Whey Protein Sodium-Caseinate as a Deliverable Vector for EGCG: In Vitro Optimization of Its Bioaccessibility, Bioavailability, and Bioactivity Mode of Actions.

Epigallocatechin gallate (EGCG), the principal catechin in green tea, exhibits diverse therapeutic properties. However, its clinical efficacy is hindered by poor stability and low bioavailability. This study investigated solid particle-in-oil-in-water (S/O/W) emulsions stabilized by whey protein isolate (WPI) and sodium caseinate (NaCas) as carriers to enhance the bioavailability and intestinal absorption of EGCG. Molecular docking revealed binding interactions between EGCG and these macromolecules. The WPI- and NaCas-stabilized emulsions exhibited high encapsulation efficiencies (>80%) and significantly enhanced the bioaccessibility of EGCG by 64% compared to free EGCG after simulated gastrointestinal digestion. Notably, the NaCas emulsion facilitated higher intestinal permeability of EGCG across Caco-2 monolayers, attributed to the strong intermolecular interactions between caseins and EGCG. Furthermore, the emulsions protected Caco-2 cells against oxidative stress by suppressing intracellular reactive oxygen species generation. These findings demonstrate the potential of WPI- and NaCas-stabilized emulsions as effective delivery systems to improve the bioavailability, stability, and bioactivity of polyphenols like EGCG, enabling their applications in functional foods and nutraceuticals.

Ammonia-Responsive Colorimetric Film of Phytochemical Formulation (Alizarin) Grafted onto ZIF-8 Carrier with Poly(vinyl alcohol) and Sodium Alginate for Beef Freshness Monitoring.

In this study, we devised a photothermally stable phytochemical dye by leveraging alizarin in conjunction with the metal-organic framework ZIF-8 (AL@ZIF-8). The approach involved grafting alizarin into the microporous structure of ZIF-8 through physical adsorption and hydrogen-bonding interactions. AL@ZIF-8 significantly enhanced the photostability and thermostability of alizarin. The nanoparticles demonstrate substantial color changes in various pH environments, showcasing their potential for meat freshness monitoring. Furthermore, we introduced an intelligent film utilizing poly(vinyl alcohol)-sodium alginate-AL@ZIF-8 (PA-SA-ZA) for detecting beef freshness. The sensor exhibited a superior water contact angle (52.34°) compared to the alizarin indicator. The color stability of the film was significantly enhanced under visible and UV light (ΔE < 5). During beef storage, the film displayed significant color fluctuations correlating with TVB-N (R2=0.9067), providing precise early warning signals for assessing beef freshness.

RuBisCo can conjugate and stabilize peonidin-3-O-p-coumaroylrutinoside-5-O-glucoside in isotonic sport models: Mechanisms from kinetics, multispectral, and libDock assays.

The co-pigmentation behaviour of RuBisCo proteins (with different concentrations) on peonidin-3-O-p-coumaroylrutinoside-5-O-glucoside (P3C5G, extracted from Rosetta potato's peels) conjugates in isotonic sport drinks (ISD) was examined using multispectral, thermal stability kinetics, and libDock-based molecular docking approaches. The colorant effects of RuBisCo on P3C5G were also studied in spray-dried microencapsulated ISD-models. RuBisCo, especially at a concentration of 10 mg/mL in ISD, showed a co-pigmentation effect on the color of P3C5G, mostly owing to its superior hyperchromicity, pKH-levels, and thermal stability. Results from multispectral approaches also revealed that RuBisCo could noncovalently interact with P3C5G as confirmed by libDock findings, where P3C5G strongly bound with RuBisCo via H-bonding and π-π forces, thereby altering its secondary structure. RuBisCo also preserved color of P3C5G in ISD-powdered models. These detailed results imply that RuBisCo could be utilized in ISD-liquid and powder models that might industrially be applied as potential food colorants in products under different conditions.

Effect of sono-pre-texturization on ß-lactoglobulin-anthocyanins energy appetizers.

