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Complexes of hesperidin with different plant proteins (rice protein, pea protein, pea/rice complex protein) were prepared by pH-driven method to improve the water solubility, environmental stability, and bioavailability of hesperidin. The complexes were characterized by scanning electron microscopy, dynamically scattered light, and X-ray diffraction. Meanwhile, the high performance liquid chromatography was used to determine the hesperidin content to analyze the environmental stability of complexes and bioavailability of hesperidin. The results showed that three plant proteins were able to improve the water solubility of hesperidin, among which the pea/rice complex protein improved 19.6-fold, and the solubility of hesperidin in water reached 340.78 μg/mL. The environmental stability of hesperidin-pea/rice complex protein complex was basically better than that of single plant protein, in which the heat stabilization was the most effective, and the retention of hesperidin was at 65.09% after heating at 80 °C for 2 h. The in vitro digestion results showed that the bioavailability of hesperidin in hesperidin-pea/rice complex protein complex was the highest, which was about 5.22-fold of free hesperidin. This study provided a new idea to enhance the stability and bioavailability of hesperidin and helped to expand the application of hesperidin. [ABSTRACT FROM AUTHOR]

In order to expand the application range of chickpea protein isolate (CPI) and improve the stability of low oil emulsion systems, this study used CPI as an emulsifier in oil-in-water (O/W) type CPI emulsions and investigated the effect of ultrasound treatment (20 kHz, 450 W) with different durations (0 min, 3 min, 6 min, 9 min, and 12 min) on the stability of CPI emulsions. The results showed that ultrasound treatment could significantly improve the stability of CPI emulsions compared with the untreated CPI emulsions. At 12 min of ultrasound treatment, the emulsification activity index (EAI) and emulsion stability index (ESI) were increased to (51.67±0.12) m²/g and (99.32±0.13) min, respectively. The average particle size became the smallest ((3.52±0.25) µm), resulting in finer and more uniform oil droplets. The absolute value of zeta-potential was the largest (52.57±1.31 mV), the Turbiscan stability index (TSI) was the lowest, and the storage, thermal and freeze-thaw stability of the CPI emulsions were all improved. As revealed by cold-field electron microscopy, CPI emulsions treated by ultrasound had a dense and regular internal structure, with smaller droplets and less spacing. In conclusion, a certain duration ultrasound treatment could improve the stability of CPI prepared emulsions, and the better effect was achieved at 12 min of ultrasound treatment. [ABSTRACT FROM AUTHOR]

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Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

To improve the solubility and stability of lutein (LUT), this study utilized the electrostatic self-assembly method to encapsulate LUT within food-grade protein nanoparticles and composite nanoparticles derived from soybean protein isolates (SPI) and fucoidin (FUD). The impact of the SPI/FUD mass ratio on the formation of ternary composite nanoparticles, known as lutein-soybean protein isolate-fucoidin nanoparticles (LUT-SPI-FUD NPs), was examined. The preparation process underwent optimization through single-factor experiments and the Box-Behnken response surface methodology. Various characterization techniques, including ultraviolet spectroscopy, Fourier-transform infrared spectroscopy, differential scanning calorimetry and X-ray diffraction were employed to delve into the mechanisms governing the formation of these two types of nanoparticles to compare with their solubility, stability, and antioxidant properties. The results showed that LUT-SPI-FUD NPs with SPI/FUD mass ratio of 4:1 had an absolute value of zeta potential greater than 30 mV, a polydispersity index, and a smaller particle size. Under these conditions, the most favorable formulation and process parameters were as follows: A LUT/SPI mass ratio of 1:7.587, SPI mass concentration of 0.83 mg/mL, and a stirring time of 1.493 hours. Characterization analysis verified the ideal particle size and more concentrated distribution of both LUT-SPI NPs and LUT-SPI-FUD NPs, and the binding forces were the interplay of hydrogen bonds, hydrophobic interactions, and electrostatic forces. Solubility, stability, and antioxidant assessments indicated that the conversion of LUT into LUT-SPI NPs and LUT-SPI-FUD NPs substantially increased its solubility in purified water by 350.74 and 432.42 times, respectively. Moreover, both formulations very significant (P<0.01) enhanced the stability and antioxidant capacity of LUT when subjected to ultraviolet light, high temperatures, and oxygen exposure, with LUT-SPI-FUD NPs exhibiting superior performance over LUT-SPI NPs. Consequently, the composite food-grade nanocarrier system, built upon SPI and FUD, represented a more effective technology for augmenting the solubility, stability, and antioxidant properties of LUT, and would offer a promising avenue for future LUT applications. [ABSTRACT FROM AUTHOR]

