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FOOD RESEARCH INTERNATIONAL · 2023 · IF 8.1

Magnetic field-assisted cascade effects of improving the quality of gels-based meat products: A mechanism from myofibrillar protein gelation

Jingwen Wang,Qiyuan Lu,Junming Gong,Fei Gao,Xinglian Xu,Huhu Wang

Physics-assisted processing technologies have huge potential in the meat processing industry. By modeling two essential procedures (pickling and preheating) of gels-based meat products, this work investigated the cascade effects of a new physical technology (magnetic field) on the conformational structures and gel properties of myofibrillar proteins (MPs). Samples were subjected with four magnetic field (MF)-assisted treatments (group A, both processes without MF; group B, pickling without MF combining with preheating with 4.5 mT MF; group C, pickling with 3.0 mT MF combining with preheating without MF; group D, pickling with 3.0 mT MF combining with preheating with 4.5 mT MF). The result showed that MF-assisted treatments significantly improved water holding capacity (WHC) of MP gels compared with group A (46.9%), reaching the maximum value of 52.1% in group D.   According to the low-field nuclear magnetic results, group D decreased the percentages of P 22 (6.97%) and increased the percentages of P 21 (93%), which showed that water molecules were more tightly bound to each other. Meanwhile, the unfolding of α-helix and the formation of random coil of MF-assisted treatments resulted in more exposure of internal groups, leading to the formation of a dense network. These findings would provide new insights to improve the quality of gels-based meat products via the MF.

CAS / MDL: 69-78-3 67-42-5
研究领域: 食品科学 · 物理学 · 蛋白质化学
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INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY · 2019 ·Vol. 55 ·期 2 ·601-609 · IF 2.281

Water holding capacity of sodium-reduced chicken breast myofibrillar protein gel as affected by combined CaCl2 and high-pressure processing

Yu Wang,Ying Zhou,Xi-xi Wang,Pei-jun Li,Bao-cai Xu,Cong-gui Chen

Summary The water holding capacity (WHC) of sodium-reduced (0.3 m sodium chloride, corresponding to the salt percentage (w/v) of 1.755%) myofibrillar protein (MP) gel in response to combined calcium chloride (CaCl 2 , 20, 60, 100 m m ) and high-pressure processing (HPP, 200 MPa, 10 min) was investigated. The results showed that 200 MPa + 20 m m CaCl 2 synergistically increased the WHC of MP gel via reducing particle size of MP solutions, strengthening hydrogen-bonding and disulphide-bonding, promoting formation of β-sheet and uncoiling of α-helix, exposing tryptophan residues, enhancing hydrophobic interactions of aliphatic residues and forming a compact and continuous networked gel structure. However, high concentrations (≥60 m m ) of CaCl 2 could attenuate the enhancing effects of HPP on the WHC by inducing decreased hydrogen bonds, fewer tryptophan residues exposed and coarser and aggregated gel structures with large cavities. Therefore, a combined moderate HPP and low concentration of CaCl 2 is a potential alternative for developing sodium-reduced meat products.

CAS / MDL: 10043-52-4
研究领域: 食品科学 · 蛋白质化学 · 肉类加工技术
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Foods · 2023 ·Vol. 12 ·期 8 ·1684 · IF 5.2

Dose-Dependent Effect of Hyperoside on the Physicochemical and Gel Properties of Porcine Myofibrillar Proteins at Different NaCl Concentrations under Oxidative Stress

