Thermally Induced Interactions and Gelation of Combined Myofibrillar Protein from White and Red Broiler Muscles

The gelling properties of broiler myofibrillar protein were studied by determining protein-protein interactions during heating. Breast and leg salt-soluble protein (SSP) showed 1–3 transitions in protein-protein interactions within pH 5.5–6.5. The maximum transition temperatures of leg SSP decreased when leg SSP was mixed with breast SSP. The combined breast/leg myofibrils formed stronger gels than leg myofibrils alone at pH ≥ 6.0, and stronger gels than breast myofibrils alone at pH < 6.0. The results suggest that interactions existed between breast and leg myofibrillar proteins, and the transitions in these interactions were useful for predicting gel strength of the combined breast/ leg myofibrils.     

猪腿纤维蛋白的热致胶凝与功能性质(英文)

本实验探讨了蛋白浓度和 pH 值对猪腿纤维蛋白的溶解度、凝胶强度、蒸煮失重以及热致胶凝性质的影响。在 0.6mol/L、pH6.0 的 NaCl 溶液中,纤维蛋白的胶凝性最强,凝胶强度随着蛋白浓度的增加而增加。然而,蛋白浓度的增加对蒸煮失重和蛋白质溶解度产生不利影响。猪腿纤维蛋白在 4℃贮存一段时间后,其溶解度有所增加。实验结果表明:pH 值对猪腿纤维蛋白的溶解度、凝胶强度、蒸煮失重和粘弹性都有一定的影响。在 pH6.0 时,蛋白的凝胶强度最大,而在 pH7.0 时,蛋白溶解度最大,蒸煮失重最小。     

Thermal Gelation of Stretched and Cold-Shortened Bovine Sternomandibularis Muscle and Myofibrils

Muscle gels (10% protein) and myofibril gels (8% protein) were prepared at pH 6.0 with 2% NaCl and a heating rate of 0.7°C/min. No difference in gel strength occurred between stretched and cold-shortened muscles, but cooking loss was lower for stretched muscle. Stretched muscle sarcomeres were longer than those of cold-shortened muscle. The myofibril fraction from stretched muscle had higher gel strength, viscosity index, elasticity, and lower cooking loss than that from cold-shortened muscle. These results suggest that the contractile state of the muscle affects protein binding and water binding of the myofibrillar fraction.     

不同盐对鲤鱼肌原纤维蛋白结构和凝胶特性的影响

肌原纤维蛋白是鱼肉中的主要蛋白质,对鱼糜类制品的质量起到关键的作用。文中研究了NaCl、CaCl2和Na4P2O73种盐类及其浓度对鲤鱼肌原纤维蛋白结构特性(表面疏水性、蛋白聚合程度)和凝胶特性(质构、微观结构、蛋白浊度)的影响。结果表明:鲤鱼肌原纤维蛋白的等电点为5.5;3种盐加入肌原纤维蛋白后会引起肌原纤维蛋白发生一定程度的聚集,表面疏水性降低;随着盐浓度的增大,肌原纤维蛋白凝胶硬度、弹性、浊度降低;添加CaCl2比其它盐类更明显降低鱼糜的凝胶硬度、弹性和浊度,且差异性显著(P<0.05);NaCl和Na4P2O7使鱼糜凝胶微观结构更致密、CaCl2使鱼糜凝胶微观结构变得松散。因此,在鲤鱼肌原纤维蛋白中添加NaCl、CaCl和NaPO对鱼糜肌原纤维蛋白结构和凝胶特性均有不同程度的影响。     

牛血浆蛋白对猪肉盐溶蛋白质凝胶特性的影响

以牛血浆和猪后腿肉为原料,研究牛血浆蛋白对猪肉盐溶蛋白质加工特性的影响。结果表明：牛血浆具有改善猪肉盐溶蛋白质凝胶特性的作用,当pH6.5时,添加牛血浆蛋白0.9g/100mL时效果最佳;添加0.9g/100mL牛血浆蛋白的猪肉盐溶蛋白凝胶煮制损失、凝胶保水性、凝胶强度与添加0.125g/100mL微生物转谷氨酰胺酶(MTG)的凝胶相当。     

