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In this study, a combined method of physical and chemical modification was used to improve the functional characteristics of porcine liver protein (PLP). PLP was modified by mild heating assisted alkaline pH shift treatment. The hydration properties, surface properties, particle size distribution, denaturation degree and molecular structure of modified PLP were measured. The results showed that heat treatment combined with a large shift in pH toward the alkaline side significantly increased the solubility and emulsifying activity of PLP, reduced the particle size while resulting in uniform size distribution, increased the absolute value of zeta potential, and decreased the free sulfhydryl content, changed the primary, secondary and tertiary structures, and increased the surface hydrophobicity. The combined treatment was superior to either treatment alone. In terms of improvements in the hydration and surface properties of PLP, heating at 50 ℃ combined with pH shift toward pH 11 was the best modification condition for PLP.

Objective: A new type of natural food preservative with pork liver as the main raw material was developed. Methods: Water-soluble porcine liver protein (WSLP), salt-soluble porcine liver protein (SSLP) and chitosan (CS) were combined to create edible composite membranes. The edible membrane components were then examined from a variety of perspectives using mechanical properties, Fourier transform infrared spectroscopy (FT-IR) and microstructure analysis. Utilized to preserve pork, and by contrasting the changes in the physical and chemical indices during the chilling process, the freshness retention capabilities of the composite film were investigated. Results: With the addition of WSLP and SSLP, the mechanical properties of edible film showed a trend of increasing firstly and then decreasing. The film was best when the amount was 40%, its film thickness was (0.267±0.001 43) and (0.264±0.001 21) mm, the tensile strength was (9.63±0.29) and (4.43±0.37) MPa, and the elongation at break was (58.37±0.90)% and (28.24±0.63)%, respectively, which were significantly different from CS film (P

In order to obtain peptide fractions, duck liver proteins were recovered by isoelectric precipitation, and then hydrolyzed simultaneously by alcalase and flavorzyme. The molecular mass distribution of the hydrolysate was determined by using a gel permeation chromatography (GPC) system followed by fractionation using a combination of gel filtration chromatography (GFC) and reversed phase-high performance liquid chromatography (RP-HPLC). Ten novel peptides with molecular mass less than 1 300 Da were identified from the subfraction with high inhibitory effect on cytokine release from macrophages using liquid chromatography-tandem mass spectrometry (LC-MS/MS). The anti-inflammatory activity of the synthetic peptides was tested in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells. Peptides LVYPFPGPI and VIESPPEI inhibited the release of NO from inflammatory cells in a dose-dependent manner, with inhibition percentages of 48.24% and 56.32% at the concentration of 100 μg/mL, respectively. VIESPPEI at the concentration of 100 μg/mL inhibited TNF-α release by 42.48%. Notably, IDVSPDSPDHY showed the strongest ability to inhibit the release of IL-6, with an inhibition percentage of 27.04% at the concentration of 25 μg/mL. This study may provide new ideas for the high-valued comprehensive utilization of duck by-products and their application in safe treatment of inflammation.

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. Lipid oxidation level and particle size of the lipid dispersions were monitored for 14 days of storage at 25 °C., Results: Radical scavenging activity and reducing power were the highest at 45 °C after 24 h of hydrolysis. Electrophoresis pattern showed that the antioxidant activity was arising from the peptides with molecular weight around 10 kDa. Lipid oxidation occurred more rapidly in samples without LPH during storage. In emulsions, lower thiobarbituric acid-reactive substance and conjugated diene values were measured with increasing concentrations of LPH at day 14. Accordingly, particle size of the samples containing 5 mg/g of LPH was smaller than those of other groups. Phase separation was observed only in lecithin emulsion without LPH at day 14. The use of LPH in liposome limited the lipid oxidation and maintained the size of the particles independently from the concentration., Conclusion: This study highlights the potential applications of animal by-products as natural antioxidants in complex food systems. The results demonstrate that LPH, particularly when hydrolyzed at optimized conditions, can effectively inhibit lipid oxidation. The findings suggest that biphasic systems incorporating LPH have promising prospects for enhancing the stability and quality of food products. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry., (© 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.)