Xiuyun Guo,Shuangyi Xu,Xiangren Meng,Zengqi Peng

The effects of HYP (10, 50, and 250 μM/g protein) on the physicochemical and gel properties of myofibrillar proteins (MPs) at different NaCl concentrations under oxidative stress were explored. The incorporation of HYP significantly reduced carbonyl content and decreased the loss of free amine groups in a dose-dependent manner, regardless of NaCl concentration. In addition, HYP induced a dose-dependent decrement in total sulfhydryl content regardless of NaCl concentration, which might result from the formation of thiol-quinone adducts via Michael addition. The surface hydrophobicity was significantly increased with HYP addition. Nevertheless, compared with samples treated with 50 μM/g HYP, 250 μM/g HYP caused a significant decrease in surface hydrophobicity, which might be due to the increase in the extent of MPs unfolding and the concomitant aggregation of MPs by hydrophobic interaction. Furthermore, HYP also showed a dose-dependent increment in the water-holding capacity (WHC) and gel strength of MPs gels, which might be due to more orderly crosslinks via fibrous filaments at 0.2 M NaCl and more regular and lamellar structures with smaller and more homogeneous pores at 0.6 M NaCl. In summary, HYP reduced the oxidation-mediated changes of physicochemical characteristics, preventing the oxidative damage of MPs and reinforcing the ordered crosslinks of MPs–MPs and MPs–HYP during thermal gelation, ultimately resulting in a better gel quality. These results provide a theoretical support for the practical application of HYP as a natural antioxidant in gel-type meat products.Keywords:myofibrillar proteins;HYP;oxidative characteristics;gel properties

研究领域: 食品科学 · 生物化学 · 营养学
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FOOD CHEMISTRY · 2021 · IF 7.514

Preparation of Pickering emulsion gels based on κ-carrageenan and covalent crosslinking with EDC: Gelation mechanism and bioaccessibility of curcumin

Bao Zhang,Ran Meng,Xiao-Long Li,Wen-Jie Liu,Jie-Shun Cheng,Wu Wang

Pickering emulsions stabilized by zein/carboxymethyl dextrin nanoparticles were added to the κ-carrageenan-based gel matrix to prepare emulsion gels via EDC - induced covalent crosslinking. Texture, WHC and freeze–thaw stability of the emulsion gels increased after crosslinking. The Confocal laser scanning microscope and SEM suggested that droplet clusters could be observed in gel with higher concentration of emulsion. The rheological measurements indicated that the viscosity and gel-like structure were relied on crosslinking agent and emulsion concentration. The photothermal stability of curcumin was significantly enhanced after crosslinking. In addition, in vitro digestion study suggested that the bioaccessibility of curcumin in emulsion gel crosslinked was lower compared to emulsion gel without crosslinking agent. These studies might facilitate the preparation of emulsion gels with excellent stability for bioactive compounds delivery in food and pharmaceutical applications.

CAS / MDL: 25952-53-8 6066-82-6
研究领域: 食品科学 · 药学 · 材料科学
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Food Bioscience · 2024 · IF 4.8

Effects of different isochoric freeze-thaw cycles on the physicochemical quality attributes of chicken breast meat

Tsekwi Gracious Rinwi,Da-Wen Sun,Ji Ma,Qi-Jun Wang

This study investigated the impact of isochoric freezing-thawing (ISF-T) cycles (C0–C5) on the quality of chicken breast. The results indicated a significant increase (P < 0.05) in pH from 5.41 to 5.96 after C1 to C4 before slightly decreasing to 5.72 (C5). Lightness (L*) varied between 50.13 and 44.55 across C1 to C4, with redness notably decreasing from −1.15 after C0 to −2.09 after C5 while yellowness (b) sharply increased from 2.65 (C0) to 4.65 (C5). Moisture content decreased from 74.01% to 68.13% after C5. WHC slightly reduced from 89.25% after C0 to 85.66% after C4, with an 83.78% reduction after C5. Cooking loss increased linearly across the ISF-T cycles from 18.08% reaching 24.14% after C5. Conversely, shear force decreased to 21.83 N after C5 from 25.21 N after C1. Protein solubility slowly increased to 88.79% after C3, then decreased to 72.84 after C5. The myofibrillar index remained stable until C3, then increased from 35.51 after C5. Lipid oxidation slowly increased to 0.27 mg MDA/kg after C3, then sharply increased to 0.44 mg MDA/kg after C5. In addition, Ca 2+ -ATPase activity showed that the samples obtained after C1 to C3 fluctuated between 23.59% and 24.71%, followed by a substantial reduction to 12.35% after C5. Furthermore, validation of the results by magnetic resonance imaging and nuclear magnetic resonance analysis confirmed the findings, suggesting that isochoric freezing could offer a viable solution to control temperature fluctuations, a challenging problem during meat storage and distribution in the cold chain food industry.