Thermal Gelation Properties of Protein Fractions from Pork and Chicken Breast Muscles

Thermal gelation properties of myosin, actin, myofibrils (MF), sarcoplasmic protein (SP) and connective tissue (CTS) from pork semimem-branosus and chicken breast (CB) were evaluated. Gels were prepared at pH 6.0, 2% NaCl and cooked to 70°C at 0.7°C/min. Pork myosin had a higher gel strength and a lower cooking loss than CB myosin at 7% protein. Actin from both species did not form a measurable gel. MF gels from pork and CB had the lowest cooking loss while CTS and SP had the highest cooking loss. Difference in gel strength between muscle and MF+SP+CTS at 7% protein was not consistent with that at 10% protein.     

3种鱿鱼冻藏过程中肌原纤维蛋白功能特性变化

为探讨阿根廷鱿鱼、北太平洋鱿鱼(以下简称北太鱿鱼)和秘鲁鱿鱼冻藏过程中肌原纤维蛋白功能特性的变化情况.将3种鱿鱼于-18℃C冰箱中冻藏,分别于0、15、30、45、60、75、90、105 d和120 d进行取样,分析测定鱿鱼肌肉中肌原纤维蛋白质量浓度、溶解性、浊度、乳化能力、Ca2+-ATPase活力、起泡性及泡沫稳...     

肌原纤维蛋白热诱导凝胶特性研究进展

肌原纤维蛋白质是肌肉中一类重要的结构蛋白质群,它对于肉食制品的品质和特性具有非常重要的影响.肌原纤维蛋白的凝胶特性是形成肉制品独特的质构、保水性、乳化性以及感官特性的决定性因素.本文介绍了肌原纤维蛋白凝胶机制、功能特性及其影响因素,为进一步了解肉制品加工特性提供一定理论指导.     

Chemical Modification and Functional Properties of Acylated Beef Heart Myofibrillar Proteins

Beef heart myofibrils were acylated with 0.1, 0.3, 0.6, 0.8, 1.0, 1.5, 2.0, 3.0, and 5.0 mmoles anhydride/g protein, at pH 8.0–8.5 and 2–3°C, with acetic anhydride (AA), succinic anhydride (SA), cis,cis,cis,cis-tetrahydrofuran-2,3,4,5-tetracarboxylic dianhydride (FA), and 1,2,4-benzenetricarboxylic anhydride (BA). The anhydride reacted with e-amino groups of lysine, sulfhydryl groups, and hydroxyl groups of tyrosine, serine, and threonine. Chemically modified beef heart myofibriliar proteins were superior to native heart myofibriliar proteins in solubility, emulsifying capacity, emulsion activity, and emulsion stability in a low salt solution of 0.1M NaCl, 0.05M potassium phosphate at pH 7.4 and 6.0. Protein modified with 0.5 mmole anhydride/g protein in 0.2M NaCl had a solubility greater than unmodified proteins in 0.6M NaCl at pH 7.4. Chemical modification also altered the pH-solubility profile. The chemically modified beef heart myofibrillar proteins exhibited an emulsifying capacity at pH 6.0 and 7.4 that was greater than that of the native proteins at pH 7.4. The recommended extent of acylation for modifying beef heart myofibrils on a gram protein basis is 0.6 mmole AA, 1.5 moles SA, 0.6 mmole FA, and 0.6 mmole BA.     

大足黑山羊宰后成熟过程中肌原纤维蛋白功能性质的变化

以大足黑山羊后腿肉为原料,研究羊肉宰后成熟过程中肌原纤维蛋白（myofibrillar protein,MP）功能性质的变化。结果表明：随着宰后成熟时间的延长,羊肉MP的溶解度、乳化活性指数和乳化稳定性均呈先下降后上升的趋势,且在宰后24 h达到最小值;表面疏水性、凝胶硬度和弹性及凝胶蒸煮损失均呈先增加后下降的变化趋势,且在宰后24 h达到最大值。综合各项指标的变化规律,从羊肉加工性能的角度考虑,大足黑山羊羊肉的最佳成熟时间为72 h。     

