Publications by authors named "Youling Xiong"

Background: The quality of Acipenser sinensis deteriorates significantly during frozen storage due to its high water, protein, and unsaturated fatty acid content. Conventional freezing methods are insufficient to preserve it effectively. This study investigated the effects of liquid nitrogen freezing (LNF) on the quality and myofibrillar protein (MP) characteristics of A.

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The increasing preference for plant-based proteins over animal-derived equivalents has intensified research into alternative protein sources, with oats emerging as a noteworthy specialty crop due to their rich array of functional and bioactive components. Despite the growing interest, research into oat proteins remains in its early stages, particularly in understanding the structure-function relationship and modification strategies within food systems. Designing novel food products using oat protein presents both opportunities and challenges; the compact quaternary structure and high thermal stability of oat globulin limit its functionality in diverse applications.

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Whey protein isolate (WPI) was reacted with 20, 120, and 240 μmol/g gallic acid (GA) or epigallocatechin gallate (EGCG) at 21 °C. Equilibrium dialysis testing indicated a stronger binding capacity of whey proteins with EGCG compared to GA. Both phenolics, especially EGCG, tended to reduce the adsorption of WPI at the oil-water interface and decreased the elasticity modulus (E) of the interfacial film.

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The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 → 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues.

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This paper aims to provide an updated review and current understanding of the impact of extreme temperatures-focusing on heat stress (HS)-on the quality of pork and poultry meat, particularly amidst an unprecedented global rise in environmental temperatures. Acute or chronic HS can lead to the development of pale, soft, and exudative (PSE) meat during short transportation or of dark, firm, and dry (DFD) meat associated with long transportation and seasonal changes in pork and poultry meat. While HS is more likely to result in PSE meat, cold stress (CS) is more commonly linked to the development of DFD meat.

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The effects of resonant acoustic mixing (RAM) with different treatment times (0, 5, 10, 15, 20 and 30 min) on the structural and emulsifying properties of pea protein isolate (PPI) were investigated for the first time. Increasing the RAM treatment time from 0 to 20 min decreased the α-helix/β-sheet ratio and particle size of the PPI samples by 37.84 % and 46.

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As natural antioxidants added to meat products, polyphenols can interact with proteins, and the acid-base environment influenced the extent of non-covalent and covalent interactions between them. This study compared the bio-functional characteristics and metabolic outcomes of the myofibrillar protein-chlorogenic acid (MP-CGA) complexes binding in different environments (pH 6.0 and 8.

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Background: The influence of protein hydrolysate produced from bovine liver protein hydrolysate (LPH) by enzymatic hydrolysis, using Alcalase/Protamex (1:1), on lipid dispersions was investigated. LPH production was optimized to maximize the antioxidant activity (at 45, 50, and 55 °C for 12, 18, and 24 h). Different concentrations of LPHs (1, 3, and 5 mg/g) were added to emulsions and to liposomes.

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Oat protein is becoming an important ingredient in beverages and formulated foods owing to its high nutritive value and bland flavor; yet, its functionality remains largely unexplored. This study sought to enhance the surface activity of oat protein isolate (OPI) through high-intensity ultrasound (HIU; at 20 or 60 °C) combined with high pressure homogenization (HP; 30 MPa) treatments. Sonication disturbed the protein conformation and significantly improved surface hydrophobicity (19.

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The effects of different concentrations of eugenol (EG = 0, 5, 10, 20, 50, and 100 mg/g protein) on the structural properties and gelling behavior of myofibrillar proteins (MPs) were investigated. The interaction of EG and MPs decreased free thiol and amine content, and reduced tryptophan fluorescence intensity and thermal stability, but enhanced surface hydrophobicity and aggregation of MPs. Compared with the control (EG free), the MPs' gels treated with 5 and 10 mg/g of EG had a higher storage modulus, compressive strength, and less cooking loss.

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The effects of Astragalus polysaccharide (APS) on rheological, textural, water-holding, and microstructural properties of mung bean starch (MBS)/flaxseed protein (FP) composite gels were investigated. Results showed that the storage modulus (G') of gels with APS were significantly lower than that of the control gel, while different concentrations of APS possessed diverse effects on the hardness, gumminess and cohesiveness of the gels. Adding APS significantly improved the water retention capacity by trapping more immobilized and free water in the gel network.

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The muscle and adipose tissue histological properties in wether and ewe lambs of Gentile di Puglia breed, fed diets including two protein sources [soybean meal (SB) and SB plus distillers dried grain with solubles (DD)] and three protein levels (12.5, 15.7, and 18.

