Effect of sodium starch octenyl succinate-based Pickering emulsion on the physicochemical properties of hairtail myofibrillar protein gel subjected to multiple freeze-thaw 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.

Oxidative mechanism of chicken wooden breast myofibrillar protein

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.

The effect of protein oxidation on the formation of advanced glycation end products after chicken myofibrillar protein glycation

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.

Effects of phosphorylated ovalbumin on the quality of pork myofibrillar protein gel:an insight into gelling and physicochemical properties

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.

Dynamic viscoelastic behaviour,gelling properties of myofibrillar proteins and histological changes in shrimp(L.vannamei)muscles during ice storage

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.

Improvement of gelation properties of myofibrillar proteins from porcine longissimus dorsi muscle through microwave combined with air convection thawing treatment

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.

Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources:A Comparative Study

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.

冻融与冻藏对乌鳢肌原纤维蛋白与酸菜鱼汤中特征风味物质结合特性的影响

为探究冷冻处理对于鱼片与酸菜鱼汤中风味物质的结合特性影响,以乌鳢的肌原纤维蛋白为对象,研究冻融及冻藏处理对其理化特性及与己醛、辛醛、芳樟醇、月桂烯结合能力的变化。结果表明经过7 d贮藏后,冻融组肌原纤维蛋白溶解度降低了约26%,相较于冻藏组,蛋白质氧化和三级结构变化程度更高,产生了更多可溶性聚集体;冻藏组溶解度降低了约33%,相较于冻融组,溶解度降低更加显著(P<0.05),产生了更多不溶性聚集体。影响肌原纤维蛋白冷冻聚集的主要作用力是非共价键。分子对接结果表明,芳樟醇、己醛和辛醛通过疏水作用和氢键与蛋白质结合,月桂烯与蛋白结合的主要驱动力为疏水相互作用。冷冻处理通过减少蛋白质与醛类化合物结合的巯基基团和氢键,降低了对己醛和辛醛的结合能力,蛋白质表面疏水性的提高,增加了对月桂烯和芳樟醇的结合能力,冻融处理后蛋白质对于月桂烯的结合能力强于冻藏处理组。研究结果可以为冷冻酸菜鱼预制品的风味控制提供理论依据和参考。

虾肉蛋白在乳酸菌发酵过程中的降解及其体外抗氧化活性的动态变化

本实验探究了在乳酸肠球菌发酵过程中虾肉肌原纤维蛋白和肌浆蛋白的降解及其产物(肽)抗氧化活性变化。结果表明,与未发酵时相比,随发酵时间的延长,两种蛋白的pH值均显著下降(P<0.05),蛋白酶活力均显著升高(P<0.05)。凝胶电泳结果表明,发酵使两种蛋白质均发生了降解,其中肌浆蛋白的降解程度更为明显。发酵后两种蛋白体系的2,2’-联氮双(3-乙基苯并噻唑啉-6-磺酸)(2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid),ABTS)阳离子自由基清除率、1,1-二苯基-2-三硝基苯肼(1,1-diphenyl-2-picrylhydrazyl,DPPH)自由基清除率、Fe^(3+)还原力均显著增强(P<0.05),其中肌浆蛋白降解产物(肽)的抗氧化能力显著高于肌原纤维蛋白降解产物(P<0.05)。相关性分析显示,蛋白酶活力与肌浆蛋白的水解度及其产物的ABTS阳离子自由基清除率、DPPH自由基清除率以及Fe^(3+)还原能力呈显著正相关(P<0.05、P<0.01)。综上,通过乳酸肠球菌发酵虾肉蛋白,尤其是肌浆蛋白可得到具有较高抗氧化能力的肽。本研究可为水产加工(如鱼糜)过程中产生肌浆蛋白的充分利用和抗氧化活性肽的开发提供理论依据。