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Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Ice cream is a kind of complex colloidal system of solid-liquid-gas three-phase coexistence with thermodynamic instability. A series of physical and chemical changes occur during the storage stage, leading to ice crystal coarsening, water loss in the matrix and uneven air dispersion, which consequently lead to ice cream decline. Therefore, how to improve the stability of the ice cream system is an urgent problem to be solved in the food industry. Milk protein is a kind of natural animal protein, which can be used as an emulsifier and stabilizer in ice cream systems, preventing droplets from aggregating through intermolecular interaction with oil and polysaccharide, adsorption film viscosity, electrostatic repulsion, and steric hindrance. Thus, the stability of ice cream was improved. The structural characteristics and formation mechanism of the ice cream system were summarized. Then the behavior characteristics of milk protein in the oil-water interface, bubble interface, and continuous phase of ice cream as well as its influence on stability were discussed to provide a theoretical basis for the processing and application of milk protein in the ice cream system. [ABSTRACT FROM AUTHOR]

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This study aimed to investigate the effects of Portulaca oleracea extracts (PE) on the gelation and emulsification properties of pork myofibrillar proteins (MPs). A myofibrillar protein-Fenton oxidation system (0.0049 g/L FeCl3, 0.0176 g/L ascorbic acid, 5 mmol/L H2O2) was established, and different concentrations of PE (0.00, 2.00, 4.00, 8.00 mg/mL) were added. The changes in gelation and emulsification properties of MPs were analyzed to assess the impact of PE on the functional characteristics of MPs in pork tenderloin under oxidative conditions. The results demonstrated that PE significantly reduced the cooking loss of the gel (P<0.01) and improved its water-holding capacity (P<0.01) compared with the oxidation control group. Specifically at a concentration of 4.00 mg/mL, the addition of PE resulted in a 6.72% decrease in cooking loss and a 11.98% increase in water-holding capacity compared with the oxidation control group. However, the addition of PE led to a significant decrease in the whiteness of the gel (P<0.05), with the degree of whiteness being inversely related to the concentration of PE. Furthermore, the addition of PE increased the storage modulus (G') and loss modulus (G") of the gel. At a concentration of 4.00 mg/mL PE, the microscopic structure of the gel exhibited greater regularity and order than that after oxidation, with an increase of 10.10% in hardness and 7.16% in elasticity. SDS-PAGE results indicated that the cross-linking between PE and proteins could be reduced, and PE significantly enhanced the emulsifying activity and emulsifying stability of the proteins (P<0.01). Overall, based on the comprehensive findings, it can be concluded that 4.00 mg/mL PE effectively inhibits the oxidation of MPs and improves the functional characteristics of proteins. [ABSTRACT FROM AUTHOR]

