椰肉蛋白对文昌鸡肌原纤维蛋白凝胶保水性影响

提取文昌鸡肉中的肌原纤维蛋白,以浓缩肌原纤维蛋白质量为指标。研究表明,提取肌原纤维蛋白较优p H为7.0,较优离子强度为0.6 mol/L,在优化条件下,提取浓缩蛋白质含量为17.84%。测得肌原纤维蛋白凝胶的保水性为79.09%。     

干酪乳杆菌6033蛋白酶降解肌肉蛋白质的作用研究

本试验将干酪乳杆菌(Lactobacillus casei，Lc)6033蛋白酶液按5％的比例分别加入肌浆蛋白和肌原纤维蛋白提取液，然后设定不同的pH值，于15℃培养7d，定时取样，测定反应后的pH值、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)检测蛋白质的变化。结果发现：不同设定的肌浆蛋白和肌原纤维蛋白试验组在反应初期pH值均稍稍降低，随着反应进程，各试验组的pH值呈现出逐步升高的趋势；其中，肌浆蛋白以pH5．0、4．5组的变化较为明显，肌原纤维蛋白则以pH6．0、5．0、4．5组的变化较为明显。经7d振荡培养后，电泳检测发现，各试验组肌浆蛋白均表现出分解现象，尤其以pH5．0组和pH4．5组更为明显；而肌原纤维蛋白也都表现出了明显的分解现象，尤以pH5．0组肌原纤维蛋白分解最明显。     

添加海藻粉对鸡肉肌原纤维蛋白低钠热凝胶特性的影响

研究海藻粉的添加比例（0、2％、4％、6％、8％）对低食盐含量（0．2mol／L）条件下鸡胸肉肌原纤维蛋白的热凝胶强度和保水性的影响,并对流变学特性和T2弛豫时间进行分析,以探索低钠条件下肌原纤维蛋白热凝胶特性的改善途径.实验结果表明：添加海藻粉能显著提高（p〈0．05）肌原纤维蛋白低钠热凝胶的强度和保水性,在添加量为8％时分别达到最大值58．42g和88.3％;随着海藻粉添加量的增加,贮能模量C’呈现的初始值和终值均显著增大（p〈0．05）,同时T22向快的弛豫方向移动。对实验结果进行主成分分析表明,海藻粉的最适添加比例为4％～6％。     

NaCl对添加丝氨酸蛋白酶的肌原纤维蛋白凝胶特性的影响

以养殖大黄鱼作为研究对象,探究NaCl对添加了丝氨酸蛋白酶的肌原纤维蛋白凝胶特性的影响。首先对养殖大黄鱼肉经过提取分离纯化得到的丝氨酸蛋白酶进行研究,探讨其最适温度、最适pH以及NaCl对丝氨酸蛋白酶活性的影响。并进一步研究NaCl对含有丝氨酸蛋白酶的肌原纤维蛋白凝胶的质构特性、持水性、白度、拉曼光谱、荧光分析、微观结构等特性的影响。结果发现,丝氨酸蛋白酶的最适温度为50℃,最适pH值为7.0。NaCl的添加使肌原纤维蛋白凝胶的二级结构发生改变,蛋白凝胶结构越来越紧密稳定,但荧光强度相对有所下降。在NaCl质量浓度为0~20 g/L时,肌原纤维蛋白凝胶的胶黏性、咀嚼性不断上升,且白度增大。在NaCl添加量为40 g/L时,肌原纤维蛋白凝胶的持水性最强。因此可得出结论,添加NaCl后,丝氨酸蛋白酶的活性受到抑制,使其对肌原纤维蛋白凝胶的破坏减弱,从而改善鱼糜凝胶特性。     

菊粉对鲤鱼肌原纤维蛋白凝胶特性的影响

提取鲤鱼肌原纤维蛋白,通过不同温度热诱导条件研究不同浓度菊粉对肌原纤维蛋白凝胶的硬度、弹性、持水性和色差的影响,目的是提高鲤鱼肌原纤维蛋白凝胶特性.并且在肌原纤维蛋白中添加NaCl、CaCl2和Na4P2O7,研究三种盐对凝胶特性的影响.结果表明:在80℃加热条件下菊粉添加量为1%,肌原纤维蛋白凝胶的硬度和弹性最大;凝胶的持水性随着菊粉浓度增加先下降后升高;凝胶的白度随着菊粉的浓度增大而降低.添加1%菊粉条件下,同时添加不同浓度的NaCl、CaCl2和Na4P2O7表明,这几种盐均会使肌原纤维蛋白凝胶硬度和弹性显著降低.添加NaCl、CaCl2会降低肌原纤维蛋白的凝胶持水性,但添加Na4P2O7能够获得最大的凝胶持水性;添加CaCl2获得的凝胶白度最大.总之,菊粉添加量、加热温度和盐类会对鲤鱼肌原纤维的凝胶特性产生显著的影响.     