Duck liver is an important by-product of duck food. In this study, we investigated the effects of glucose, fructose, and xylose on the antioxidant properties of glycosylated products of duck liver protein and their protective effects on HepG2 cells. The results show that the glycosylation products of the three duck liver proteins (DLP-G, DLP-F, and DLP-X) all exhibit strong antioxidant activity; among three groups, DLP-X shows the strongest ability to scavenge DPPH, ·OH free radicals, and ABTS+ free radicals. The glycosylated products of duck liver protein are not toxic to HepG2 cells and significantly increase the activity of antioxidant enzymes such as SOD, CAT, and GSH-Px in HepG2 cells at the concentration of 2.0 g/L, reducing oxidative stress damage of cells (p < 0.05). DLP-X has a better effect in reducing oxidative damage and increasing cellular activity in HepG2 cells than DLP-G and DLP-F (p < 0.05). In this study, the duck liver protein glycosylated products by glucose, fructose, and xylose were named as DLP-G, DLP-F, and DLP-X, respectively.

In this study, we investigated the effects of a porcine liver protein hydrolysate (PLH) diet on lipid metabolism in Otsuka Long-Evans Tokushima Fatty (OLETF) rats, a model of type II diabetes. OLETF rats (20-wk-old males) were pair-fed with either a PLH diet containing 20% PLH or a casein diet for 14 wk. Dietary PLH significantly lowered serum cholesterol and phospholipid concentrations, mainly by decreasing low-density lipoprotein and high-density lipoprotein fractions. Fecal cholesterol was significantly increased in the PLH diet group; however, the total bile acid concentration in the feces was not significantly different between the groups. In addition, the PLH diet significantly decreased serum thiobarbituric acid reactive substance concentrations. These results suggest that dietary PLH exerts hyperlipidemic and antioxidant effects, indicating that it is a novel functional food ingredient.

Goose liver isolate treated by pH shifting and pH shifting/non-enzyme phosphorylation with goose liver isolate was used as a control. The functional property differences in the protein and proteins involved in the interfacial layer treated with pH shifting and non-enzyme phosphorylation were studied. Compared with the goose protein isolates (GPIs) at pH 7.0, the GPIs treated by pH shifting was not a good choice to be an emulsifier in a neutral environment, and non-enzyme phosphorylation inhibited the negative effects of pH shifting treatment and improved protein properties. The results of proteomics showed that the identified proteins in the interfacial layer belong to hydrophilic proteins. Non-enzyme phosphorylation increased the abundances of most proteins due to ion strength, including some phosphorylated proteins. Correlation analysis indicated that protein solubility was highly positively related with S0, intrinsic fluorescence, total sulfhydryl, free sulfhydryl, A0A0K1R5T3, R0KA48, R0KFP7, U3J1L1, P01989, R0JSM9, and R0LAD1, and was also highly negatively related with particle size and R0M210, R0M714, and R0LFA3. The emulsifying activity index (EAI) demonstrated highly positive correlation with protein solubility, and was correlated with R0JKI4, R0KK84, R0L1Y3, R0LCM7, A0A068C605, and U3IW62.

This study investigated the feasibility to improve the emulsifying capacity of chicken liver (CL) protein using different isoelectric solubilization/precipitation (ISP) processes. The CL proteins were first solubilized at alkaline pH 10.5, 11.0, 11.5, and 12.0, followed by precipitation at pH 5.0, 5.5, and 6.0, respectively. Fresh CL paste was set as the control (raw). With the increase in solubilization pH, the protein recovery yield increased under the same precipitation pH, and the pH 12.0, 5.5 treatment obtained the highest recovery yield of 82% (p < 0.05), followed by the pH 5.0 precipitation treatments and the pH 12.0, 6.0 treatment. The particle size distribution of D3,2 and D4,3 was smaller for the pH 10.5 (except for the D4,3 of pH 10.5, 5.0) and pH 11.0 solubilization treatments than those of the other treatments (p < 0.05), regardless of precipitation pH. Compared with that of the raw control, the emulsions of the pH 10.5 and pH 11.0 solubilization treatments, and pH 12.0, 6.0 treatment showed good stability. The pH 10.5, 6.0 treatment showed the best emulsification activity, followed by the pH 10.5, 5.5, pH 11.0, 6.0, pH 12.0, 6.0, pH 10.5, 5.0, pH 11.0, 5.5, and pH 11.0, 5.0 treatments, which were uniformly distributed and were stable without the stratification of emulsions. It was concluded that CL protein recovered through suitable ISP showed potential as an emulsifier, and thus expanded the application of CL protein for human consumption.

