To explore the oxidation mechanism of wooden breast myofibrillar protein(WBMP),oxidative breast MP(OBMP)was obtained from different doses(3,10,and 20 mmol/L)of H2O2 oxidized normal breast MP(NBMP).The results showed t...To explore the oxidation mechanism of wooden breast myofibrillar protein(WBMP),oxidative breast MP(OBMP)was obtained from different doses(3,10,and 20 mmol/L)of H2O2 oxidized normal breast MP(NBMP).The results showed that the Zeta-potential,particle size,solubility,sulfhydryl,and carbonyl contents of OBMP-3(3 mmol/L,low-dose free radicals)and WBMP were similar.Fluorescence spectrum analysis showed that the oxidation of low-dose free radicals led to a significant increase in the surface hydrophobicity(from 214.03±10.03 to 393.50±10.33)and tryptophan fluorescence intensity(from 185.71 to 568.32).In addition,theα-helix content of WBMP decreased significantly from(37.46±1.15)%(NBMP)to(34.70±2.04)%,whileβ-sheet and random coil contents increased significantly(P<0.05)from(14.37±0.69)%and(22.24±0.78)%(NBMP)to(17.70±0.87)%and(25.20±1.47)%(WBMP).In summary,low-dose free radical oxidation attacks protein groups,inducing secondary and tertiary structural changes,leading to the formation of WBMP.This work will provide a theoretical basis at the molecular level for exploring the mechanism of functional degradation of WBMP.展开更多
A Pickering emulsion based on sodium starch octenyl succinate(SSOS)was prepared and its effects on the physicochemical properties of hairtail myofibrillar protein gels(MPGs)subjected to multiple freeze-thaw(F-T)cycles...A Pickering emulsion based on sodium starch octenyl succinate(SSOS)was prepared and its effects on the physicochemical properties of hairtail myofibrillar protein gels(MPGs)subjected to multiple freeze-thaw(F-T)cycles were investigated.The whiteness,water-holding capacity,storage modulus(G')and texture properties of the MPGs were significantly improved by adding 1%-2%Pickering emulsion(P<0.05).Meanwhile,Raman spectral analysis demonstrated that Pickering emulsion promoted the transformation of secondary structure,enhanced hydrogen bonds and hydrophobic interactions,and promoted the transition of disulfide bond conformation from g-g-g to g-g-t and t-g-t.At an emulsion concentration of 2%,theα-helix content decreased by 10.37%,while theβ-sheet content increased by 7.94%,compared to the control.After F-T cycles,the structure of the MPGs was destroyed,with an increase in hardness and a decrease in whiteness and water-holding capacity,however,the quality degradation of MPGs was reduced with 1%-2%Pickering emulsion.These findings demonstrated that SSOS-Pickering emulsions,as potential fat substitutes,can enhance the gel properties and the F-T stability of MPGs.展开更多
Investigation that protein oxidation to the formation of advanced glycation end products(AGEs)after chicken myofibrillar protein glycation is limited.Models of protein oxidation induced by different concentrations of ...Investigation that protein oxidation to the formation of advanced glycation end products(AGEs)after chicken myofibrillar protein glycation is limited.Models of protein oxidation induced by different concentrations of hydroxyl radicals(·OH)were developed after the chicken myofibrillar protein mild glycation(MPG).Results exhibited that levels of AGEs and surface hydrophobicity(H_(0))steadily increased with the a ddition of h ydrogen peroxide(H_(2)O_(2))concentration.However,levels of s ulfhydryl group,free amino group,and particle size gradually decreased with the H_(2)O_(2)concentration.The protein carbonyl value increased in H_(2)O_(2)concentration until 10 mmol/L.Pearson's correlation indicated that MPG structure modification(unfolding and degradation)induced by protein oxidation were significantly positively correlated with AGEs concentration(P<0.05).Finally,a mechanism was proposed to hypothesize t he effect of protein oxidation on the formation of AGEs under MPG conditions.展开更多
