RESUMO
BACKGROUND: Vacuum packaging has the ability to reduce oxidative deterioration and microbial-induced spoilage of meat. However, in an oxygen-free environment, it can lead to the development of an unappealing purplish-red color and a decrease in the water-holding capacity of meat, thereby impacting the overall meat quality. Portulaca oleracea L. (POL) is a homology of medicine and food known for its exceptional antioxidant and antimicrobial properties. RESULTS: The aim of our present study was to investigate the antioxidant and antimicrobial ability of n-butanol phase extract of POL and the effect of POL extract incorporation on the quality (water-holding capacity, shear force, color, and texture) and physicochemical (pH, total volatile base nitrogen, and total viable counts) attributes of vacuum-packed seasoned steaks at 4 °C over a 15-day period. Results showed that the POL extract had excellent antioxidant and antimicrobial capacity. Furthermore, the addition of POL extract significantly inhibited protein oxidation and microbial growth of steaks (P < 0.05), and improved the water-holding capacity, color properties, and tenderness (P < 0.05). Moreover, there were no significant differences (P > 0.05) in the color, water-holding capacity, or tenderness between the 0.5 and 1 g kg-1 POL extract treatment groups compared to the sodium nitrite control group. CONCLUSION: These results indicate that POL extract had the potential to replace sodium nitrite due to its ability to hinder protein oxidation and microbial growth of vacuum-packed seasoned steaks, while enhancing the color, water-holding capacity, and tenderness of seasoned steaks. © 2024 Society of Chemical Industry.
Assuntos
Antioxidantes , Embalagem de Alimentos , Conservação de Alimentos , Armazenamento de Alimentos , Extratos Vegetais , Portulaca , Portulaca/química , Extratos Vegetais/farmacologia , Extratos Vegetais/química , Embalagem de Alimentos/instrumentação , Vácuo , Animais , Conservação de Alimentos/métodos , Antioxidantes/farmacologia , Antioxidantes/química , Bovinos , Carne/análise , Carne/microbiologia , Cor , Anti-Infecciosos/farmacologia , Anti-Infecciosos/químicaRESUMO
BACKGROUND: Myosin is the most important component of myofibrillar protein, with excellent gelling properties. To date, heating treatment remains the mainstream method for forming gel in meat products, and it has the most extensive application in the field of meat industry. However, at present, there are few reports on the effects of heating rates on myosin self-assembly and aggregation behavior during heating treatment. RESULTS: The present study aimed to investigate the effects of different heating rates (1, 2, 3 and 5 °C min-1 ) on the self-assembly behavior, physicochemical, structural and gelling properties of myosin. At the lowest heating rate of 1 °C min-1 , the myosin gel had a dense microstructure, the highest elastic modulus (G') and water holding capacity compared to higher heating rates (2, 3 and 5 °C min-1 ). At higher temperatures (40, 45 °C), the surface hydrophobicity, turbidity, particle size distribution and self-assembly behavior of myosin in pre-gelling solutions showed that myosin had sufficient time to denature, underwent full structure unfolding before aggregation at the heating rate of 1°C min-1 , and formed regular and homogeneous spherical aggregates. Therefore, the myosin gel also had a better three-dimensional network. CONCLUSION: The heating rates had an important effect on the quality of myosin gels, and had theoretical implications for improving the quality of meat gel products. © 2023 Society of Chemical Industry.
Assuntos
Calefação , Miosinas , Animais , Bovinos , Miosinas/química , Temperatura Alta , Interações Hidrofóbicas e Hidrofílicas , Géis/químicaRESUMO
Glucosamine (GlcN) and microbial transglutaminase (Tgase) are used separately or together to improve the emulsifying properties of whey protein isolate (WPI). However, little is known about how the emulsifying properties change when GlcN residues are incorporated into WPI cross-linked by Tgase. We used Tgase as a biocatalyst to cross-link WPI in the presence of GlcN in a liquid system for 12 h at a moderate temperature (25°C). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analyses indicated that protein polymerization and GlcN conjugation occurred simultaneously, phenomena also supported by the loss of free amines (9.4-20.5%). Addition of 5 U Tgase/g protein improved the emulsifying properties of moderately cross-linked WPI polymers. The Tgase-treated WPI polymers had a larger particle size (â¼2.6-fold) than native WPI, which may have reduced coalescence and flocculation in an oil-in-water emulsion system. However, the incorporation of GlcN residues into WPI, predominantly via enzymatic glycation, partly inhibited the cross-links between the WPI molecules catalyzed by Tgase, reducing the size of the WPI polymers 0.81- to 0.86-fold). Consequently, WPI+GlcN conjugates provided less stability to the emulsion. Moreover, high NaCl concentration (0.2 M) decreased the emulsifying properties of the WPI+GlcN conjugates by neutralizing negative electric charges in the glycoconjugates. However, the improved emulsifying properties of WPI cross-linked by Tgase may be useful in food processing at higher NaCl concentrations due to the formation of the thicker steric barrier at the oil-water interface.
