemical changes and digestion simulation: The vital role of hydrophobicity.

Chicken breast muscle hydrolysates (CBMHs) could promisingly activate alcohol dehydrogenase (ADH) and ameliorate alcohol-induced liver injury. The aim of this work was to investigate the stability of CBMHs against physicochemical treatments and gastrointestinal digestion simulation. Results indicated that CBMHs showed good stability towards heating (25-121 °C), pH treatment (pH 2-12) and remained stable in the presence of NaCl (0.01-2 M) and low concentration of metal ions (0.1 mM Zn2+, Ca2+, Fe2+, and Fe3+). Results from in vitro digestion implied a retained activity of CBMHs after gastric tract, but marked decrease (33.42%) after intestinal tract. UPLC-ESI-Q-ToF-MS/MS analysis together with in silico assessments then revealed that the degradation of hydrophobic peptides (i.e., VAPEEHPTLL, YPGIADRM, ADGPLKGIL, and KDLFDPVIQ) during simulated intestinal digestion may be account for the decreased activity. Conformational changes of ADH upon hydrophobic interaction with synthetic peptides were further confirmed by fluorescence quenching study, possibly responsible for the enhanced ADH activity. Hence, CBMHs noticeably showed good stability against physicochemical treatments and digestion simulation, while attempt establishing the structure-activity relationship of peptides is also fundamental before applying CBMHs as functional ingredient.

Data on bioactive peptides derived from chicken hydrolysate with potential alcohol dehydrogenase stabilizing activity and in silico analysis of their potential activity and applicability.

Bioactive peptides have attracted extensive attention worldwide as natural alternatives to promote human health and wellness. Previous studies have shown that chicken hydrolysates could enhance alcohol dehydrogenase, and subsequently they facilitate alcohol metabolism and ameliorate alcohol-induced liver injury. The data presented in this article support the accompanying research article "Isolation and identification of alcohol dehydrogenase stabilizing peptides from Alcalase digested chicken breast hydrolysates". Present article details all 82 peptides identified from the most active fractions of chicken hydrolysates, and 154 peptides from in silico digestion of the 82 identified peptides, together with the prediction of their potential bioactivity and applicability using several in silico assays.

Antioxidant efficiency and mechanisms of green tea, rosemary or maté extracts in porcine Longissimus dorsi subjected to iron-induced oxidative stress.

Plant extracts from rosemary (RE), green tea (GTE), and maté (ME) were compared for the protection against iron-induced oxidation in porcine homogenates at total phenolic concentrations from 25 to 250 ppm. Lipid oxidation as indicated by TBARS was in all cases sufficiently suppressed, especially for RE. Hydrophobic RE retarded overall oxidation in the homogenates with an inverted dose-dependent response. Optimum delay of oxygen consumption was found at the lowest concentration applied, similar to protection against thiols and formation of protein radicals as measured by ESR, whereas the high concentration increased oxygen consumption and caused additionally thiol loss possibly due to thiol-quinone interactions, generating protein-phenol complexes. Hydrophilic ME or GTE increased the initial oxygen consumption rate as an indication of prooxidant activities at elevated concentrations. However, they were found to protect myoglobin and protein at those high concentrations with GTE being more efficient, possibly due to better chelation effect.

In Vitro Digestion and Fermentation of Three Polysaccharide Fractions from Laminaria japonica and Their Impact on Lipid Metabolism-Associated Human Gut Microbiota.

Our previous study has proved that the three polysaccharide fractions from L. japonica (LP-A4, LP-A6, and LP-A8) had significantly different structure characterization. Herein, we conducted in vitro simulated digestion and fermentation to study the digestive mechanism of LP-As. The results of gastrointestinal digestion indicated that LP-A6 and LP-A8 would be easier to trap the enzyme molecules for their denser interconnected macromolecule network compared with LP-A4. Fermentation of LP-As by human gut microbiota, especially for LP-A8, generated a large amount of short-chain fatty acids (SCFAs), which could upregulate the abundance of Firmicutes ( Lachnoclostridium and Eubacterium). The high content of sulfate and highly branched sugar residue of LP-A8 might help it be easily used by Firmicutes in gut microbiota of hyperlipidemic patients. Functional analysis revealed that the increased metabolic activities of glycerophospholipid metabolism, ether lipid metabolism, and fatty acid metabolism induced by LP-A8 treatment were closely associated with metabolic syndromes and hyperlipidemia.

Alcalase-hydrolyzed oyster (Crassostrea rivularis) meat enhances antioxidant and aphrodisiac activities in normal male mice.

The antioxidant and aphrodisiac properties of oyster meat (OM) and its hydrolysates by alcalase (OMA) were compared. The results showed that OMA displayed a higher antioxidant activity than OM with or without gastrointestinal digestion. Furthermore, the study reported that oral administration of OM or OMA could induce aphrodisiac activities and consequently enhance the sexual behavior in normal male mice, at a dose of 250 mg/kg. Additionally, OMA also exhibited better antioxidant activity in vivo than OM by improving the activities of the endogenous cellular antioxidant enzymes and decreasing the MDA levels, which may be helpful in improving the sexual function. These results indicated that oysters' could be a potential functional ingredient with antioxidant and aphrodisiac activities, and the activities could be improved by alcalase hydrolysis.

Protective Effect of Bovine Elastin Peptides against Photoaging in Mice and Identification of Novel Antiphotoaging Peptides.