This study aimed to investigate the effects of phosphorylated-ovalbumin(P-OVA)at different concentrations(0.5%and 1.0%)on the gel properties of pork myofibrillar protein(MP).The results showed that the textural proper...This study aimed to investigate the effects of phosphorylated-ovalbumin(P-OVA)at different concentrations(0.5%and 1.0%)on the gel properties of pork myofibrillar protein(MP).The results showed that the textural properties such as gel hardness,cohesiveness,springiness and chewiness were improved with P-OVA addition at 0.5%.The water holding capacity(up to 75.89%)and gel strength(up to 168.56 g·mm)of MP gel were markedly increased after P-OVA addition.The absolute value of zeta potential reached 13.85 mV and maximum hydrophobicity(15.2μg)resulted from the addition of 0.5%P-OVA.The storage modulus(G’)and loss modulus(G’’)of MP gel were significantly increased from 50°C,and the G’and G’’significantly increased after 1.0%P-OVA addition,evidencing that the cross-linking effect of MP protein gel was enhanced.In addition,the P-OVA addition improved the structure of MP gel protein by reducing theα-helix,while increasing theβ-sheet and the r-value(the ratio between two ultraviolet second-derivative peak-to-trough distances),which further promoted the uniform and compact gel network structure.This work demonstrated that P-OVA is a highly effective modifier that significantly improves the quality of MP gel.From a view of practice,0.5%P-OVA is the optimal addition amount.展开更多
Changes in protein quality during ice storage affects the muscle structure,the textural quality,functional properties and the eating quality.Dynamic viscoelastic behaviour and gelling properties ofmeat proteinsin rela...Changes in protein quality during ice storage affects the muscle structure,the textural quality,functional properties and the eating quality.Dynamic viscoelastic behaviour and gelling properties ofmeat proteinsin relation to histological changes in white leg shrimp muscles were assessed for 14 days in ice storage.Reduction in Ca2+ATPase activity of fresh myofibrillar protein(MFP),fading of myosin banding pattern and increased gapping in myofibrils were clearly observed with progress of storage.The quality indices of the shrimp muscle were well correlated with histological and functional properties as a function of ice storage.Solubility of fresh MFP was 86.76%which decreased to 77.06%on the 14th day of storage period.Emulsion capacity found to increase during storage period.Gel strength of white leg shrimp meat was low(81±14 g cm)and further,reduced nearly 60%compared to fresh sample at the end of storage.The considerable reductions(from 535.77 kPa to 246.56 kPa)in storage modulus values were evident of diminishing elasticity and gelling ability of the meat due to ice storage.Therefore,this study usherd that the histological deterioration in myofibrils may be used as an indication of diminishing biochemical quality and gelling behaviour of the proteins.展开更多
The effects of the microwave combined with air convection thawing(MAT)on the gelling properties of pork myofibrillar proteins(MPs)were further studied and compared with those of fresh meat(FM),and single thawing metho...The effects of the microwave combined with air convection thawing(MAT)on the gelling properties of pork myofibrillar proteins(MPs)were further studied and compared with those of fresh meat(FM),and single thawing methods(microwave thawing(MT)and air convection thawing(AT)).Results revealed that the thawing methods,excluding MAT,induced deterioration in the gelling properties of MPs.There was no significant difference(p>0.05)in the water holding capacity(WHC),cooking loss,whiteness,and strength of gel samples subjected to MAT and those of FM samples,demonstrating that the gelling properties were retained after MAT.As well,protein aggregation was limited,since MAT reduced the change in zeta potential and turbidity compared to that observed with MT or AT.The dynamic rheology and scanning electron microscopic results were relatively consistent,revealing that among the different thawing techniques,MAT had the least negative impact on the microstructure of MPs gel,leading to the generation of a more elastic and uniform gel structure than that of the MT or AT gels.Moreover,MAT resulted in higher water retention in the gels than that achieved with MT or AT.These findings indicated that MAT improved the gelling properties of MPs,thereby confirming the suitability of this treatment for use in the meat processing industry.展开更多