小麦麸膳食纤维对猪肉肌原纤维蛋白凝胶功能特性的影响

为开发低脂肪多纤维的健康肉制品,明确膳食纤维添加对肉制品品质的影响,以猪肉肌原纤维蛋白为研究对象,利用单因素分析法研究肌原纤维蛋白热诱导凝胶性质及小麦麸膳食纤维对猪肉肌原纤维蛋白功能特性的影响。结果表明：肌原纤维蛋白变性聚集的温度范围是40～70 ℃;肌原纤维蛋白凝胶硬度和保水性随肌原纤维蛋白质量浓度增加而增大,当质量浓度到达70 mg/mL时,凝胶硬度和保水性趋于稳定;pH值为5.5时肌原纤维蛋白凝胶硬度达到最大,凝胶保水性在pH 7.0时趋于稳定;离子强度为0.6 mol/L时凝胶的硬度和保水性趋于稳定。随着小麦麸膳食纤维添加量的增加,肌原纤维蛋白乳化性有所升高但是不明显,当添加量为5%时,乳化性增加7.4%,肌原纤维蛋白乳化稳定性降低;蛋白的弹性模量增大;凝胶硬度和保水性提高,添加量为4%时变化趋于平缓。随着膳食纤维粒径的减小,肌原纤维蛋白凝胶硬度和保水性逐渐提高;微观结构更加致密;蛋白弹性模量降低。由此可见,膳食纤维能够明显改变肌原纤维蛋白功能特性,通过在肉制品中添加适量的膳食纤维可以明显改良肉制品的风味,并替代脂肪,减少人体热量的摄入。     

影响鸭肉肌原纤维蛋白凝胶保水性的因素研究

以鸭胸肉为材料,提取鸭肉中的肌原纤维蛋白,研究溶液环境(蛋白浓度、NaCl浓度、pH)和加热方法(加热温度、加热时间、加热速率),对肌原纤维蛋白热诱导凝胶保水性的影响。研究结果表明:在一定范围内,鸭肉肌原纤维蛋白凝胶的保水性与蛋白溶解度呈正相关;随着蛋白浓度越大,NaCl浓度升高,凝胶保水性也相应提高;pH偏离蛋白的等电点越远,保水性越好;加热温度为70℃,加热时间为20 min,加热速率0.2℃/min～0.5℃/min,凝胶保水性最好。     

养殖暹罗鳄肉肌原纤维蛋白的理化性质

筛选养殖暹罗鳄肌原纤维蛋白含量最高部位,提取并分析离子强度、pH值和温度对肌原纤维蛋白溶液的溶解性、乳化性和热诱导凝胶特性的影响。结果表明：暹罗鳄尾部肌原纤维蛋白所占比例最高（（7.95±0.12） g/100 g,以湿质量计）,暹罗鳄尾肉中肌原纤维蛋白主要为肌球蛋白重链、副肌球蛋白、肌动蛋白和原肌球蛋白。在低离子强度条件下,肌原纤维蛋白的溶解度和乳化性较低,但有良好的凝胶特性,随着离子强度的升高,肌原纤维蛋白的溶解度和乳化性升高,凝胶特性则呈现下降趋势。随着pH值升高,肌原纤维蛋白溶解度呈现先迅速下降后升高的趋势,乳化性和凝胶特性则呈现持续缓慢下降的趋势,其中溶解度和保水性在pH 5.5达到最低点。随着热变温度升高,其凝胶特性显著增加,保水性先下降后略有升高,在低温（40 ℃）下有较好的保水性,在80 ℃保水性升高至又一峰值随后下降。结论：肌原纤维蛋白在NaCl浓度0.2 mol/L进行调配,并在80 ℃条件下加热处理,暹罗鳄肉类产品将具有较好的质构特性及保水性。     

宰后初期不同温度处理对鸭肉肌原纤维蛋白氧化及凝胶品质的影响

研究不同温度处理对宰后初期鸭肉肌原纤维蛋白氧化及凝胶特性的影响。分别将鸭胸肉在不同温度处理（0、40℃分别孵育1 h）,之后提取肌原纤维蛋白,测定蛋白氧化特征变化（羰基含量、巯基含量）以及对其凝胶特性（流变特性、质构和微观结构）的影响,并对蛋白特征使用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（sodium dodecyl sulfate-polyacrylamide gel electropheresis,SDS-PAGE）进行分析。结果表明：与对照组（0℃）肌原纤维蛋白相比,热处理组（40℃）肌原纤维蛋白中的羰基含量升高,而巯基含量降低52.7%,蛋白凝胶的保水性降低14.1%,凝胶强度降低45.5%,三者均显著降低（P<0.05）;两组间蛋白流变特性差异不明显,而SDS-PAGE分析发现,40℃处理组中部分肌浆蛋白附着于肌原纤维蛋白上,且凝胶网格结构整体较松散,说明在热处理过程中会伴随鸭肉肌原纤维蛋白发生氧化,从而使其凝胶特性受到影响。     