The occurring of glycation reaction and protein-protein interaction in the energy appetizers caused browning and hardness instability while storing these appetizers, leading to the loss of consumer acceptability. Amassing among anthocyanins and proteins could mitigate the appetizers' instability. We, therefore, investigated the anti-aggregation and ant-glycoxidation impacts of mulberry anthocyanins combined with ultrasonic treatment (UT) pre-texturization in an energy appetizer model throughout storage via multi-dimensional methods, containing UPLC-ESI-MS/MS, SDS-PAGE, FTIR, texture analyser, and a molecular docking analysis. Results noted that UT-anthocyanins significantly downgraded the browning progress, advanced glycation end-products, and/or N-(carboxymethyl)-l-lysine intensities of energy appetizers after 45 d of storage at 45 °C. UT-anthocyanins also relegated the protein insolubility, accumulation, oligomerization, and glycoxidation throughout the late storage. A molecular docking analysis evidenced that cyanidin 3-O-glucoside and cyanidin 3-O-rutinoside networked with ß-lactoglobulin subunits via H-bonding and π-π forces. This binding hindered some glycoxidation residues of ß-lactoglobulin the lysyl residues. Finally, these findings recommended that the UT-anthocyanins could be employed as an encouraging antiglycative approach to alleviate AGEs-creation and other consequent undesirable fluctuations in protein-rich food patterns, thereby enhancing the energy appetizer's post-processing stability during storage.

Polyacylated anthocyanins constructively network with catalytic dyad residues of 3CLpro of 2019-nCoV than monomeric anthocyanins: A structural-relationship activity study with 10 anthocyanins using in-silico approaches.

Coronavirus epidemic 2019 (COVID-19), caused by novel coronavirus (2019-nCoV), is newly increasing worldwide and elevating global health concerns. Similar to SARS-CoV and MERS-CoV, the viral key 3-chymotrypsin-like cysteine protease enzyme (3CLPro), which controls 2019-nCoV duplications and manages its life cycle, could be pointed as a drug discovery target. Herein, we theoretically studied the binding ability of 10 structurally different anthocyanins with the catalytic dyad residues of 3CLpro of 2019-nCoV using molecular docking modelling. The results revealed that the polyacylated anthocyanins, including phacelianin, gentiodelphin, cyanodelphin, and tecophilin, were found to authentically bind with the receptor binding site and catalytic dyad (Cys145 and His41) of 2019-nCoV-3CLpro. Our analyses revealed that the top four hits might serve as potential anti-2019-nCoV leading molecules for further optimization and drug development process to combat COVID-19. This study unleashed that anthocyanins with specific structure could be used as effective anti-COVID-19 natural components.

Phytosterols disaggregate bovine serum albumin under the glycation conditions through interacting with its glycation sites and altering its secondary structure elements.

Discovering small molecules with protein-disaggregation effects is recently needed. For the first time, we intensely studied the anti-amyloidogenic effects of 3 structurally different phytosterols (PS), namely stigmasterol, ß-sitosterol, and γ-oryzanol, on bovine serum albumin (BSA) under aggregations-promoting conditions using multispectral, microstructure, and molecular docking methods. Results found that PS dose- and structure- dependently inhibited BSA-aggregations under the glycation conditions through separating BSA-peak size, quenching Tryptophan-intensity, altering BSA-hydrophobicity, and microstructural declining the aggregates of glycated-BSA. Throughout the underlying mechanism beyond its disaggregation effects, PS reformed cross-ß-sheet structure, SDS-PAGE-bands, and XRD-peaks of glycated-BSA aggregates. Most importantly, PS were found to bind with some lysyl and arginine glycation sites of BSA, specifically Lys114, Lys116, Lys136, Lys431, Arg427, and Arg185, via Hydrogen-bonding with their -OH-groups and pi-pi interactions of their steroid core. Taken together, the current results unleash that PS could restrict BSA-aggregations under the glycation conditions and their subsequent changes, which can assist in the design of reasonable therapeutics.

