Insights into the oil-water interfacial adsorption properties of whey protein-γ-oryzanol Pickering emulsion gel during in vitro simulated digestion.

This work elucidated the digestion behavior of low-oil phase Pickering emulsion gel (LOPPEG) stabilized by whey protein isolate (WPI) -γ-Oryzanol (γO) aggregated particles and interfacial adsorption properties of its simulated digestion products. Initially, following simulated digestion, WPI-γO LOPPEG exhibited lower free fatty acid release and protein digestibility compared to WPI LOPPEG. WPI-γO LOPPEG maintained lower interfacial tension and higher interfacial thickness than WPI LOPPEG.

Consequence of high-pressure homogenization on the whipping characteristics of soybean oil body cream.

The study explored the effect of different high-pressure homogenization (HPH) pressure (30-70 MPa) on the whipping characteristics of soybean oil body (SOB) cream. With the increase of HPH treatment, fat globules were further broken, and their adsorption on the interface was promoted, which further enhanced the stability of cream, leading to smaller particle size and higher apparent viscosity. Moreover, whipping performance of cream is the best at 30 MPa.

Characterization and comparison of chemical compositions and biological activities of an edible mushroom (Lactarius volemus) of three different sizes.

Characterization and comparison of the chemical compositions and biological activities of Lactarius volemus of three different sizes (large size, medium size, small size) were investigated in this work. By comparing three sizes of Lactarius volemus, the small-sized Lactarius volemus had the highest content of crude fiber, fat, crude protein, total sugar, reducing sugar, polyphenols, and total flavonoids, whereas medium-sized Lactarius volemus showed the highest content of ash and total amino acids. Meanwhile, the small-sized Lactarius volemus also exhibited the best 2,2-Diphenyl-1-picrylhy drazyl (DPPH) radical scavenging ability, α-amylase inhibitory activity, α-glucosidase inhibitory activity, and xanthine oxidase inhibitory activity.

Comparison in structure, physicochemical and emulsifying properties of alpha lactoglobulin and beta lactalbumin exposed to prior γ-oryzanol by the multi-spectroscopic and silico methods.

In this work, effects of γ-oryzanol (GO) on structure, physicochemical and emulsifying properties of α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) were compared by using multi-spectroscopic analysis and computer simulation. Specifically, the intrinsic fluorescence of both whey proteins was quenched by GO, with GO being a stronger quenching for β-Lg than for α-La. The addition of GO caused the backbone of α-La to become denser, whereas for β-Lg, its spatial structure shifted from ordered to disordered after the addition of GO.

-cold extrusion synergized with cysteine for enhancing physicochemical, rheological characteristics and digestibility of whey protein isolate.

Impacts of co-cold extrusion (≤50 °C) of whey protein isolate (WPI) and cysteine (Cys, 0, 20, 40, 60, 80 and 100 mmol/L) on its physicochemical, digestion and rheological properties were investigated. As Cys concentration increased, the emulsifying properties and digestibility of co-extruded WPI-Cys products showed an increasing trend. Specifically, when Cys reached 100 mmol/L, surface hydrophobicity, emulsification activity index (EAI), emulsification stability index (ESI) and stomach digestibility of the co-extruded WPI-Cys products increased by 205.

Exploring the role of γ-Oryzanol on stabilization mechanism of Pickering emulsion gels loaded by α-Lactalbumin or β-Lactoglobulin via multiscale approaches.

The research explored the role of γ-oryzanol (γs) on stabilization behavior of Pickering emulsion gels (PEGs) loaded by α-lactalbumin (α-LA) or β-lactoglobulin (β-LG), being analyzed by experimental and computer methods (molecular dynamic simulation, MD). Primarily, the average particle size of β-LG-γS was expressed 100.07% decrease over that of α-LA-γS.

Unraveling the significance of calcium as a biofilm promotion signal for Bacillus licheniformis strains isolated from dairy products.

Bacillus licheniformis, a quick and strong biofilm former, is served as a persistent microbial contamination in the dairy industry. Its biofilm formation process is usually regulated by environmental factors including the divalent cation Ca. This work aims to investigate how different concentrations of Ca change biofilm-related phenotypes (bacterial motility, biofilm-forming capacity, biofilm structures, and EPS production) of dairy B.