4种提取方法对对虾肌原纤维蛋白提取率、空间结构和热稳定性的影响

【目的】获取提取率高且结构完整的凡纳滨对虾(Litopenaeus vannamei)肌原纤维蛋白。【方法】通过0.5 mol/L KCl、53 kHz超声辅助0.5 mol/L KCl、53 kHz超声辅助质量分数5%十二烷基硫酸钠(SDS)和RIPA裂解液这4种提取方法提取对虾肌原纤维蛋白,以肌原纤维蛋白提取率和结构完整性为评价指标,采用光谱学和凝胶电泳生化,评价四种提取方法对对虾肌原纤维蛋白提取率、空间结构和热稳定性的影响。【结果】53 kHz超声辅助0.5 mol/L KCl、0.5 mol/L KCl、53 kHz超声辅助5%SDS和RIPA裂解液4种方法所得提取率分别为(87.99±3.08)%、(53.76±3.90)%、(75.59±0.95)%和(95.46±4.49)%。53 kHz超声辅助0.5 mol/L KCl提取的蛋白中肌钙蛋白和原肌球蛋白蛋白丰度较高,0.5 mol/L KCl和53 kHz超声辅助质量分数5%SDS提取的肌球蛋白重链和肌动蛋白蛋白丰度较高;相较于0.5 mol/L KCl,超声辅助提取可最大限度保持肌原纤维蛋白天然结构,α-螺旋结构保留完好;0.5 mol/L KCl提取可较好维持肌原纤维蛋白的酰胺Ⅰ带结构。RIPA裂解液提取对肌原纤维蛋白二级结构有明显破坏,热稳定性仅为原蛋白的(60.63±4.46)%。【结论】综合提取率、空间结构和热稳定性结果,采用53 kHz超声辅助5%SDS提取可获得质量最佳的凡纳滨对虾肌原纤维。本研究可为后续深入解析冷藏对虾品质劣变和开发高效控制技术提供高质量的肌原纤维蛋白。

坛紫菜多糖对微冻南美白对虾仁肌原纤维蛋白氧化和结构特性的影响

该研究通过探讨坛紫菜多糖浸泡的南美白对虾仁在微冻过程中肌原纤维蛋白氧化特性和结构特性的变化规律,从蛋白质角度揭示坛紫菜多糖抗冻保鲜的潜在机制。将虾仁分别用5 mg/mL坛紫菜多糖,蒸馏水(空白对照)和5 mg/mL焦磷酸钠(阳性对照)浸泡处理后于-3℃微冻贮藏,每5 d测定指标。结果表明,与对照组相比,坛紫菜多糖浸泡虾仁可显著延缓总巯基含量下降,防止羰基含量和表面疏水性上升,阻碍平均粒径增加和Zeta电位绝对值的下降(P<0.05),抑制肌原纤维蛋白的氧化和聚集。圆二色光谱分析表明,坛紫菜多糖显著抑制肌原纤维蛋白α-螺旋相对含量的降低(P<0.05)。内源荧光光谱分析表明,坛紫菜多糖能缓解肌原纤维蛋白中发色基团暴露,维持蛋白空间结构稳定性。扫描电镜结果显示,坛紫菜多糖能保持虾肌肉组织微观结构的完整性。该研究为坛紫菜多糖作为新型绿色无磷抗冻保鲜剂添加到水产品冷冻过程中保护蛋白质特性提供理论依据。

不同形态的可得然凝胶对肌原纤维蛋白凝胶特性和体外消化特性的影响

本文主要研究可得然胶以热可逆凝胶(Thermal reversible curdlan gum,TRC)和热不可逆凝胶(Thermal irreversible curdlan gum,TIRC)形态添加对肌原纤维蛋白(Myofibrillar Protein,MP)凝胶特性及其体外消化特性的影响。结果表明,随着TRC或TIRC浓度的增加,MP凝胶的凝胶强度和持水性显著增加(P<0.05),在添加量为0.4%时达到最大值,此结果可以通过动态流变学行为得到证实。同时,TRC或TIRC的存在促进α-螺旋转化为β-折叠,疏水相互作用和二硫键是维持共混凝胶的主要作用力。微观结构表明,TRC或TIRC添加可以促进形成致密且均匀的蛋白网状结构。然而,由于TRC或TIRC与MP之间互作方式不同,引起共混凝胶微观结构存在差异。此外,TRC或TIRC添加阻碍蛋白质分解成小分子肽和氨基酸,显著降低蛋白消化率(P<0.05),尤其当添加量为0.3%(w/w)时,消化率从77.53%降低到71.66%。然而,每种添加形式对MP凝胶的体外消化率没有显著的影响(P>0.05)。因此,本研究为TRC或TIRC对MP凝胶形成和体外消化的影响提供理论依据,同时为可得然胶在肉类工业中的应用奠定技术支撑。