In the present study,myofibrillar proteins were extracted from the meat proteins of beef,lamb,chicken,tuna and emperor fish using non-denaturation method,and their physico-chemical and rheological properties were asse...In the present study,myofibrillar proteins were extracted from the meat proteins of beef,lamb,chicken,tuna and emperor fish using non-denaturation method,and their physico-chemical and rheological properties were assessed.The myofibrillar proteins of beef,emperor and lamb samples had higher percentage of protein extractability than tuna and chicken samples.The tuna sample showed significantly higher bound bromophenol blue(BPB)value while lamb samples showed lower value(P<0.05).The myofibrillar protein of chicken sample was found to have more ionic and hydrogen bonds than all other myofibrillar samples.The disulphide bonds in tuna and lamb myofibrillar protein samples were significantly higher than other three samples(P<0.05).The myofibrillar protein samples showed major bands myosin heavy chain,α-actinin,desimin,actin,troponin,tropomyosin and myosin light chain with wider molecular weight distribution in the range of 20-200 ku.The myofibrillar proteins exhibited Newtonian and shear thickening nature behaviour at lower protein concentration(1 mg/mL)as revealed by flow profile and visco-elastic analysis using rheometer.展开更多
基金supported by the Shandong Modern Agricultural Technology and Industry System(SDAIT-11-11)China Agricultural Research System(CARS-41-Z06)Natural Science Foundation of Shandong Province(ZR2022MC087).
文摘To explore the oxidation mechanism of wooden breast myofibrillar protein(WBMP),oxidative breast MP(OBMP)was obtained from different doses(3,10,and 20 mmol/L)of H2O2 oxidized normal breast MP(NBMP).The results showed that the Zeta-potential,particle size,solubility,sulfhydryl,and carbonyl contents of OBMP-3(3 mmol/L,low-dose free radicals)and WBMP were similar.Fluorescence spectrum analysis showed that the oxidation of low-dose free radicals led to a significant increase in the surface hydrophobicity(from 214.03±10.03 to 393.50±10.33)and tryptophan fluorescence intensity(from 185.71 to 568.32).In addition,theα-helix content of WBMP decreased significantly from(37.46±1.15)%(NBMP)to(34.70±2.04)%,whileβ-sheet and random coil contents increased significantly(P<0.05)from(14.37±0.69)%and(22.24±0.78)%(NBMP)to(17.70±0.87)%and(25.20±1.47)%(WBMP).In summary,low-dose free radical oxidation attacks protein groups,inducing secondary and tertiary structural changes,leading to the formation of WBMP.This work will provide a theoretical basis at the molecular level for exploring the mechanism of functional degradation of WBMP.
基金supported by the National Natural Science Foundation of China(U20A2067,32272360)。
文摘A Pickering emulsion based on sodium starch octenyl succinate(SSOS)was prepared and its effects on the physicochemical properties of hairtail myofibrillar protein gels(MPGs)subjected to multiple freeze-thaw(F-T)cycles were investigated.The whiteness,water-holding capacity,storage modulus(G')and texture properties of the MPGs were significantly improved by adding 1%-2%Pickering emulsion(P<0.05).Meanwhile,Raman spectral analysis demonstrated that Pickering emulsion promoted the transformation of secondary structure,enhanced hydrogen bonds and hydrophobic interactions,and promoted the transition of disulfide bond conformation from g-g-g to g-g-t and t-g-t.At an emulsion concentration of 2%,theα-helix content decreased by 10.37%,while theβ-sheet content increased by 7.94%,compared to the control.After F-T cycles,the structure of the MPGs was destroyed,with an increase in hardness and a decrease in whiteness and water-holding capacity,however,the quality degradation of MPGs was reduced with 1%-2%Pickering emulsion.These findings demonstrated that SSOS-Pickering emulsions,as potential fat substitutes,can enhance the gel properties and the F-T stability of MPGs.