籽瓜种子蛋白对肌原纤维蛋白功能的影响

本研究以籽瓜种子为原料,利用碱溶酸沉方法提取籽瓜种子蛋白,在40、60、80℃条件下获得不同籽瓜种子蛋白,分别进行分子质量、溶解度测定,并与肌原纤维蛋白形成凝胶,对凝胶作用力、弹性、回弹性、粘结性、水相分度、白度进行试验。结果表明,40~80℃范围内随着提取温度的升高,籽瓜种子蛋白溶解度先升高后降低差异显著(P0.05),并获得4个吸收峰,峰1为699~103ku的大分子蛋白聚集体,峰2、峰3分别为340、212 ku的球蛋白,及10~54 ku部分清蛋白、球蛋白的亚基,随着碱溶温度继续升高,峰2、峰3逐渐消失。籽瓜种子蛋白与肌原纤维蛋白形成凝胶的三维网状结构稳定性通过疏水键、氢键、以及二硫键维持,其中疏水键、氢键为主要作用力。碱溶温度为60℃时,WPS与MP形成凝胶弹性较好、保水性较好,差异显著(P0.05)。随着温度的增加,凝胶白度逐渐加,WPS结构发生改变、变性,差异显著(P0.05)。由此可知,温度对籽瓜种子蛋白结构、功能影响较大,不同碱溶温度提取的籽瓜种子蛋白对肌原纤维蛋白功能影响差异显著,碱溶温度为60℃时,获得籽瓜种子蛋白与肌原纤维蛋白形成的凝胶有利于改善对肉制品品质,可作为非肉蛋白稳定剂添加到猪肉制品中。     

Heat-Induced Gelation of Myofibrillar Proteins and Myosin from Fast- and Slow-Twitch Rabbit Muscles

Heat-induced gelation of myofibrillar proteins and myosin (0.6M; pH 6.0) from rabbit fast- and slow-twitch muscles was analyzed by thermal scanning rheometry. Proteins from slow-twitch muscle exhibited higher thermostability and lower gel strength than those from fast-twitch muscle. Purifying myosin from myofibrillar proteins changed heat-gelation profiles and generally increased gel rigidity at 80°C. However, the effect of some proteins on the gelation of myosin was muscle dependent. Complete elimination of actin decreased the heat-gelling ability of slow myosin and increased that of fast myosin. Also, elimination of C-protein led to a greater increase in rigidity of gels from slow myosin than from fast myosin. The heat-behavior of the different protein fractions was related to the degree and type of aggregation in the gel.     

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。     

牛血浆蛋白凝胶特性研究

研究不同加工条件如蛋白浓度、加热温度、离子强度和pH对牛血浆蛋白凝胶特性的影响。结果表明:蛋白浓度的提高有利于凝胶的形成,且形成凝胶的最低血浆蛋白浓度是4.0%;4.8%的血浆蛋白,线性升温到85℃保温20 min,能够很好形成凝胶,呈果冻状,光滑有弹性;NaCl浓度在1.0 mol/L以下时,血浆蛋白凝胶强度随离子强度的变化是先增加后减小,0.3 mol/L时取得最佳效果;在pH6.0~9.0范围内,pH为9.0时牛血浆蛋白凝胶的凝胶强度较好,保水性高,蒸煮损失低。NaCl和pH对于牛血浆蛋白的凝胶特性有极显著的互作效应。     

桑叶蛋白的功能特性研究

采用超声波辅助提取结合盐酸沉析法提取桑叶蛋白,研究pH值、离子强度、蔗糖质量浓度和温度对桑叶蛋白功能特性的影响。结果表明：远离其等电点时,桑叶蛋白具有良好的持水性、溶解度、乳化性及乳化稳定性、起泡性;桑叶蛋白的持水性、溶解度和起泡性与NaCl浓度(0～1.0mol/L)呈正相关,而过高的离子强度(NaCl浓度高于0.6～0.8mol/L)会使桑叶蛋白的乳化性和乳化稳定性下降;蔗糖的加入会增加桑叶蛋白的持水性,但会降低其溶解度和起泡性,对桑叶蛋白的乳化性和乳化稳定性影响不大;桑叶蛋白的吸油性和起泡性与温度(4～80℃)呈正相关,持水性、溶解度、乳化性及乳化稳定性于60℃时最好。     