Assuntos
Proteínas do Leite/metabolismo , Proteínas do Soro do Leite , Animais , Emulsões/química , Glucosamina , Transglutaminases/metabolismoRESUMO
BACKGROUND: Different techniques have been applied to alter myofibril protein (MP) structure, which further promotes protein-protein interactions and influencing the MP gelling characteristics. Influence of BslA from natto food (protein concentration, 30 mg mL-1 ; at 0.001, 0.005, 0.01, 0.05 and 0.1 g kg-1 ) on the characteristics of MP gel of chicken breast was investigated. RESULTS: Results show that cooking loss significantly (P < 0.05) decreased with increased percentage of BslA. Hardness of MP gel did not significantly change at 0.01 g kg-1 BslA. Differential scanning calorimetry disclosed that MP was modified by the addition of BslA. Moreover, BslA produced a high value of storage modulus (G') and low value of phase angle (tan δ) during heating, especially at 0.01 g kg-1 . Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis proved the formation of higher-molecular-weight polymers by developing non-disulfide covalent bonds between MP at 0.01 g kg-1 BslA. Surface hydrophobicity of the MP gel was decreased with increased percentage of BslA. Scanning electron microscopy confirmed the increasing number of uniform cavities of MP gel with the increased percentage of BslA. CONCLUSION: Addition of 0.01 g kg-1 BslA significantly improved the water holding capacity and rheological properties of MP by developing non-disulfide covalent bonds. © 2017 Society of Chemical Industry.
Assuntos
Proteínas de Bactérias/farmacologia , Biofilmes , Galinhas , Géis/química , Proteínas Musculares/química , Miofibrilas/química , Animais , Varredura Diferencial de Calorimetria , Fenômenos Químicos , Eletroforese em Gel de Poliacrilamida , Interações Hidrofóbicas e Hidrofílicas , Carne/análise , Microscopia Eletrônica de Varredura , Proteínas Musculares/efeitos dos fármacos , Reologia , Água/análiseRESUMO
Oxidation is an important factor for denaturing of whey protein isolate (WPI) during food processing. We studied the effects of chemical oxidation on physicochemical and structural changes along with in vitro digestibility of WPI in this work. Evaluation of physicochemical changes showed that carbonyl level and dityrosine content increased, whereas total and free thiol group levels decreased for oxidized WPI samples. For the structural changes, protein aggregation was measured by surface hydrophobicity, turbidity, and particle diameter, which was increased for oxidized WPI samples. The increase of the secondary structure ß-sheets and antiparallel ß-sheet also supported the aggregation of oxidized WPI. A direct quantitative relationship between physicochemical and structural changes and protein digestibility indicated that oxidation-related damage restricts the susceptibility of WPI to proteases. In conclusion, WPI had high susceptibility to oxidative stress, and both physicochemical and structural changes caused by severe oxidative stress could decrease the rate of in vitro digestibility of WPI.