基金supported by National Key R&D Program of China(2021YFD2100104)griculture Research System of China(CARS-41-Z)+2 种基金Science and Technology Project of Nanjing City(202002040)Jiangsu Province Policy Guidance Program(BX2020008)Postgraduate Research&Practice Innovation Program of Jiangsu Province(KYCX21_0579),China。
文摘Investigation that protein oxidation to the formation of advanced glycation end products(AGEs)after chicken myofibrillar protein glycation is limited.Models of protein oxidation induced by different concentrations of hydroxyl radicals(·OH)were developed after the chicken myofibrillar protein mild glycation(MPG).Results exhibited that levels of AGEs and surface hydrophobicity(H_(0))steadily increased with the a ddition of h ydrogen peroxide(H_(2)O_(2))concentration.However,levels of s ulfhydryl group,free amino group,and particle size gradually decreased with the H_(2)O_(2)concentration.The protein carbonyl value increased in H_(2)O_(2)concentration until 10 mmol/L.Pearson's correlation indicated that MPG structure modification(unfolding and degradation)induced by protein oxidation were significantly positively correlated with AGEs concentration(P<0.05).Finally,a mechanism was proposed to hypothesize t he effect of protein oxidation on the formation of AGEs under MPG conditions.
基金the Innovation-Driven Development Capacity Enhancement Fund of Shanxi Province(SXYBKY2019041)National Key Research and Development Program(2021YFD1600604-03)+1 种基金Shanxi Scholarship Council of China(2021-068)Shanxi Agricultural University High-Level Talent Project(2021XG013).
文摘This study aimed to investigate the effects of phosphorylated-ovalbumin(P-OVA)at different concentrations(0.5%and 1.0%)on the gel properties of pork myofibrillar protein(MP).The results showed that the textural properties such as gel hardness,cohesiveness,springiness and chewiness were improved with P-OVA addition at 0.5%.The water holding capacity(up to 75.89%)and gel strength(up to 168.56 g·mm)of MP gel were markedly increased after P-OVA addition.The absolute value of zeta potential reached 13.85 mV and maximum hydrophobicity(15.2μg)resulted from the addition of 0.5%P-OVA.The storage modulus(G’)and loss modulus(G’’)of MP gel were significantly increased from 50°C,and the G’and G’’significantly increased after 1.0%P-OVA addition,evidencing that the cross-linking effect of MP protein gel was enhanced.In addition,the P-OVA addition improved the structure of MP gel protein by reducing theα-helix,while increasing theβ-sheet and the r-value(the ratio between two ultraviolet second-derivative peak-to-trough distances),which further promoted the uniform and compact gel network structure.This work demonstrated that P-OVA is a highly effective modifier that significantly improves the quality of MP gel.From a view of practice,0.5%P-OVA is the optimal addition amount.
文摘Changes in protein quality during ice storage affects the muscle structure,the textural quality,functional properties and the eating quality.Dynamic viscoelastic behaviour and gelling properties ofmeat proteinsin relation to histological changes in white leg shrimp muscles were assessed for 14 days in ice storage.Reduction in Ca2+ATPase activity of fresh myofibrillar protein(MFP),fading of myosin banding pattern and increased gapping in myofibrils were clearly observed with progress of storage.The quality indices of the shrimp muscle were well correlated with histological and functional properties as a function of ice storage.Solubility of fresh MFP was 86.76%which decreased to 77.06%on the 14th day of storage period.Emulsion capacity found to increase during storage period.Gel strength of white leg shrimp meat was low(81±14 g cm)and further,reduced nearly 60%compared to fresh sample at the end of storage.The considerable reductions(from 535.77 kPa to 246.56 kPa)in storage modulus values were evident of diminishing elasticity and gelling ability of the meat due to ice storage.Therefore,this study usherd that the histological deterioration in myofibrils may be used as an indication of diminishing biochemical quality and gelling behaviour of the proteins.