Male MS-NASH mice were maintained on a high-fat diet for 16 weeks with and without red algae-derived minerals. Obeticholic acid (OCA) was used as a comparator in the same strain and diet. C57BL/6 mice maintained on a standard (low-fat) rodent chow diet were used as a control. At the end of the in-life portion of the study, body weight, liver weight, liver enzyme levels and liver histology were assessed. Samples obtained from individual livers were subjected to Tandem Mass Tag labeling / mass spectroscopy for protein profile determination. As compared to mice maintained on the low-fat diet, all high-fat-fed mice had increased whole-body and liver weight, increased liver enzyme (aminotransferases) levels and widespread steatosis / ballooning hepatocyte degeneration. Histological evidence for liver inflammation and collagen deposition was also present, but changes were to a lesser extent. A moderate reduction in ballooning degeneration and collagen deposition was observed with mineral supplementation. Control mice on the high-fat diet alone demonstrated multiple protein changes associated with dysregulated fat and carbohydrate metabolism, lipotoxicity and oxidative stress. Cholesterol metabolism and bile acid formation were especially sensitive to diet. In mice receiving multi-mineral supplementation along with the high-fat diet, there was reduced liver toxicity as evidenced by a decrease in levels of several cytochrome P450 enzymes and other oxidant-generating moieties. Additionally, elevated expression of several keratins was also detected in mineral-supplemented mice. The protein changes observed with mineral supplementation were not seen with OCA. Our previous studies have shown that mice maintained on a high-fat diet for up to 18 months develop end-stage liver injury including hepatocellular carcinoma. Mineral-supplemented mice were substantially protected against tumor formation and other end-state consequences of high-fat feeding. The present study identifies early (16-week) protein changes occurring in the livers of the high-fat diet-fed mice, and how the expression of these proteins is influenced by mineral supplementation. These findings help elucidate early protein changes that contribute to end-stage liver injury and potential mechanisms by which dietary minerals may mitigate such damage.

This study aimed at mining antioxidant peptides derived from duck liver as a strategy for valorizing poultry byproducts utilization via the isolation and characterization of peptide molecules with great antioxidant potential and cytoprotective effects against hydrogen peroxide-induced oxidative stress. Six novel peptides, including GEHGDSSVPVWSGVN, HLDYYLGK, HLTPWIGK, DTYIRQPW, WDDMEKIWHH, and MYPGIAD were isolated and purified by Sephadex G-15 and reverse-phase high-performance liquid chromatography, followed by the identification with liquid chromatography-tandem mass spectrometry. Among the hydrolysates from different enzymes, the alcalase-originated peptides presented the strongest antioxidant capacity as revealed by DPPH and ABTS assays. The synthesized peptides were used to validate the antioxidant activities, identifying that DTYIRQPW and WDDMEKIWHH were the major antioxidative peptides capable of protecting HepG2 cells from H2O2-induced oxidative damage via stimulating antioxidant enzymes such as superoxide dismutase and catalase to eliminate free radicals and to decrease lipid peroxidation products. Molecular docking suggested that the antioxidative properties of the isolated peptides were related to the site and number of hydrogen bonds. This investigation indicated the great potential of duck liver protein hydrolysates as a base material for producing and developing dietary bioactive peptides.

The data were obtained by a label-free quantification approach from a shotgun proteomics experiment, using STrap sample processing technique for protein digestion and high-performance liquid chromatography with tandem mass spectrometry (HPLC-MS/MS) for peptide analysis. MaxQuant data processing was used to obtain proteomics data. The dataset reflects changes in the liver protein profile of Japanese medaka exposed to 0, 5, 40 and 80 mg/L nominal concentrations of Sigma-Aldrich humic acid for 96 h. Actual concentrations of humic acid were measured using the potassium dichromate photometric method and reported in mg organic carbon/L. These proteomics data are relevant for further insights into fish stress responses to humic substances-related challenge.

The aim of this study was to optimize the protein hydrolysates from chicken liver with xylose under Maillard reaction (MR) conditions using response surface methodology. The correlation between the browning degree, grafting degree, and the antioxidant activities of the Maillard reaction products (MRPs) was investigated. The optimal reaction conditions were achieved with a reaction temperature of 138.78°C, an initial pH of 7.99, and a reaction time of 93.14 min. The grafting degree (41.98%) and browning degree (2.582) of chicken liver protein hydrolysate MRPs (CLPHM) were notably higher (P