Assuntos
Fenômenos Químicos , Oxirredução , Proteínas do Soro do Leite/química , Proteínas do Soro do Leite/isolamento & purificação , Digestão , Manipulação de Alimentos , Interações Hidrofóbicas e Hidrofílicas , Estrutura Secundária de Proteína , Espectroscopia de Infravermelho com Transformada de Fourier , Tirosina/análogos & derivados , Tirosina/análiseRESUMO
Cronobacter spp. are opportunistic pathogens that can cause serious diseases in neonates and infants via consumption of contaminated milk powder. To determine Cronobacter spp. contamination status, 632 samples, including 15 evaporated milk, 45 intermediate powder, 150 finished products, and 422 manufacturing environment samples, were collected from 3 goat milk powder factories in Shaanxi province, China, from July 2013 to April 2014. The recovered Cronobacter isolates were subtyped using pulsed-field gel electrophoresis to trace the potential dissemination routes during the whole production processing. Sixty-seven Cronobacter spp. isolates were recovered. The prevalence rates in manufacturing environment, intermediate powder, and finished products were 92.5, 6.0, and 1.5%, respectively. The predominant species were Cronobacter sakazakii (88.1%); no Cronobacter turicensis, Cronobacter condimenti, or Cronobacter dublinensis were detected. Sixty-seven Cronobacter isolates were grouped in 26 clusters by pulsed-field gel electrophoresis, and substantial genetic similarity was observed among isolates from different sampling sites in the same factory. Isolates in the main clusters were commonly recovered from intermediate powder, floor powder, and shoes. These data indicated that air, powder, and personnel movement were potential routes for Cronobacter dissemination, and manufacturing environment is the key control point for Cronobacter contamination.
Assuntos
Cronobacter/classificação , Cronobacter/isolamento & purificação , Contaminação de Alimentos/análise , Leite/microbiologia , Animais , China , Cronobacter/crescimento & desenvolvimento , Eletroforese em Gel de Campo Pulsado , Microbiologia de Alimentos , CabrasRESUMO
This study aimed to develop an ammonia and pH super-sensitive label by incorporating methyl red and bromothymol blue (MR-BTB, MB) into gellan gum/sodium carboxymethyl cellulose (GG/CMC-Na, GC). Furthermore, E-nose as an auxiliary tool combined with the labels to monitor meat freshness. Results showed that MB had more color change than pure MR or BTB, and the detection limit of ammonia about the MR-BTB (1:2) group was only 2.82 ppm. The addition of MB significantly increased tensile strength, moisture content, and water solubility, but decreased elongation at break and transmittance of the GC label (p < 0.05). The result of FTIR and SEM indicated the formation of hydrogen bonds and well compatibility between MB and GC. Furthermore, the color of the GC-10.0MB label was constantly obviously changing during meat storage, indicating that the GC-10.0MB label had great potential for monitoring the freshness of the lamb meat. A high correlation was found between ΔE of GC-10.0MB label and TVB-N (R2 = 0.9092) and pH (R2 = 0.9114) of meat. Interestingly, the high correlation between ΔE of GC-10.0 MB label and the response value of S2 (R2 = 0.7531), S6 (R2 = 0.9921), and S7 sensor (R2 = 0.8325) of E-nose was also found.
Assuntos
Amônia , Carboximetilcelulose Sódica , Colorimetria , Polissacarídeos Bacterianos , Carboximetilcelulose Sódica/química , Polissacarídeos Bacterianos/química , Polissacarídeos Bacterianos/análise , Concentração de Íons de Hidrogênio , Amônia/análise , Amônia/química , Animais , Colorimetria/métodos , Ovinos , Corantes/química , Corantes/análise , Carne Vermelha/análise , Carne/análise , CorRESUMO
Traditional absorbent pads are composed of hard-to-degrade polyethylene film and non-woven bottom layer, which have the characteristic of low absorption rate, without antibacterial effect. The objective of this study is to fabricate a novel superabsorbent and antibacterial aerogel, which consists of whey protein isolate (WPI) and chitosan (CS). The citric acid (CA) and ε-polylysine hydrochloride (ε-PLH) are incorporated into WPI/CS-based aerogel as cross-linking and antibacterial agent, respectively. The application in meat preservation as an absorbent pad is investigated. Results of water absorption, water vapor absorption and stress-strain show that aerogel comprised of 6 % WPI, 1.2 % CS, 2.0 % CA, and 2.0 % ε-PLH have the best water absorption capacity and stress. The density of WPI/CS/CA/ε-PLH aerogel is 82.7 ± 6.4 mg/cm3, and has a uniform and polyporous microstructure, resulting in superabsorbent capacity. Antibacterial rate of WPI/CS/CA/ε-PLH aerogel against Staphylococcus aureus, Escherichia coli, Salmonella and Listeria monocytogenes reach around 80 %. The WPI/CS/CA/ε-PLH aerogel significantly reduces increased velocity of bâ, pH, total volatile base nitrogen, and total viable counts and decreased velocity of Lâ and bâ of chicken meat (P < 0.05). Results indicate WPI/CS/CA/ε-PLH aerogel effectively extends shelf-life of chicken meat to 7 days, and could be used as an absorbent pad in meat preservation.