This study aimed to investigate the protective effects of bovine elastin hydrolysates on UV-induced skin photoaging in mice and to identify the potent antiphotoaging peptides. Results showed that the ingestion of elastin peptides could obviously ameliorate epidermis hyperplasia and fibroblast apoptosis, and increase the content of hydroxyproline and water in photoaging skin in vivo ( p < 0.05). Furthermore, four peptides with elastase inhibitory activity were purified and identified, including GLPY, PY, GLGPGVG, and GPGGVGAL. Interestingly, GLPY and GPGGVGAL exhibited the highest inhibition activity with 58.77% and 42.91% at 10 mΜ, respectively. This might be attributed to the N-terminal Gly, C-terminal Leu, and Pro at the third position of the N-terminus, which showed stronger affinity and interaction with elastase. Moreover, GLPY and GPGGVGAL could also inhibit the apoptosis of fibroblasts effectively at 50 µΜ ( p < 0.01). It suggested that elastin peptides had great potential to prevent and regulate skin photoaging.

Interaction of ß-conglycinin with catechin-impact on physical and oxidative stability of safflower oil-in-water emulsion.

The study aimed at improving the antioxidant activity of ß-conglycinin to enhance the oxidative and physical stabilities of safflower oil-in-water emulsion stabilized by ß-conglycinin. Heating promoted binding affinity and antioxidant activity of ß-conglycinin. Catechin and chlorogenic acid showed higher binding affinities towards unheated (or heated) ß-conglycinin than caffeic acid and quercetin. The enhancement efficiencies of the phenolics on the antioxidant activity of unheated (or heated) ß-conglycinin decreased in the order of catechin > quercetin > chlorogenic acid > caffeic acid. Hydrophobic force and hydrogen bonding were the important binding forces for the selected phenolics to ß-conglycinin. The complexation with catechin has no side effect on interfacial behavior and emulsifying property of ß-conglycinin. The use of heated ß-conglycinin-catechin complex as an emulsifier for preparing safflower oil emulsion effectively improved the oxidative and physical stabilities of the emulsion treated with lipoxygenase through inhibition of lipid oxidation, protein carbonyl formation and sulfhydryl loss.

Development of a Sono-Assembled, Bifunctional Soy Peptide Nanoparticle for Cellular Delivery of Hydrophobic Active Cargoes.

Soy proteins are prone to aggregate upon proteolysis, hindering their sustainable development in food processing. Here, a continuous work on the large insoluble peptide aggregates was carried out, aiming to develop a new type of soy peptide-based nanoparticle (SPN) for active cargo delivery. Sono-assembled SPN in spherical appearance and core-shell structure maintained by noncovalent interactions was successfully fabricated, exhibiting small particle size (103.95 nm) in a homogeneous distribution state (PDI = 0.18). Curcumin as a model cargo was efficiently encapsulated into SPN upon sonication, showing high water dispersity (129.6 mg/L, 104 higher than its water solubility) and storage stability. Additionally, the pepsin-resistant SPN contributed to the controlled release of curcumin at the intestinal phase and thus significantly improved the bioaccessibility. Encapsulated curcumin was effective in protecting glutamate-induced toxicity in PC12 cells, where the matrix SPN can simultaneously reduce lipid peroxidation and elevate antioxidant enzymes levels, innovatively demonstrating its bifunctionality during cellular delivery.

Particulate nanocomposite from oyster (Crassostrea rivularis) hydrolysates via zinc chelation improves zinc solubility and peptide activity.

An oyster protein hydrolysates-zinc complex (OPH-Zn) was prepared and investigated to improve zinc bioaccessibility. Zinc ions chelating with oyster protein hydrolysates (OPH) cause intramolecular and intermolecular folding and aggregation, homogeneously forming the OPH-Zn complex as nanoclusters with a Z-average at 89.28 nm (PDI: 0.16 ±â€¯0.02). The primary sites of zinc-binding in OPH were carboxyl groups, carbonyl groups, and amino groups, and they were related to the high number of charged amino acid residues. Furthermore, formation of the OPH-Zn complex could significantly enhance zinc solubility both under specific pH conditions as well as during simulated gastrointestinal digestion, compared to the commonly used ZnSO4. Additionally, after digestion, either preserved or enhanced antioxidant activity of OPH was found when chelated with zinc. These results indicated that the OPH-Zn complex could be a potential functional ingredient with improved antioxidant bioactivity and zinc bioaccessibility.

Long-Lived and Thermoresponsive Emulsion Foams Stabilized by Self-Assembled Saponin Nanofibrils and Fibrillar Network.

Nanofibrils from the self-assembly of the naturally occurring saponin glycyrrhizic acid (GA) can be used to produce an oil-in-water emulsion foam with a long-term stability. Through homogenization and aeration followed by rapid cooling, stable emulsion foams can be produced from the mixtures of sunflower oil and saponin nanofibrils. At high temperatures, the GA fibrils form a multilayer assembly at the interface, creating an interfacial fibrillar network to stabilize the oil droplets and air bubbles generated during homogenization. A subsequent rapid cooling can trigger the self-assembly of free GA fibrils in the continuous phase, forming a fibrillar hydrogel and thus trapping the oil droplets and air bubbles. The viscoelastic bulk hydrogel showed a high yield stress and storage modulus, which lead to a complete arrest of the liquid drainage and a strong slowdown of the bubble coarsening in emulsion foams. The jamming of the emulsion droplets in the liquid channels as well as around the bubbles was also found to be able to enhance the foam stability. We show that such stable foam systems can be destroyed rapidly and on demand by heating because of the melting of the bulk hydrogel. The reversible gel-sol phase transition of the GA hydrogel leads to thermoresponsive emulsion foams, for which the foam stability can be switched from stable to unstable states by simply raising the temperature. The emulsion foams can be further developed to be photoresponsive by incorporating internal heat sources such as carbon black particles, which can absorb UV irradiation and convert the absorbed light energy into heat. This new class of smart responsive emulsion foams stabilized by the natural, sustainable saponin nanofibrils has potential applications in the food, pharmaceutical, and personal care industries.