不同漂洗处理后冻藏对鲤鱼蛋白功能特性的影响

蛋白质氧化是引起食品加工及贮藏过程中品质发生劣变的一个主要原因。本文以鲤鱼肉为研究对象,主要研究鱼糜加工过程中经不同漂洗处理后冻藏对鲤鱼肌原纤维蛋白功能特性的影响。把鱼肉经不同方式漂洗[未漂洗;传统漂洗;添加抗坏血酸钠漂洗;添加没食子酸丙酯(PG)漂洗]后置于-25℃,经不同时间(0、30、60、90、120 d)冷冻贮藏后,利用质构仪、电子显微镜、流变仪等设备对鲤鱼肌原纤维蛋白乳化性、凝胶性以及流变性等指标进行测定,结果表明冻藏过程中发生的蛋白质氧化会引起鲤鱼肌原纤维蛋白各项功能特性降低,在漂洗过程中加入PG处理的鱼肉功能特性改变最小,说明添加PG漂洗可以有效地抑制蛋白质氧化的发生,从而减少鲤鱼肌原纤维蛋白功能特性的改变。     

芬顿氧化体系处理对白斑狗鱼肌原纤维蛋白结构和功能特性的影响

研究芬顿氧化体系诱导的不同氧化水平(0、1、5、10、20?mmol/L?H2O2)对白斑狗鱼肌原纤维蛋白结构和功能特性的影响.随着氧化水平的升高,肌原纤维蛋白的羰基和浊度增加、溶解度显著降低(P<0.05).十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析结果显示氧化后的肌原纤维蛋白中产生更多交联和蛋白质聚合.傅里叶变换红外光...     

魔芋粉对鲤鱼肌原纤维蛋白凝胶特性的影响

从鲤鱼背部肌肉中提取肌原纤维蛋白,分别添加0.05、0.10、0.15、0.20g/100mL的魔芋粉,研究其在不同加热温度(70、80、90℃)和不同NaCl浓度(0.05、0.10、0.15、0.20mol/L)条件下对肌原纤维蛋白凝胶的硬度、弹性、白度和保水性的影响。结果表明：相同魔芋粉添加量条件下,加热温度80℃时形成的肌原纤维蛋白凝胶的硬度和弹性显著高于70℃和90℃(P＜0.05);90℃时凝胶白度高于70℃和80℃;90℃时保水性显著高于70℃时的保水性(P＜0.05),与80℃的凝胶保水性差异不显著(P＞0.05)。在此条件下,随着NaCl浓度增加,凝胶的硬度和弹性增大;肌原纤维蛋白凝胶的保水性显著提高。同一温度条件下,添加0.10g/100mL魔芋粉的蛋白凝胶硬度达到最大值,且80℃时硬度最大为129g,凝胶的白度随着魔芋粉质量浓度增加呈现下降趋势,保水性随着魔芋粉质量浓度的增加而增大;添加NaCl可以显著提高凝胶的白度。     

Denaturation Kinetics of Myofibrillar Proteins in Bovine Muscle

Differential scanning calorimetry was used to monitor the thermal denaturation kinetics of myofibrillar proteins in bovine muscle at pH 5.6. The activation energy, pre-exponential factor, rate constant and mean life time for each transition were calculated by means of a dynamic method. The kinetic values and the proposed reaction order (n= 1) were confirmed applying an isothermal method as a test. The position of the endothermal peaks proved to be pH dependent. Evidences suggest that peak III is a result of actin denaturation and possibly other thin filament proteins. Peaks I and II would represent the thermal transition of thick filaments. The number of bonds involved in each transition were estimated.     

糖基化反应改进肌原纤维蛋白质功能特性的研究进展

肌原纤维蛋白是肌肉中具有重要功能性质的一类蛋白质,肌原纤维蛋白的功能性质对食品的保水性、质构特性及感官品质具有重要的影响。糖基化反应是蛋白质改性的一种有效方法,具有一定的应用前景。文章综述肌原纤维蛋白与还原糖进行糖基化反应的机理与方法,糖基化反应对肌原纤维蛋白的溶解性、乳化性、热稳定性等特性的改善效果,并提出了今后的研究方向。