Assuntos
Quitosana , Animais , Proteínas do Soro do Leite , Quitosana/farmacologia , Quitosana/química , Galinhas , Antibacterianos/farmacologia , Antibacterianos/química , Carne/microbiologia , Escherichia coliRESUMO
Herein, an EGCG-Histidine complex is prepared, characterized, and further used to improve gel properties of myofibrillar proteins (MP). Results of FTIR, XRD, UV-Vis spectroscopy showed that histidine is covalently bound to EGCG by Michael addition or Schiff base reaction to form EGCG-Histidine complex, and antioxidant activity of EGCG-Histidine complex is significantly increased compared to EGCG or histidine alone (P < 0.05). The addition of EGCG-Histidine complex results in cooking loss of gel decreasing from 66.7 ± 0.23 % to 40.3 ± 2.02 %, and improves rheological properties of MP, and enhances gel strength from 0.10 ± 0.01 N to 0.22 ± 0.03 N, indicating positive effect of EGCG-Histidine complex on MP gel formation, above results is supported by results of SEM, CD spectroscopy, SDS-PAGE, and tryptophan fluorescence. These results indicated that EGCG-Histidine complex can be used as a functional ingredient to improve gel quality of meat products.
Assuntos
Catequina , Catequina/análogos & derivados , Géis , Histidina , Proteínas Musculares , Animais , Histidina/química , Catequina/química , Suínos , Proteínas Musculares/química , Géis/química , Miofibrilas/química , Reologia , Produtos da Carne/análise , Antioxidantes/químicaRESUMO
This study primarily investigated the improvement of high-dose Epigallocatechin-3-Gallate (EGCG)-induced deterioration of MP gel by soy protein isolate (SPI) addition. The results showed that EGCG could interact with MP, SPI, and HSPI (heated), indicating the competitive ability of SPI/HSPI against EGCG with MP. EGCG was encapsulated by SPI/HSPI with high encapsulation efficiency and antioxidation, with antioxidant activities of 78.5% â¼ 79.2%. FTIR and molecular docking results revealed that MP, SPI, and HSPI interacted with EGCG through hydrogen bonding and hydrophobic interactions. SPI/HSPI competed with MP for EGCG, leading to the restoration of MHC and Actin bands, alleviating the aggregation caused by EGCG and oxidation. Additionally, SPI/HSPI-E significantly reduced the high cooking loss (23.71 and 26.65%) and gel strength (13.60 and 17.02%) induced by EGCG. Hence, SPI competed with MP for EGCG binding site to ameliorate MP gel properties, thereby alleviating the detrimental changes in MP caused by high-dose EGCG and oxidation.
RESUMO
This study investigated the effect of different hydrocolloids on the improvement of the printability and post-processing stability of minced chicken meat, each hydrocolloid was prepared with 1 % formulation and compared with the control. The effects of these hydrocolloids on the rheological properties of chicken mince and complex model printing capability were explored separately, while the cooking loss and microstructure changes of the samples before and after heating were analyzed. The results showed that the chicken mince gel containing carrageenan was more suitable for printing, increased the yield stress and apparent viscosity of the samples, and the printing process was easier to mold. In addition, carrageenan increased the hardness of the samples, and the microstructures were compact and changed little during the heating process, and the water was locked in the gel matrix, reducing shape changes during the heating process. The use of hydrocolloids improves the stability of post-processing of chicken 3D printing.