Genotype-phenotype evaluation of the heterogeneity in biofilm formation by diverse Bacillus licheniformis strains isolated from dairy products.

The spoilage bacterium Bacillus licheniformis has been identified as a quick and strong biofilm former in the dairy industry. In our previous study, intra-species variation in bacterial biofilms has been observed in diverse B. licheniformis strains from different genetic backgrounds; however, the mechanisms driving the observed heterogeneity of biofilms remain to be determined.

Calcium-mediated modulation of Pseudomonas fluorescens biofilm formation.

Biofilm formation is usually affected by many environmental factors, including divalent cations. The purpose of the current work was to analyze how calcium (Ca) affects the biofilm formation of dairy Pseudomonas fluorescens isolates by investigating their growth, swarming motility, biofilm-forming capacity, extracellular polymeric substance production, and biofilm structures. Moreover, the regulation mechanism of Ca involved in its biofilm formation was explored through RNA-sequencing analysis.

Invited review: Current perspectives for analyzing the dairy biofilms by integrated multiomics.

Biofilms formed by pathogenic or spoilage microorganisms have become serious issues in the dairy industry, as this mode of life renders such microorganisms highly resistant to cleaning-in-place (CIP) procedures, disinfectants, desiccation, and other control strategies. The advent of omics techniques, especially the integration of different omics tools, has greatly improved our understanding of the features of microbial biofilms, and provided in-depth knowledge on developing effective methods that are directly against deleterious biofilms. This review provides novel insights into the single use of each omics tool and the application of multiomics tools to unravel the mechanisms of biofilm formation, specific molecular phenotypes exhibited by biofilms, and biofilm control strategies.

Insight into the physicochemical characteristics, functionalities and digestion behavior of protein isolate derived from Lactarius volemus (L.volemus): Impacts of microwave-assisted extraction.

The impacts of microwave assisted-extraction (MAE) on the physicochemical characteristics, functionalities, and digestion behavior of Lactarius volemus (L. volemus) protein isolate (LPIs) was investigated. Compared with the conventional water bath assisted-extraction method (WAE), MAE significantly enhanced the extraction rate of LPIs by 30.

Evaluating the role of glycyrrhizic acid on the dynamic stabilization mechanism of the emulsion prepared by α-Lactalbumin: Experimental and silico approaches.

The role of glycyrrhizic acid (GA) on the dynamic stabilization mechanism of the α-Lactalbumin (α-La) emulsion was evaluated in this study. Smaller particle size and higher zeta potential value were observed in the α-La/GA emulsion as compared to the α-La emulsion. Ultra-high-resolution microscopy revealed that the interfacial film formed around oil droplets by α-La/GA complex was thicker compared to that of either α-La or GA.

Extrusion of casein and whey protein isolate enhances anti-hardening and performance in high-protein nutrition bars.

Model high-protein nutrition bars (HPNBs) were formulated by incorporating whey protein isolate (WPI) and casein (CN) at various extrusion temperatures (50, 75, 100, 125, and 150 °C) with a protein content of 45 g per 100 g. The free sulfhydryl groups, amino groups, hardness, and microstructures of HPNBs were analyzed periodically at 37 °C over a storage period of 45 days. Specifically, sulfhydryl group, amino group and surface hydrophobicity of extruded whey protein isolate (WPE) and extruded casein (CE) were significantly reduced (P < 0.

Physical treatment synergized with natural surfactant for improving gas-water interfacial behavior and foam characteristics of α-lactalbumin.

The purpose of this study was to investigate effect of physical treatment (ultrasound, U/high pressure homogenization, H/combined treatment, UH or HU) and surfactant (Mogroside V, Mog) on air/water interface adsorption and foaming properties of α-lactalbumin (ALa). Firstly, the binding of Mog and all physical-treated ALa was a static quenching process. Mog had the greatest binding affinity for HU-ALa among all treated samples.

Comparison of interaction, structure, and cell proliferation of α-lactalbumin-safflower yellow complex induced by microwave heating or conventional heating.