Heat treatment is an important factor affecting the stability of the protein emulsion. This paper investigated the effects of different heat treatment temperature (30, 50, 70, 80 and 90 t, 30 min) on the physicochemical properties of tuna protein emulsion. The results showed that the emulsifying property of the heat-treated protein emulsion changed significantly compared with those without heat treatment (P<0.05). Surface hydrophobicity, viscosity, Zeta-potential, emulsifying activity and emulsion stability of tuna protein emulsion increased first and then decreased with the rise of heat treatment temperature. Within 30~70 °C of heating, protein secondary structure unfolded, hydrophobic groups exposed, the viscosity of emulsion increased, the particle size of the droplet decreased and the stability of the emulsion increased. After the heating temperature exceeded 70 °C, the protein molecules reassembled, the amino acid residues bound to the oil droplets reentered the protein interior, the droplets appeared flocculation and the emulsion became unstable. The results of SDS-PAGE illustrated that the amount of protein adsorption at the oil-water interface increased, the droplet distribution was uniform, the particle size reached the minimum value of 102.6 nm, the viscosity reached the maximum of 43.87 Pas at 70 °C for 30 min. There was no stratification in the emulsion after 28-days of storage and the emulsion had the best stability at this temperature. To sum up, appropriate heat treatment could improve the stability of the tuna protein emulsion. [ABSTRACT FROM AUTHOR]

Shelled shrimps (Penaeus vannamei) vacuum-treated with sodium pyrophosphate, sodium tripolyphosphate, trehalose, alginate oligosaccharide or carrageenan oligosaccharide solutions were stored at −18 ℃ and evaluated for thawing loss, thermodynamic properties, myofibril protein content, Ca2+-ATPase activity, and surface hydrophobicity of myofibril proteins after 0, 30, 60 and 90 days and molecular mass distribution of proteins after 90 days. Our aim was to investigate the effect of different additives combined with vacuum permeation treatment on the stability of myofibrillar proteins from peeled shrimps. The results showed that compared with distilled water, vacuum treatment with each of the five additives effectively reduced the thawing loss of frozen shrimp muscle, improved the low-temperature stability of myofibrillar proteins, and inhibited their freeze denaturation. Among these additive, trehalose, alginate oligosaccharide and carrageenan oligosaccharide had more significant cryoprotective effects. This study can provide a basis for the research and utilization of natural antifreeze agents, and also provide a scientific basis for the processing of new shrimp products.

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Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

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Objective: To screen the recombinant hemagglutinin (HA) protein with high expression and good hemagglutination activity for H3N2 influenza virus. Methods: Based on the HA ectodomain gene of A/MINNESOTA/41/2019 (H3N2) strain, GP67 signal sequences and trimerization motifs were respectively fused to the N-and C-terminals of the full-length HA ectodomain gene and the near transmembrane domain two residues truncated gene. The recombinant genes were expressed in baculovirus system. At the same time, the corresponding recombinant HA proteins without containing trimerization motifs were generated. The expressions of these recombinant HA proteins were identified by Western blot. The recombinant proteins were purified by affinity chromatography. Then, the hemagglutination titer and stability of the recombinant proteins were analyzed. Results: Four kinds of HA recombinant proteins were effectively expressed, among which the expression level of HA ectodomain full-length fusion trimerization motif (HA-T) was the highest, and the yield of it was up to 30 mg per liter suspension medium purified by Strep tag affinity chromatography. The cross-linking analysis showed that HA-T was in the form of stable trimer of HA. In addition, the hemagglutination activity analysis showed that HA-T had the highest activity, and its hemagglutination titer can reach 29. Dynamic light scattering showed that it was stable at 4 ℃ for 3 months. Conclusions: HA-T has the advantages of high expression, good stability, high hemagglutination activity and easy purification. The research provides a useful reference for the development strategy of HA recombinant protein vaccines. [ABSTRACT FROM AUTHOR]