Cyanidin 3-rutinoside defibrillated bovine serum albumin under the glycation-promoting conditions: A study with multispectral, microstructural, and computational analysis.

Findings small molecules with protein disaggregation effects are lately needed. For the first time, we studied the in vitro-antifibrillogenic effects of cyanidin 3-rutinoside (C3R), purified from mulberry fruits, on bovine serum albumin (BSA) under aggregation-promoting conditions, using multispectral, microstructure, and molecular docking approaches. Results showed that C3R dose-dependently inhibited BSA-aggregations under the glycation conditions through separating the size peak, influencing Trp-intensity and hydrophobicity, affecting cross-ß-sheet conformations, and microstructural declining the aggregates of glycated-BSA. Throughout the underlying mechanism behind the disaggregation effects, C3R altered the secondary structure, SDS-PAGE-bands, and XRD-peaks of glycated-BSA aggregates, as well as interacted with some of lysyl and arginine (Lys114, Lys431, Arg427, and Arg185) glycation sites of BSA. Overall, these results unleash that monomeric anthocyanins restrict BSA-aggregations under the glycation conditions which can assist in the design of reasonable therapeutics and functional foods.

In vitro evaluation of anti-methylglyoxal/glyoxal activity of three phytosterols using glycated bovine serum albumin models.

Reactive intermediate dicarbonyls, such as methylglyoxal (MGO) and glyoxal (GO), have received extensive attention recently due to their high reactivity and capability to form advanced glycation end products (AGEs) in foods, which have been implicated in the progression of age-related complaints. We aimed to investigate the effects of three structurally different phytosterols (PS), including stigmasterol (SS), ß-sitosterol (ßS), and γ-oryzanol (γO), on AGEs-formation by measuring their anti-GO/MGO activity. The glycoxidation-based products, SDS-PAGE intensity, free lysine, protein thiols, fluorescence microscopy clicks, scavenging of dicarbonyl activity, and protein aggregation in bovine serum albumin (BSA) models were therefore measured. The results showed that PS could strongly inhibit fluorescent-AGEs, lysine residues, intermediate di-carbonyls, beside their disaggregation effects in a dose and structure dependent manner. Additionally, γ-oryzanol strongly inhibited AGEs more than the other PS, mostly due to its distinctive structure. Our results will provide a new foundation for development of different structure of PS as natural AGEs-inhibitors.

The noncovalent conjugations of bovine serum albumin with three structurally different phytosterols exerted antiglycation effects: A study with AGEs-inhibition, multispectral, and docking investigations.

The antiglycation effects of three structurally different phytosterols (PS) including stigmasterol, ß-sitosterol, and γ-oryzanol on bovine serum albumin (BSA) were deeply studied in a BSA-glucose model by measuring the glycoxidation-based products, SDS-PAGE intensity, free lysine, and their fluorescence microscopy clicks. For the first time, the underlying mechanisms of the antiglycation effects of PS were wholly elucidated by measuring their interaction ability with BSA and their antiradical activity during the glycation reactions. The results showed that PS could partially inhibit the formation of advance glycation end products, block some of the lysyl residues of BSA (Lys127, 357, 434, and 524), prevent the glucose-BAS bonding, and their disaggregation effects on the glycated BSA. Throughout the underlying mechanism behind the antiglycation activity, PS were found to structurally quench the fluorescence intensity of BSA in a static mode, leading to fluctuations in its Z-average size, UV-vis spectrum, and secondary structure. Additionally, PS mitigated the formation the advanced glycation end products by scavenging the radicals produced during the glycation reactions. Overall, these results unleash that PS prevent the glycation reactions and their subsequent changes through shielding the NH2 groups via H-bonding with their OH-groups and pi-pi interaction of the steroid core, besides the antiradical activity of PS on the free radicals generating during the glycation reactions.