复合肌原纤维蛋白的凝胶特性

温度是影响蛋白质凝胶特性的主要因素。实验通过研究复合肌原纤维蛋白凝胶(猪肉肌原纤维蛋白、鲢鱼肉肌原纤维蛋白质量比分别为2∶0、1∶1、0∶2)在70、80、90、100℃加热时色泽、凝胶强度、质构特性、水分分布的变化,对复合肌原纤维蛋白凝胶和单一肌原纤维蛋白凝胶之间凝胶特性的差异和相关性进行研究,优化蛋白凝胶加热温度。结果表明:1∶1复合的肌原纤维蛋白凝胶能结合单一蛋白凝胶的特点,改善肌原纤维蛋白的凝胶特性;低场核磁共振表明,温度可通过影响水分分布来影响蛋白质的凝胶特性;蛋白凝胶特性随温度升高而增强,但温度过高会出现劣化,90℃是较为理想的加热温度。     

ROLE OF INITIAL MUSCLE pH ON THE SOLUBILITY OF FISH MUSCLE PROTEINS IN WATER

The solubility of the myofibrillar and cytoskeletal proteins in water was determined for the muscle tissue often species offish. The flesh of six white-muscled fish had pH's at the time of processing above pH 6.6 and greater than 80% of their myofibrillar/cytoskeletal proteins were soluble in water. The flesh of three pelagic species and a shark had pH values when processed below 6.6 and the water solubility of their myofibrillar and cytoskeletal proteins was less than 40%. When the washed minced muscle of one of the white-fleshed species, cod, was exposed to low pH, the solubility of its myofibrillar and cytoskeletal proteins decreased substantially. The water solubility of the cod myofibrillar and cytoskeletal proteins could be reestablished by washing the acid-treated cod flesh with neutral salt solutions. It is suggested that pH values below 6.6 modify certain proteins which prevent the water-extractability of the rest of the myofibrillar and cytoskeletal proteins from being expressed.     

离子强度和pH值对肌原纤维蛋白热诱导凝胶特性的影响

以肌原纤维热诱导凝胶的保水性和质构特性,包括硬度、弹性、内聚性、胶黏性、回复性为指标,考察离子强度和pH值对猪背最长肌肌原纤维热诱导凝胶特性的影响.结果表明,离子强度和pH对凝胶不同特性的影响存在差异,综合各种指标,离子强度为0.5,pH值在6.5和7.0之间有利于形成较好的凝胶.不同条件下凝胶形成的机制可能存在差异.凝胶的硬度与弹性、胶黏性和保水性相关性显著(P＜0.05),可以作为重点考察的指标.     

SOLUBILITY OF THE PROTEINS OF MACKEREL LIGHT MUSCLE AT LOW IONIC STRENGTH

Over 90% of the proteins of mackerel light muscle were soluble in solutions of physiological ionic strength or less. To accomplish this solublization, it was necessary to extract certain proteins at moderate ionic strength and neutral pH before extracting the rest of the myofibrillar and cytoskeletal proteins in water. Six proteins were favorably solubilized by sodium chloride solutions of moderate ionic strength at neutral pH under conditions that allowed later dissolution of myofibrillar and cytoskeletal proteins in water. The possibility is suggested that three of these proteins were involved in preventing the solubilization in water of other myofibrillar and cytoskeletal proteins of mackerel light muscle. Based on molecular masses and relative abundance, these proteins could possibly be M-protein (166 kDa), α-actinin (95 kDa) and desmin (56 kDa).     

ROLE OF pH IN GEL FORMATION OF WASHED CHICKEN MUSCLE AT LOW IONIC STRENGTH

This work was designed to test the hypothesis that it is not solubilization of the myofibrillar proteins per se that is required to form good gels at low salt concentrations, but the protein‐containing structures must be disorganized. Gels were made from washed minced chicken breast muscle at 0.15, 0.88, and 2.5% sodium chloride. The gels made with varying salt concentrations were evaluated either at pH 6.0–6.5 or pH 7.0–7.4. Strain values, an indicator of protein quality, were high only at neutral pH in the gels containing 0.15 or 0.88% salt. At 2.5% salt, strain values of gels made at acid pH were superior to those at the low salt concentrations at acid pH, but inferior to gels with 2.5% salt at neutral pH. Poor gels were obtained at 0.15% salt and low pH whether or not there was an intermittent adjustment to neutral pH. A neutral salt wash markedly increased the water content of the mince, suggesting that solubility‐inhibiting proteins were removed. Good quality gels were obtained in the absence of any detectable solubilization of myosin and only minimal solubilization of actin.     