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Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Native mass spectrometry (MS) enables the maintenance of intramolecular and intermolecular noncovalent interactions in the gas phase, thus can be used for characterization of proteins and protein complexes under the near “native” conditions. Ion mobility spectrometry (IMS) is a technique that separates ions based on the time they travel through a gas-filled chamber under the influence of an electric field, the combination of IMS and MS can act as a tool to separate complex mixtures, to resolve ions that may be indistinguishable by MS alone, or to determine structural, and it is complementary to more traditional structural biology techniques, such as NMR, X-ray crystallography and cryo-electron microscopy. In this review, the basic principle of IM-MS and the information extracted during IM-MS measurements were firstly introduced. Ion mobility separation adds a third dimension to MS analyses, an IM-MS three-dimensional spectrum containing information regarding the mass to charge ratio, abundance of ions, and the drift time the ions travel through the IM cell. Arrival time distribution reflecting the structural heterogeneity of proteins and complexes, as well as IM-derived collision cross section (CCS) that closely related to the crystal structure of an ion can also be obtained. Another remarkable toolkit often used in IM-MS experiments is collision induced unfolding method, which enables the rapid differentiation of subtly different protein isoforms based on their unfolding patterns and stabilities. In the following sections, the applications of native IM-MS in the study of protein conformation and non-covalent interactions were summarized, including the determination of variation in conformation states or isomers that would result in the same m/z measurement, differentiating proteins with different labile PTMs, and probing protein stability and conformational changes induced by ligand binding. How this technique can be used to understand protein conformational dynamics and analyze highly heterogenous protein mixtures were also discussed. The progress has been made in applying IM-MS to identify transiently populated monomeric and oligomeric species for a number of amyloid systems are highlighted. Although native IM-MS is unable to reveal resolution at the atomic level, the ability to analyze protein heterocomplexes and protein-ligand interactions in their native conformations offers competitive advantages over other structural approaches. More recently, the integration of IM-MS with the native top-down method and multiple dissociation methods has enable native IM-MS to provide multi-dimensional structural information and be applicable to more diverse analytical settings. With the ongoing development and improvement of a new generation of high-resolution, sensitive and convenient ion mobility mass spectrometry technology, as well as the further integration with diversified mass spectrometry technologies, it is believed that native IM-MS will become an invaluable tool for analyzing biological macromolecules structure and interactions. [ABSTRACT FROM AUTHOR]

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Glycerol is a simple polyol compound, it has many biological and industrial applications when mixed with water. It can stabilize proteins under extreme conditions, such as heat stress, cold shock, high pressure, etc. Most proteins are usually stored in a buffer system with the presence of glycerol after purification to maintain the stability of their biological activity. At present, there are still some controversies about the protective mechanism of glycerol on proteins. Most studies were focused on the effect of high concentrations of glycerol on protein structure. However, there were few related studies on low concentrations of glycerol. Therefore, an in-depth understanding of the effects of low concentrations of glycerol on protein structure is beneficial to protein-related research and applications. Electrospray ionization-mass spectrometry (ESI-MS) has become a commonly used technique to study protein structure and function, which is reliable and time-efficient. Protein conformational change can be described in more detailed by ESI combined with ion mobility spectrometry. Ion mobility provides an additional dimension of resolution. When ions with different sizes, charges and shapes pass through the chamber, they are migrated and separated in neutral media according to the collision cross-section (CCS). By measuring the molecular weight, charge state distribution, drift time and CCS, the structural change information of the protein can be obtained. In this study, bovine serum albumin (BSA) was used as a model protein, and ion mobility-mass spectrometry (IM-MS) and dynamic light scattering were used to investigate the effect of low concentration glycerol on protein structure under approximate physiological conditions. The results showed that glycerol within a certain concentration range could cause an increase in the average charge and CCS of BSA. Meanwhile, a single charge state of BSA also experienced an increase of CCS in presence of glycerol. In addition, the hydration radius of BSA were increased with the increase of glycerol concentration. The results indicated that low concentrations of glycerol can loosen proteins. It is interesting to note that the unfolding voltage of BSA containing 0.5% glycerol was higher than BSA without glycerol and the unfolding transition occurred in a wider voltage range, indicating that low concentration of glycerol can improve the stability of the protein. These results provide further insight into the mechanism of glycerol stabilizing proteins and may also provide references for the related research and development of proteins. [ABSTRACT FROM AUTHOR]