Assuntos
Galinhas , Coloides , Impressão Tridimensional , Reologia , Animais , Coloides/química , Viscosidade , Carragenina/química , Culinária , Temperatura Alta , Temperatura , Produtos da Carne/análiseRESUMO
Long-term excessive intake of sodium negatively impacts human health. Effective strategies to reduce sodium content in foods include the use of salty and salt taste-enhancing peptides, which can reduce sodium intake without compromising the flavor or salt taste. Salty and salt taste-enhancing peptides naturally exist in various foods and predominantly manifest as short-chain peptides consisting of < 10 amino acids. These peptides are primarily produced through chemical or enzymatic hydrolysis methods, purified, and identified using ultrafiltration + gel filtration chromatography + liquid chromatography-tandem mass spectrometry. This study reviews the latest developments in these purification and identification technologies, and discusses methods to evaluate their effectiveness in saltiness perception. Additionally, the study explores four biological channels potentially involved in saltiness perception (epithelial sodium channel, transient receptor potential vanilloid 1, calcium-sensing receptor (CaSR), and transmembrane channel-like 4 (TMC4)), with the latter three primarily functioning under high sodium levels. Among the channels, salty taste-enhancing peptides, such as γ-glutamyl peptides, may co-activate the CaSR channel with calcium ions to participate in saltiness perception. Salty taste-enhancing peptides with negatively charged amino acid side chains or terminal groups may replace chloride ions and activate the TMC4 channel, contributing to saltiness perception. Finally, the study discusses the feasibility of using these peptides from the perspectives of food material constraints, processing adaptability, multifunctional application, and cross-modal interaction while emphasizing the importance of utilizing computational technology. This review provides a reference for advancing the development and application of salty and salt-enhancing peptides as sodium substitutes in low-sodium food formulations.
Assuntos
Peptídeos , Cloreto de Sódio na Dieta , Percepção Gustatória , Paladar , HumanosRESUMO
The two diets, a duck meat diet (DMD) and a control casein diet (CD) were isocaloric (15.9 kJ/g dry matters), and contained 18.3% protein, 7.4% fat, 60.0% carbohydrate. The selenium contents in casein, duck meat powder, CD and DMD were 0.061, 0.549, 0.123 and 0.225 mg/kg. Rats in the DMD group had higher serum selenium concentrations (p<0.05) and liver 5'-deiodinase activities (p<0.05). As a result, duck meat consumption increased serum tri-iodothryonine (T3) concentrations (p<0.05) and decreased serum thyroxine (T4) concentrations (p<0.05). The lower serum T4 concentrations (p<0.05) were also supported by the lower total content of tyrosine and phenylalanine in duck meat powder compared to casein (7.72 vs 10.13). Compared to casein, duck meat powder had higher total content of glutamic acid, leucine, aspartic acid, serine, and alanine (44.68 vs 49.21), which led to higher serum TBG concentrations (p<0.05) in the DMD group. Hence, the DMD group had lower serum free T4 (FT4) concentrations (p<0.05), and lower serum free T3 (FT3) concentrations on day 14 (p<0.05), which significantly decreased the energy expenditure of rats in the DMD group, with lower liver Na,K-ATPase and Ca-ATPase activities (p<0.05), lower OCRs and rectal temperature, especially on day 13 (p<0.05), higher body weight (p<0.05), and body-weight gain (p<0.05). We concluded that duck meat consumption decreased the energy metabolism of rats by multiple-step regulation of THs.
Assuntos
Dieta , Patos , Metabolismo Energético , Carne , Hormônios Tireóideos/sangue , Aminoácidos/análise , Animais , Temperatura Corporal , ATPases Transportadoras de Cálcio/metabolismo , Caseínas/química , Iodeto Peroxidase/metabolismo , Fígado/enzimologia , Masculino , Carne/análise , Ratos , Ratos Sprague-Dawley , ATPase Trocadora de Sódio-Potássio/metabolismo , Tiroxina/sangue , Tiroxina/metabolismo , Tri-Iodotironina/sangue , Tri-Iodotironina/metabolismo , Aumento de PesoRESUMO
This study aimed to investigate the application potential of Portulaca oleracea extract (POE) in active packaging for the preservation of chilled meat. First, the antioxidant capacity and active ingredients of POE were systematically studied. The results demonstrated that POE has excellent antioxidant capacity and contains abundant antioxidant compounds. Subsequently, antioxidant-active packaging films based on chitosan and starch containing different concentrations of POE (CS/POE films) were successfully developed. The main physicochemical and mechanical properties of the CS/POE films were characterized and evaluated. The CS/POE films exhibited remarkable antioxidant activity and can significantly reduce lipid oxidation in meat. Compared with polyethylene film, the CS/POE films-treated meats had better preservation effects and longer shelf-life. These findings suggested that CS/POE film has the potential to become a good alternative to conventional plastics in food packaging. In conclusion, Portulaca oleracea extract is an excellent natural antioxidant with great potential in active packaging for chilled meat preservation.