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Background: Extracted proteins of alternative animal origin tend to present strong off-flavor perception due to physicochemical interactions of coextracted off-flavor compounds with proteins. To investigate the relationship between absorption behaviors of volatile aromas and the processes-induced variations in protein microstructures and molecular conformations, duck liver protein isolate (DLp) was subjected to heating (65/100 °C, 15 min) and ultra-high pressure (UHP, 100-500 MPa/10 min, 28 °C) treatments to obtain differential unfolded protein states., Results: Heat and UHP treatments induced the unfolding of DLp to varied degrees, as revealed by fluorescence spectroscopy, ultraviolet-visible absorption, circular dichroism spectra and surface hydrophobicity measurements. Two types of heating-denatured states with varied unfolding degrees were obtained, while UHP at both levels of 100/500 MPa caused partial unfolding of DLp and the presence of a molten-globule state, which significantly enhanced the binding affinity between DLp and (E,E)-2,4-heptadienal. In particular, significantly modified secondary structures of DLp were observed in heating-denatured samples. Excessive denaturing and unfolding degrees resulted in no significant changes in the absorption behavior of the volatile ligand, as characterized by observations of fluorescence quenching and analysis of headspace concentrations., Conclusion: Defining process-induced conformational transition behavior of matrix proteins could be a promising strategy to regulate food flavor attributes and, particularly, to produce DLp coextracted with limited off-flavor components by modifying their interaction during extraction processes. © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

Duck liver is an important by-product of duck food. In this study, we investigated the effects of glucose, fructose, and xylose on the antioxidant properties of glycosylated products of duck liver protein and their protective effects on HepG2 cells. The results show that the glycosylation products of the three duck liver proteins (DLP-G, DLP-F, and DLP-X) all exhibit strong antioxidant activity; among three groups, DLP-X shows the strongest ability to scavenge DPPH, ·OH free radicals, and ABTS + free radicals. The glycosylated products of duck liver protein are not toxic to HepG2 cells and significantly increase the activity of antioxidant enzymes such as SOD, CAT, and GSH-Px in HepG2 cells at the concentration of 2.0 g/L, reducing oxidative stress damage of cells ( p < 0.05). DLP-X has a better effect in reducing oxidative damage and increasing cellular activity in HepG2 cells than DLP-G and DLP-F ( p < 0.05). In this study, the duck liver protein glycosylated products by glucose, fructose, and xylose were named as DLP-G, DLP-F, and DLP-X, respectively.

Goose liver isolate treated by pH shifting and pH shifting/non-enzyme phosphorylation with goose liver isolate was used as a control. The functional property differences in the protein and proteins involved in the interfacial layer treated with pH shifting and non-enzyme phosphorylation were studied. Compared with the goose protein isolates (GPIs) at pH 7.0, the GPIs treated by pH shifting was not a good choice to be an emulsifier in a neutral environment, and non-enzyme phosphorylation inhibited the negative effects of pH shifting treatment and improved protein properties. The results of proteomics showed that the identified proteins in the interfacial layer belong to hydrophilic proteins. Non-enzyme phosphorylation increased the abundances of most proteins due to ion strength, including some phosphorylated proteins. Correlation analysis indicated that protein solubility was highly positively related with S 0 , intrinsic fluorescence, total sulfhydryl, free sulfhydryl, A0A0K1R5T3, R0KA48, R0KFP7, U3J1L1, P01989, R0JSM9, and R0LAD1, and was also highly negatively related with particle size and R0M210, R0M714, and R0LFA3. The emulsifying activity index (EAI) demonstrated highly positive correlation with protein solubility, and was correlated with R0JKI4, R0KK84, R0L1Y3, R0LCM7, A0A068C605, and U3IW62.

Pig liver is a high-quality source of animal protein, but natural pig liver protein is poorly emulsified. To improve its properties and enhance the added value of pig liver processing, this experiment prepared pig liver protein solution, measured the index of acylation, and investigated the effects on the emulsification properties, protein particle state, and molecular structure of pig liver protein with the addition amount of succinic anhydride as the variable. Results showed that with the increase of succinic anhydride addition, the acylation degree and emulsification activity of porcine liver protein showed an overall increasing trend, the emulsion zeta potential and the protein adsorption on the surface of emulsion oil droplets showed an increasing trend and then a decreasing trend, the emulsion particle size and protein surface hydrophobicity showed a decreasing trend, and the advanced structure of the protein were changed. The optimal addition of succinic anhydride for acylation treatment of porcine liver protein solution (10 mg/mL of concentration) was 0.10 g/g Pro. The emulsification activity of the porcine liver protein increased from 9.550 m²/g to 64.135 m²/g under this condition. Succinic anhydride reacted with porcine liver protein through covalent binding, causing changes in protein structure and significantly improving the emulsifying activity of the porcine liver protein. [ABSTRACT FROM AUTHOR]