Protein extractability and thermal gel formability of myofibrils isolated from skeletal and cardiac muscles at different post-mortem periods

The effects of the post-mortem ageing period on the extractability of myofibrillar proteins from pork cardiac and rabbit skeletal muscles under various conditions of pH and ionic strength were studied with particular reference to the changes in the solubility of individual myofibrillar proteins and their denaturation characteristics. The ultimate influence of these changes on the heat-induced gel forming ability of myofibrils isolated from cardiac and skeletal muscles at different post-mortem stages was also investigated. Results showed that pork cardiac myofibrils always exhibited lower solubility than those from rabbit skeletal muscles under identical conditions of pH, ionic strength and temperature. SDS-PAGE profiles indicated several quantitative differences in the relative proportion of individual protein species present in cardiac and skeletal myofibrils. The solubility of various proteins present in myofibrils was also affected differently on heating in 0-1 and 0-6 _M NaCl solution at various pH values. Thermal denaturation of cardiac myofibrils occurred at about 10°C higher than that of skeletal myofibrils as revealed by differential scanning calorimetry. Cardiac myofibrils formed much weaker heat-induced gels than those produced by skeletal myofibrils under identical conditions of temperature, pH, ionic strength and protein content.     

Timed Emulsification Studies with Chicken Breast Muscle: Soluble and Insoluble Myofibrillar Proteins

Emulsion formation with chicken breast muscle was investigated using timed emulsification. High-salt soluble proteins (pH 7.0, 0.6M NaCl) extracted from previously washed muscle (pH 7.0, 0.05M NaCl) were removed from the aqueous phase as mixing time increased. Low- and high-salt exhaustively washed muscle, resuspended in either 0.15 or 0.6M NaCl, pH 7.0, still exhibited good emulsion properties. The pellet protein decreased (> 90%) as mixing time increased from 0 to 5 min. Addition of sodium pyrophosphate to 0.6M NaCl suspensions of 0.05M NaCl washed muscle resulted in an increase in solubility of myofibrillar proteins and a general improvement in emulsification properties. High-salt insoluble proteins may play an important role in emulsion formation.     

溶液环境对PSE猪肉肌原纤维蛋白溶解度及热诱导凝胶强度的影响

以正常猪肉和PSE 猪肉背最长肌为材料,采用分光光度法、物性测定法和SDS-PAGE 凝胶电泳法研究pH值、NaCl 浓度和三聚磷酸钠(TPP)浓度对肌原纤维蛋白溶解度和凝胶强度的影响。结果表明：pH 值、NaCl 浓度和三聚磷酸钠浓度对猪肉肌原纤维蛋白质的溶解性和凝胶强度均有显著影响(P ＜ 0.05),改善体系环境、提高蛋白质溶解度可提高PSE 肉凝胶功能特性。     

儿茶素对肌原纤维蛋白氧化、结构及凝胶特性的影响

采用羟自由基氧化体系（10 μmol/L FeCl3、100 μmol/L VC和1 mmol/L H2O2）研究不同添加量儿茶素（10、50、100、150 μmol/g）对肌原纤维蛋白氧化、结构及凝胶特性的影响,同时以未氧化和氧化后未添加儿茶素（0 μmol/g）肌原纤维蛋白作为对照组,对肌原纤维蛋白羰基含量、总巯基含量、表面疏水性、溶解度、粒径分布、凝胶强度、凝胶保水性及肌原纤维蛋白流变特性进行测定,并观察凝胶微观结构。结果表明：添加儿茶素能减少羰基化合物的产生,但添加量过高会促进肌原纤维蛋白氧化;与未氧化和未添加儿茶素组相比,添加儿茶素降低了肌原纤维蛋白表面疏水性;随着儿茶素添加量增加,肌原纤维蛋白巯基含量逐渐降低,溶解度显著降低,粒径逐渐增大,凝胶强度和保水性逐渐下降,凝胶微观结构更加疏松多孔,蛋白胶束聚集,中、高添加量（50、100、150 μmol/g）儿茶素使得肌原纤维蛋白失去典型的流变曲线。中、高添加量儿茶素与肌原纤维蛋白发生共价交联,并导致肌原纤维蛋白发生疏水性聚集,最终削弱了肌原纤维蛋白的凝胶特性。