RESUMO
Ovotransferrin is the most heat-sensitive protein in egg white which alters the processing suitability. To improve thermostability, phosphorylation modification was performed under different pH values (5.0, 6.0, 7.0, 8.0, and 9.0), and the reasons for which were explored via physicochemical changes in this study. SEM and particle size results showed that phosphorylation diminished the average particle diameter and the number of attached particles. CD results revealed that the α-helix content of phosphorylated ovotransferrin increased and the random coil decreased significantly (P < 0.05). Tertiary structure, surface hydrophobicity and ζ-potential analyses showed that phosphorylation made more hydrophobic amino acids buried inside ovotransferrin. These changes might be because most of the phosphorylation occurred in α-helix and ß- sheet to promote the thermal tolerance of phosphorylated ovotransferrin by improving its structure orderliness and decreasing surface hydrophobicity. The results indicated that phosphorylation was a practical method to enhance the thermal stability of heat-sensitive ovotransferrin.
Assuntos
Conalbumina , Pasteurização , Fosforilação , Clara de Ovo , AminoácidosRESUMO
This study aimed to use edible scaffolds as a platform for animal stem cell expansion, thus constructing block-shaped cell culture meat. The tea polyphenols (TP)-coated 3D scaffolds were constructed of sodium alginate (SA) and gelatin (Gel) with good biocompatibility and mechanical support. Initially, the physicochemical properties and mechanical properties of SA-Gel-TP scaffolds were measured, and the biocompatibility of the scaffolds was evaluated by C2C12 cells. SEM results showed that the scaffold had a porous laminar structure with TP particles attached to the surface, while FT-IR results also demonstrated the encapsulation of TP coating on the scaffold. In addition, the porosity of all scaffolds was higher than 40% and the degradation rate during the incubation cycle was less than 40% and the S2-G1-TP0.1-3 h scaffold has excellent cell adhesion and extension. Subsequently, we inoculated rabbit skeletal muscle myoblasts (RbSkMC) on the scaffold and induced differentiation. The results showed good adhesion and extension behavior of RbSkMC on S2-G1-TP0.1-3 h scaffolds with high expression of myogenic differentiation proteins and genes, and SEM results confirmed the formation of myotubes. Additionally, the adhesion rate of cells on scaffolds with TP coating was 1.5 times higher than that on scaffolds without coating, which significantly improved the cell proliferation rate and the morphology of cells with extension on the scaffolds. Furthermore, rabbit-derived cultured meat had similar appearance and textural characteristics to fresh meat. These conclusions indicate the high potential of the scaffolds with TP coating as a platform for the production of cultured meat products.
Assuntos
Alginatos , Gelatina , Animais , Coelhos , Gelatina/química , Alginatos/química , Alicerces Teciduais/química , Polifenóis , Espectroscopia de Infravermelho com Transformada de Fourier , Carne , Chá/químicaRESUMO
As an emerging technology to obtain protein by culturing animal-derived cells in vitro, it is crucial to construct 3D edible scaffolds to prepare structured cell cultured meat products. In this study, a scaffold based on gellan gum (GG)-gelatin (Gel) was prepared and further cross-linked with Ca2+. FTIR confirmed the electrostatic interaction between GG and Gel and the ionic cross-linking of Ca2+ and carboxyl groups, and SEM images showed the porous structure of the scaffolds. The staining results showed that scaffolds with high concentrations of Ca2+ had higher biocompatibility than scaffolds with low concentrations of Ca2+ and non-crosslinked scaffolds, and scaffolds Ca2+-GG2-Gel3-0.5 adhered to more cells and were more conducive to cell spreading. The immunofluorescence staining, SEM images, Western blot, and RT-qPCR showed that the scaffolds supported the proliferation and myogenic differentiation of chicken skeletal muscle satellite cells (CSMSCs) and myotubes were formed on the scaffolds. Finally, the scaffolds were stained and fried after culturing. The results of the textural and chromatic analysis showed that the texture and color of the scaffolds were similar to fresh meat and meat products. These results showed that ionically crosslinked GG-Gel scaffolds are biocompatible and stable for structured cell cultured meat models.