谷氨酰胺转氨酶催化交联对肌原纤维蛋白凝胶特性影响的研究进展

在肉类工业中,谷氨酰胺转氨酶(transglutaminase,TGase)作为一种高效的蛋白质交联剂,能够在改变肌原纤维蛋白(myofibrillar protein,MP)分子结构的基础上改善其热诱导凝胶特性,进而提升肉制品的品质。与此同时,交联度(degree of cross-linking,DCL)是表征TGase催化交联效果的最重要的指标,其对于分析TGase的共价交联作用对MP构象、理化性质和凝胶特性的影响尤为重要。因此,本文系统综述了TGase催化MP共价交联过程中DCL的影响因素,同时深度解析外源添加物和新型加工技术影响TGase催化交联效果的分子作用机制。旨在建立TGase调控下的MP“结构修饰-分子机制-品质改善”之间的相互关系,以期为构建新型肉制品提供创新性理论和技术支持。

亲水胶体调控肌原纤维蛋白热诱导凝胶形成机制的研究进展

肌原纤维蛋白(myofibrillar protein,MP)是肌肉中非常重要的蛋白质,其在热诱导过程中能够形成三维凝胶网络结构,从而最终影响肉制品的品质特性。在肉类工业中,添加不同来源的亲水胶体能够显著增强MP凝胶强度、持水性及相关的功能特性,从而获得具有最佳品质的终产品。然而,在MP热诱导凝胶的形成过程中,有很多因素直接影响亲水胶体与MP之间的相互作用,最终对MP凝胶特性产生显著影响。本文系统综述了MP的凝胶机理,探讨了不同亲水胶体与MP之间的互作机制,梳理了亲水胶体调控MP热诱导凝胶形成的关键因素及其对最终MP凝胶特性的影响,为亲水胶体调控肉制品品质关键技术体系奠定理论基础,并为下一步实际应用提供技术指导。

姜黄提取物对牦牛肌原纤维蛋白抗氧化性及凝胶特性的影响

该研究在羟基自由基氧化体系诱导牦牛肉肌原纤维蛋白(MyofibrillarProtein,MP)氧化过程中加入姜黄提取物,探索姜黄提取物对氧化蛋白理化性质及结构的影响,以及对MP凝胶结构和消化率的影响。研究表明:姜黄提取物质量浓度<200μg/mL时,对氧化MP的羰基、巯基含量,溶解度、持水性等无显著影响(P>0.05);当姜黄质量浓度在200~800μg/mL时,氧化MP的羰基含量下降为7.44 nmol/mg,巯基含量、溶解度、白度、持水性、凝胶强度增大,各含量的最大值分别为41.6 nmol/mg、29.79%、81.37、90.44%、59.32,姜黄提取物对蛋白氧化有明显的抑制作用;但随着浓度继续升高,姜黄提取物中的酚类物质能破坏蛋白分子结构,使凝胶性能受到破坏,姜黄提取物添加后对牦牛肉MP凝胶的体外消化率无显著影响(P<0.05)。姜黄提取物在200~800μg/mL质量浓度范围内在牦牛肉MP氧化中表现出较好的抗氧化活性,为牦牛肉抗氧化提供一定的理论依据。

基于多光谱技术分析绿原酸与肌原纤维蛋白相互作用的初步研究

本研究以高白鲑肌原纤维蛋白(Myofibrillar Protein,MP)为研究对象,探究不同浓度(6、30、150、300μmol/g)绿原酸(Chlorogenic Acid,CA)与MP相互作用的结构变化及结合性质。在25℃下孵育形成不同CA-MP复合物,通过测定复合物的理化性质(总巯基,表面疏水性),二级,三级结构变化(傅里叶红外光谱、同步荧光、三维荧光),结合性质(紫外光谱,荧光猝灭及热力学参数)分析CA-MP复合物相互作用情况。结果表明,在300μmol/g CA存在下,蛋白总巯基含量和表面疏水性分别骤降25.65%,40.26%(P<0.05);蛋白质二级结构随之展开,α-螺旋含量下降至11.73%,造成蛋白结构稳定性降低;同步荧光与三维荧光光谱表明CA对蛋白荧光具有猝灭作用,且色氨酸比酪氨酸的猝灭效果高7.90%。紫外光谱和荧光猝灭证实CA-MP形成复合物且二者的结合为静态猝灭,热力学参数进一步验证二者相互作用的主导力为疏水作用力。本研究旨在为多酚与高白鲑MP相互作用提供有价值的信息,为后续对不同结构多酚与高白鲑肌球蛋白的相互作用机制提供研究基础。