基金This study was supported by the Henan Province University Innovation Talents Support Program(No.22HASTIT043)the Young Scientists Sponsorship Program of Henan(No.2022 HYTP008)+1 种基金the Major Science and Technology Project of Henan Province(No.221100110500)the Science and Technology Research Project of Henan Province(No.232102110075).
文摘The effects of the microwave combined with air convection thawing(MAT)on the gelling properties of pork myofibrillar proteins(MPs)were further studied and compared with those of fresh meat(FM),and single thawing methods(microwave thawing(MT)and air convection thawing(AT)).Results revealed that the thawing methods,excluding MAT,induced deterioration in the gelling properties of MPs.There was no significant difference(p>0.05)in the water holding capacity(WHC),cooking loss,whiteness,and strength of gel samples subjected to MAT and those of FM samples,demonstrating that the gelling properties were retained after MAT.As well,protein aggregation was limited,since MAT reduced the change in zeta potential and turbidity compared to that observed with MT or AT.The dynamic rheology and scanning electron microscopic results were relatively consistent,revealing that among the different thawing techniques,MAT had the least negative impact on the microstructure of MPs gel,leading to the generation of a more elastic and uniform gel structure than that of the MT or AT gels.Moreover,MAT resulted in higher water retention in the gels than that achieved with MT or AT.These findings indicated that MAT improved the gelling properties of MPs,thereby confirming the suitability of this treatment for use in the meat processing industry.
文摘In the present study,myofibrillar proteins were extracted from the meat proteins of beef,lamb,chicken,tuna and emperor fish using non-denaturation method,and their physico-chemical and rheological properties were assessed.The myofibrillar proteins of beef,emperor and lamb samples had higher percentage of protein extractability than tuna and chicken samples.The tuna sample showed significantly higher bound bromophenol blue(BPB)value while lamb samples showed lower value(P<0.05).The myofibrillar protein of chicken sample was found to have more ionic and hydrogen bonds than all other myofibrillar samples.The disulphide bonds in tuna and lamb myofibrillar protein samples were significantly higher than other three samples(P<0.05).The myofibrillar protein samples showed major bands myosin heavy chain,α-actinin,desimin,actin,troponin,tropomyosin and myosin light chain with wider molecular weight distribution in the range of 20-200 ku.The myofibrillar proteins exhibited Newtonian and shear thickening nature behaviour at lower protein concentration(1 mg/mL)as revealed by flow profile and visco-elastic analysis using rheometer.
文摘为改善低盐(1g/100mLNaCl)环境中肌原纤维蛋白的功能特性,研究不同添加量的焦磷酸钠(tetrasodium pyrophosphate,TSPP)、三聚磷酸钠(sodium tripolyphosphate,STPP)、六偏磷酸钠(sodium hexametaphosphate,SHMP)对白鲢鱼肌原纤维蛋白结构和功能特性的影响。结果表明:低盐条件下,随着磷酸盐添加量的增加,肌原纤维蛋白的溶解度、表面疏水性、乳化性均呈上升趋势;3种磷酸盐均使肌原纤维蛋白引入磷酸基团;添加0.2~0.5 g/100 mL STPP能够降低肌原纤维蛋白热解速率,提升蛋白质热稳定性,其中0.4 g/100 mL STPP修饰的蛋白质磷酸化程度最大,此时大量的磷酸根基团与肌原纤维蛋白结合;TSPP和STPP更有利于蛋白质的聚集,而SHMP磷酸化的蛋白质更稳定。综上,0.4 g/100 mL STPP对低盐条件下肌原纤维蛋白功能特性具有更好的改善作用。