Assuntos
Gelatina , Alicerces Teciduais , Animais , Alicerces Teciduais/química , Gelatina/química , Polissacarídeos Bacterianos/química , Carne , Engenharia Tecidual , Células CultivadasRESUMO
As a natural antioxidant, Epigallocatechin-3-gallate (EGCG) needed to be added in high doses to maintain the quality of meat products. However, high doses of EGCG caused the excessive aggregation of myofibrillar protein (MP), which damaged the gel properties of MP gels. Therefore, the purpose of this study was to investigate the mitigation of EGCG-induced loss of MP gelling potential by L-Lysine (L-Lys). The results showed that the addition of 20 mM L-Lys induced excessive unfolding and loose aggregation of MP at 10 µmol/g EGCG, and hence, reducing the solubility (14.5%) and the tryptophan fluorescence, and forming a network structure with a large aperture. Therefore, the cooking loss was decreased from 29.20% to 15.13%, and the strength of MP gels was decreased from 0.35 N to 0.17 N. However, L-Lys hindered the hydrogen bonding interactions and hydrophobic interactions between MP and EGCG by competing the binding sites of MP at 50 µmol/g EGCG, which was supported by the Zeta potential, surface hydrophobicity, FTIR and molecular docking analysis. Thus L-Lys mitigated the protein aggregation caused by 50 µmol/g EGCG, improved the solubility (23.02%â¼86.99%) and apparent viscosity, which were beneficial for the formation of a continuous network structure in MP gels. Therefore, the cooking loss of MP gels was decreased from 52.40% to 41.30%, and the gel strength was enhanced from 0.13 N to o.22 N with 20 mM L-Lys addition. The present study could provide a new strategy for increasing the amounts of EGCG in meat products without damaging the gel properties of meat products.
Assuntos
Lisina , Proteínas Musculares , Proteínas Musculares/química , Simulação de Acoplamento Molecular , Géis/químicaRESUMO
This work investigated the improvement of amylopectin addition on the quality of myofibrillar proteins (MP) gel damaged by high doses of epigallocatechin-3-gallate (EGCG, 80 µM/g protein). The results found that the addition of amylopectin partially alleviated the unfolding of MP induced by oxidation and EGCG, and enhanced the structural stability of MP. Amylopectin blocked the loss of the free amine group and thiol group, and increased the solubility of MP from 7.0% to 9.5%. The carbonyl analysis demonstrated that amylopectin addition did not weaken the antioxidative capacity of EGCG. It was worth noting that amylopectin significantly improved the gel properties of MP treated with a high dose of EGCG. The cooking loss was reduced from 51.2% to 35.5%, and the gel strength was reduced from 0.41 N to 0.29 N after adding high concentrations of amylopectin (A:E(8:1)). This was due to that amylopectin filled the network of MP gel after absorbing water and changed into a swelling state, and partially reduced interactions between EGCG and oxidized MP. This study indicated that amylopectin could be used to increase the polyphenol loads to provide a more lasting antioxidant effect for meat products and improve the deterioration of gel quality caused by oxidation and high doses of EGCG.
RESUMO
Cultured meat production has emerged as a breakthrough technology for the global food industry with the potential to reduce challenges associated with environmental sustainability, global public health, animal welfare, and competition for food between humans and animals. The muscle stem cell lines currently used for cultured meat cannot be passaged in vitro for extended periods of time. Here, we develop a directional differentiation system of porcine pre-gastrulation epiblast stem cells (pgEpiSCs) with stable cellular features and achieve serum-free myogenic differentiation of the pgEpiSCs. We show that the pgEpiSCs-derived skeletal muscle progenitor cells and skeletal muscle fibers have typical muscle cell characteristics and display skeletal muscle transcriptional features during myogenic differentiation. Importantly, we establish a three-dimensional differentiation system for shaping cultured tissue by screening plant-based edible scaffolds of non-animal origin, followed by the generation of pgEpiSCs-derived cultured meat. These advances provide a technical approach for the development of cultured meat.