水解对低盐鸭肉肌原纤维蛋白结构和功能特性的影响

为研究水解时间(0、20、40、60、80 min)对低盐溶液中鸭肉肌原纤维蛋白的结构和功能特性的影响,本文用胰蛋白酶水解鸭肉肌原纤维蛋白(Myofibrillar protein,MP),通过分析水解处理后的水解度、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)、溶解度、表面疏水性、二级结构、荧光光谱、Zeta电位和乳化性,对水解物的结构和功能特性进行评估。结果表明:在低盐溶液中,随着水解时间的延长,溶解度显著升高(P<0.05),表面疏水性先降低后升高,乳化性先升高后降低;当水解时间为40 min时,水解度为4.15%,鸭肉MP的溶解度和乳化性达到最高,分别达到60.57%和21.2 m2/g;表面疏水性最低(40.85 BPB/μg)。此外,蛋白结构变化显著,α-螺旋含量减少,内源性色氨酸荧光强度明显高于未水解组,且Zeta电位绝对值升高。综上所述,在低盐溶液中,水解40 min可以有效改善鸭肉MP的结构和功能特性。

南瓜籽蛋白-卡拉胶乳液脂肪替代物对肌原纤维蛋白凝胶特性的影响

为进一步开发蛋白-多糖复合脂肪替代物在低脂肉制品中的应用,本研究以南瓜籽蛋白(Pumpkin Seed Protein,PSP)和卡拉胶为原料制备复合乳液脂肪替代物,并将其加入到肌原纤维蛋白(Myofibrillar Protein,MP)中形成热诱导凝胶,通过对凝胶水分分布、质构特性、微观结构、流变学特性等指标的测定,研究不同添加量下PSP-卡拉胶形成的复合乳液对MP凝胶特性的影响。结果表明,PSP-卡拉胶复合乳液添加量为50%显著提高了凝胶持水性和凝胶强度(P<0.05),MP凝胶的质构特性得到了改善,凝胶蒸煮损失和冻融稳定性显著降低(P<0.05)。流变学特性表明,凝胶的G'始终高于G'',能够形成具有弹性的凝胶结构,并且表现出较为致密均一的微观结构。因此,PSP-卡拉胶复合乳液添加量为50%对肌原纤维蛋白的凝胶性能有较好的改善。

3种磷酸盐对白鲢鱼肌原纤维蛋白磷酸化的影响

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。

pH对大黄鱼肌原纤维蛋白结构性质及乳化性的影响

为深入探究大黄鱼肌原纤维蛋白(MP)的乳化性,以满足大黄鱼蛋白质高值化开发利用的需求。实验探究了不同pH对大黄鱼MP结构性质及其乳化性的影响。采用pH分别为2、4、6、8、10、12的低盐磷酸缓冲液处理大黄鱼MP,通过SDS-PAGE分析大黄鱼MP降解情况,利用接触角测量仪和荧光分光光度计考察其疏水性变化。将不同pH下大黄鱼MP溶液与大豆油以体积比为1∶1的比例经高速均质制备乳液,并对其乳滴电位、粒径以及乳液的乳析指数进行测定,综合分析在不同pH下乳液的稳定性。SDS-PAGE电泳结果表明,在pH 4时,大黄鱼MP条带颜色较浅,在pH 6~12时,肌球蛋白重链条带基本消失,肌动蛋白条带颜色逐渐加深,且在浓缩胶顶部出现了高分子聚集物。对接触角和荧光光谱的综合分析表明,大黄鱼MP疏水性随pH增加而增加。对不同pH下MP乳液特性分析显示,在pH 8时,乳滴带负电且Zeta电位绝对值大[(49.63±1.52)mV]、粒径较小、乳液稳定性较好,而pH 12条件下容易出现破乳,不利于乳液的稳定。在pH 8时,大黄鱼MP结构更有利于提升乳液稳定性。研究表明,在弱碱性条件下更有利于大黄鱼MP形成稳定的乳液体系。pH对大黄鱼MP结构性质和乳化性的影响探究,有望为大黄鱼MP在食品工业中的开发利用提供理论依据。