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The objective of this study was to investigate the effect of pH-shifting on the textural and microstructural properties of mung bean starch (MBS)-flaxseed protein (FP) composite gels. Results showed that different pH-shifting treatments caused changes in hydrogen bond interactions and secondary structures in composite gels, leading to the formation of loose or compact gel networks. The pH 2-shifting modified protein and starch molecules with shorter chains tended to form smaller intermolecular aggregates, resulting in the formation of a looser gel network.

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Effects of calcium gluconate (CG), calcium lactate (CL) and calcium dihydrogen phosphate (CDP) on the structural and functional properties of mung bean starch (MBS)-flaxseed protein (FP) composite gels were investigated to explore the feasibility of developing dysphagia food. The water-immobilizing, rheological and structural properties of MBS-FP composite gels adding different calcium salts (10, 30, and 50 mmol/L) were analyzed by low-field nuclear magnetic resonance measurement, rheological and textural analyses, fourier transform infrared spectroscopy, scanning electron microscopy and confocal laser scanning microscopy. Results showed that calcium salts imparted various soft gel properties to the composite gels by influencing the interactions between MBS and FP.

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Growing evidence suggests that polyphenols could mitigate type 2 diabetes mellitus (T2DM). The glucose-regulatory effects of protein-bound polyphenols, however, have been rarely studied. In this study, macrogenomic and metabolomic analyses were applied to investigate the modulation of myofibrillar protein-chlorogenic acid (MP-CGA) complexes on T2DM rats from the gut microbiota perspective.

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Disulfide bonds play an essential structural role but may hinder the molecular flexibility and functionality of proteins. The present study investigated the effect of disulfide cleavage on emulsifying activity of oat protein isolate (OPI). Four reducing agents tested (dithiothreitol, ascorbic acid, cysteine, and sodium bisulfite) except ascorbic acid disrupted inter-subunit SS bonds of OPI (up to 90 %) in a dose-dependent manner.

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The structural properties, interfacial behavior, and emulsifying ability of ultrasound-treated pea protein isolate (PPI) and the legumin (11S) and vicilin (7S) globulin fractions prepared with a salt-solubilization procedure were investigated. Of the three protein groups, PPI was strongly responsive to ultrasound perturbation (20 kHz, 57-60 W·cm) showing the greatest solubility increase, particle size reduction, structure destabilization, and conformational change. Similar but less remarkable effects were observed on 11S globulins; 7S proteins, already highly soluble (>99%), were generally less sensitive to ultrasound.

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Soy protein (SP), egg white protein (EP), and whey protein (WP) at 6% / were individually incorporated into the batter of a wheat starch (WS) and wheat gluten (WG) blend (11:1 / ratio). Moisture adsorption isotherms of WS and proteins and the viscosity, rheological behavior, and calorimetric properties of the batters were measured. Batter-breaded fish nuggets (BBFNs) were fried at 170 °C for 40 s followed by 190 °C for 30 s, and pick-up of BBFNs, thermogravimetric properties of crust, and fat absorption were determined.

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Reconstituted gluten fractions (RGF) varying in glutenin/gliadin (glu/gli) ratios was applied to change the property of wheat starch. The addition of RGF, irrespective of glu/gli ratio, significantly decreased the gelatinization enthalpy, viscosity, storage modulus (G'), and gel strength of starch. Starch particle size and leached amylose decreased by 4.

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Protein oxidation in foods remains a topic of the utmost scientific interest [...

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Emulsifying capacity (EC) of proteins is a benchmark standard widely used to evaluate the quality of protein ingredients in emulsion foods. EC (mL of oil emulsified per g of protein) is usually measured by a sudden drop in electrical resistance (phase transition) with the continuous addition of oil to a specific protein solution. However, little is known about electrochemical mechanisms behind this process because resistance, measured with an ohmmeter, is not sensitive enough to monitor changes in the concentration of protein electrolytes.

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Protein-based biodegradable packaging films are of environmental significance. The effect of oxidized ferulic acid (OFA)/tannic acid (OTA) on the crosslinking and film-forming properties of whey protein isolate (WPI) was investigated. Both of the oxidized acids induced protein oxidation and promoted WPI crosslinking through the actions of quinone carbonyl and protein sulfhydryl, and amino groups.

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The effect of polyphenol removal ("dephenol") combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI.

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