Background: The protein-polyphenol interaction mechanism has always been a research hotspot, but their interaction is affected by heat treatment, which is widely applied in food processing. Moreover, the effects of microwave or water-bath heating on the protein-polyphenol interaction mechanism have been not clarified. The pasteurization condition (65 °C, 30 min) was selected to compare the effects of microwave or water bath on binding behavior, structure, and cell proliferation between α-lactalbumin (α-LA) and safflower yellow (SY), thus providing a guide for the selection of functional dairy processing conditions.

Glycosylated whey protein isolate enhances digestion behaviors and stabilities of conjugated linoleic acid oil in water emulsions.

Although conjugated linoleic acid (CLA) has various excellent physiological functions, it exhibits poor water solubility and high oxidation sensitivity, which limits its applications in food industry. To solve this problem, a stable oil in water emulsion was used for protecting CLA. In this study, glycosylated whey protein isolate (GWPI) formed by whey protein isolate (WPI) and galactose was used to produce CLA emulsion, and then its physicochemical stabilities, gastrointestinal behaviors were evaluated.

Effects of ultrasound synergized with microwave on structure and functional properties of transglutaminase-crosslinked whey protein isolate.

In the present study, ultrasound (400 W, U), microwave heating (75 ℃ for 15 min, M) and ultrasound synergized with microwave heating (UM) pretreatments of whey protein isolate (WPI) were applied to investigate and compare their influence on structure, physicochemical and functional characteristic of transglutaminase (TGase)-induced WPI. From the results of size exclusion chromatography, it could be seen that all three physical pretreatments could promote the formation of polymers in TGase cross-linked WPI, whose polymer amounts were increased by the order of U, UM and M pretreatment. Among three physical methods, M pretreatment had the strongest effect on structure and functional characteristics of TGase-induced WPI.

Cysteine inducing formation and reshuffling of disulfide bonds in cold-extruded whey protein molecules: From structural and functional characteristics to cytotoxicity.

Polymer chemistry, rheology and cytotoxicity of cysteine initiated S-S redistribution in cold-extruded whey protein (TWPI) molecules were investigated. The locations of disulfide bonds in whey protein isolate (WPI), WPI dried without being extruded (OWPI) and cold-extruded WPI (TWPI), Cysteine (Cys)-treated WPI (WPI-Cys), OWPI (OWPI-Cys) and TWPI (TWPI-Cys) were precisely analyzed using liquid chromatography electrospray ionization tandem mass spectrometry (LC/MS/MS) combined with pLink software approaches. The numbers of intermolecular disulfide cross-linked peptides identified in Cys-treated samples increased by 4, 6 and 1, respectively, in the order of TWPI-Cys, OWPI-Cys and WPI-Cys.

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion.

α-lactalbumin was modified by ultrasound (US, 20 kHz, 43 ± 3.4 W/cm) pre-treatments (0, 15, 30 and 60 min) and laccase cross-linking of sonicated α-lactalbumin was used to evaluate the physical and oxidative stability of conjugated linoleic acid (CLA) emulsions. The emulsions prepared with laccase cross-linking US-α-lactalbumin (α-lactalbumin treated with US pre-treatment) and US-α-lactalbumin were scrutinized for oxidative and physical stability at room temperature for two weeks of storage.

Comparison of interaction between three similar chalconoids and α-lactalbumin: Impact on structure and functionality of α-lactalbumin.

Interaction between α-lactalbumin (α-LA) and three similar chalconoids was compared using a combination of multi-spectral analysis and molecular docking, and their influence on structure and functional properties of α-LA was also investigated. Chalconoids strongly quenched α-LA fluorescence in a static mode and their binding constants to α-LA were declined in the order of hydroxy safflower yellow A (SYA), neohesperidin dihydrochalcone (NHDC) and naringin dihydrochalcone (NGDC). The main interaction forces involved in the binding of SYA, NHDC and NGDC to α-LA included hydrophobic forces and hydrogen bonds.

Proteomic analysis of whey proteins in the colostrum and mature milk of Xinong Saanen goats.

Xinong Saanen goats are among the major dairy goats in China, and their milk is one of the major milk supplies for the Chinese dairy industry. To explore the whey proteome of Xinong Saanen goat milk, we analyzed the whey proteins of goat colostrum and mature milk using proteomic techniques. We identified a total of 314 and 524 proteins in goat colostrum and mature milk, respectively.