研究领域: 食品科学 · 肉类加工 · 物理化学 · 生物物理学
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FOOD HYDROCOLLOIDS · 2022 · IF 11.504

Physicochemical properties and digestibility of thermally induced ovalbumin–oil emulsion gels: Effect of interfacial film type and oil droplets size

Ruiling Li,Hui Xue,Binghong Gao,Huilan Liu,Tianfeng Han,Xiaobo Hu,Yonggang Tu,Yan Zhao

To investigate the effect of oil droplets surface film type and droplets size on the physicochemical properties and digestibility of thermally induced ovalbumin–oil emulsion gels, Tween 80 and ovalbumin were selected as individual emulsifiers for the emulsification of sunflower oil at different homogenization speeds (6000, 8000, and 10000 rpm), and the formed emulsions were mixed with ovalbumin matrix solution and then heated to form heat-induced ovalbumin emulsion gels (OEG). The OEG with ovalbumin as emulsifier had higher hardness, water holding capacity (WHC), and surface hydrophobicity, and lower digestibility, spin−spin relaxation time ( T 2 ) and free sulfhydryl content than those of the OEG with Tween 80 as the emulsifier ( p  < 0.05). As the oil droplets size decreased, the hardness increased, WHC increased, the amide A band shifted to lower wavenumbers, digestibility decreased, T 2 decreased, free sulfhydryl content decreased, and surface hydrophobicity increased for both OEG ( p  < 0.05). These results collectively indicated that the physicochemical properties of the OEG are influenced by the property of the oil interfacial film and the size of the oil droplets. The oil droplets surrounded by the interfacial protein film improved the performance of the OEG greatly, and the proteins within its OEG formed a dense gel network structure through hydrophobic aggregation, disulfide bond crosslinking, and hydrogen bonding. The oil droplets with smaller sizes favored the enhancement in the physicochemical properties of the OEG. Changes in the size of oil droplets and the type of film wrapped around them regulated the digestibility of the OEG.

CAS / MDL: 69-78-3 111-30-8
研究领域: 食品科学 · 胶体与表面化学 · 生物物理学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2024 · IF 6

Refrigerated Storage-Induced Quality Deterioration of Mandarin Fish (Siniperca chuatsi): Analyzing the Role of Endogenous Enzymes through TMT-Based Quantitative Proteomics

Zhouyi Xiong,Mingqian Zhou,Shan Xiao,Zhongli Zhang,Dan Li

Tandem Mass Tag (TMT)-based proteomics was employed to elucidate the pivotal role of endogenous enzymes in the quality deterioration of Mandarin fish ( Siniperca chuatsi ) during refrigerated storage. Proclean 300 was used to inhibit the growth of psychrophilic microorganisms, emphasizing the contribution of endogenous enzymes. Quality characteristics, including pH, water-holding capacity, color, texture, and myofibrillar fragmentation index (MFI), were compared between the Proclean 300-treated group (P-group) and the control group (C-group). Correlation analysis underscored the collaborative role of calpain and cathepsin B in postmortem degradation. Pearson correlation analysis showed that texture characteristics were significantly negatively correlated with MFI and significantly positively correlated with whiteness and L* in the P-group. Differentially expressed proteins (DEPs) analysis identified 66 DEPs, with 40 exhibiting low abundance, including cytoskeleton proteins and hemoglobin subunits, and 26 showing high abundance, primarily metabolic enzymes. Bioinformatics analysis revealed significant enrichment of DEPs within the glycolysis/gluconeogenesis pathway. Furthermore, protein-protein interaction analysis highlighted key proteins linked to the quality deterioration of Mandarin fish, including beta-enolase, phosphoglycerate kinase 1, and triosephosphate isomerase B. These findings offer valuable insights into the mechanisms behind the quality deterioration of refrigerated Mandarin fish and the intricate relationship with endogenous enzymes.

CAS / MDL: 26093-31-2
研究领域: 食品科学 · 蛋白质组学 · 生物化学 · 水产养殖
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