In order to improve the inhibition activity and light stability of the protein extract TraT2A from the fermentation broth of Trichoderma atroviride T2 strain, the ultraviolet protective agents (ascorbic acid, humic acid) and the auxiliary agent (IE-08, SP-4821A and SP-4821B) were screened, the inhibition condition of TraT2A for Alternaria alternata were optimized through the colony growth rate test, and the field control efficacy on lily leaf spot disease was determined. The results showed that TraT2A had a good inhibitory effect on A.alternata at 200.00 mg/mL and the inhibitory rate was 72.12%. With the prolongation of the UV illumination time, the inhibition activity of TraT2A gradually decreases. The addition of 5.00 mg/mL humic acid had an excellent UV protection effect on TraT2A and its inhibition rate (69.01%) increased by 39.64% compared with that without a UV protection agent (29.37%). The addition of 0.17 mg/mL adjuvant of SP-4821A increased the inhibition activity of TraT2A most significantly and the inhibition rate (95.13%) increased by 25.97% compared with the TraT2A control (69.16%). According to the optimized formula, 200 g TraT2A (the mass concentration was 200.00 mg/mL), 5 g humic acid (the mass concentration was 5.00 mg/mL), 0.17 g SP-4821A (the mass concentration was 0.17 mg/mL) and 794.83 mL sterilized water was mixed and the field control efficacy of the mixture was tested on lily leaf spot disease, the result showed that its field control efficacy was 80.37%. The research results provide a theoretical basis for the further development of TraT2A preparations for the control of lily diseases. [ABSTRACT FROM AUTHOR]

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Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Target identification of bioactive molecules is important for deciphering their functions and action mechanism in cells, as well as for drug development. Thermal proteome profiling (TPP), based on the principle that protein-ligand binding can increase the thermal stability of proteins, is a new technology for identifying target proteins of bioactive molecule. One of the advantages of TPP is that it doesn’t require functionalization of a bioactive compound, which significantly broadens its application in drug discovery and development. TH588 is an inhibitor of 7,8-dihydro-8-oxoguanine triphosphatase (MTH1), and it inhibits the proliferation of tumor cells by increasing the oxidative damage of DNA. However, previous studies showed that TH588 also executed MTH1-independent anti-tumor effects on multiple cancers by depolymerizing tubulin, increasing oxidative damage, and inactivating PI3K-AKT-mTOR signaling pathway. Therefore, identification of off-targets for TH588 is essential for understanding TH588 functions and its further chemical modification in drug development. Herein, a detailed experiment procedure of TPP workflow was presented, and 28 directly binding proteins and 53 indirectly binding proteins of TH588 was identified for understanding its anti-proliferative functions. [ABSTRACT FROM AUTHOR]

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Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of South China Fisheries Science is the property of South China Fisheries Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective This study aims to investigate the effect of the regulator of G-protein signaling 2 (RGS2) on the proliferation and invasion of oral squamous cell carcinoma (OSCC) cells and its potential molecular mechanism. Methods The expression status and clinical significance of RGS2 in head and neck squamous cell carcinomas and matched adjacent normal tissues were evaluated using TCGA database. Three OSCC cell lines (i.e., SCC-9, Cal27, and Fadu) were overexpressed with RGS2, and the effect of RGS2 on cell proliferation and invasion was determined using the Transwell, clone formation, and cell counting kit (CCK)-8 assays. Moreover, the yeast two-hybrid screening and co-immunoprecipitation (Co-IP) assays were conducted to detect the correlation of RGS2, four and a half LIM domains protein 1 (FHL1), and damage DNA-binding protein 1 (DDB1). Results The expression level of RGS2 in OSCC was significantly lower than that in matched adjacent normal tissues (P=0.023). The high RGS2 expression level was negatively correlated with lymphovascular invasion (P<0.001). After transfection with lentiv-RGS2, the expression of RGS2 was increased, and the invasion and proliferation abilities of OSCC cell lines were evidently inhibited. FHL1 could competitively bind with RGS2, which decreased the integration of DDB1 and RGS2, inhibited the ubiquitination process of RGS2, and maintained the stability of the RGS2 protein. Conclusion RGS2 plays an important role in the inhibition of OSCC proliferation and invasion. The structure stability of RGS2 is competitively regulated by FHL1 and DDB1. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)