加热温度对猪肉肌原纤维蛋白凝胶特性的影响

本实验研究在不同温度(50～90℃)条件下加热对猪肉肌原纤维蛋白凝胶特性的影响。结果显示：温度为70、80℃制备的凝胶保水性较好;50℃和60℃形成的凝胶颜色较深;70～90℃形成凝胶的白度基本相同,无显著差异(P＞0.05);凝胶硬度和咀嚼性随温度的升高先升高后降低,在温度为70～80℃时达最大值;浊度随着温度的升高而总体呈升高趋势,但达到70℃以上时,升高趋势变缓。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)研究发现,在45～65kD之间,在温度升高到70℃以上时,逐渐出现了明显的条带,表明部分蛋白发生了分解。表明肌原纤维蛋白在70～80℃所制得凝胶产品的功能特性较好。     

不同质量比鸡胸肉、鸡腿肉混合肌原纤维蛋白的热诱导凝胶特性

以鸡胸肉和鸡腿肉为材料,研究鸡胸、鸡腿肉混合肌原纤维蛋白不同质量比(9:1、3:1、1:1、1:3、1:9)热变性温度、质构特性、流变特性和保水性的差异。结果表明：鸡胸肉肌原纤维蛋白的凝胶特性显著优于鸡腿肉,鸡胸肉与鸡腿肉的混合可以显著提升鸡腿肉蛋白的硬度、保水性;混合蛋白中,m鸡胸肉蛋白:m鸡腿肉蛋白为9:1的蛋白硬度、保水性最大,分别达到167.64g和83.6%,其凝胶特性和纯鸡胸肉差异不大;m鸡胸肉蛋白:m鸡腿肉蛋白为1:9的混合蛋白硬度、保水性和贮能模量终值均为最小,分别为110.82g、48.75%和297Pa,其凝胶特性优于纯鸡腿肉肌原纤维蛋白。     

肌原纤维蛋白与脂肪替代品混合样品流变特性研究

以鸡胸肉为原料提取肌原纤维蛋白(MP),采用流变仪,研究MP与脂肪替代品(FS)的质量浓度比、pH值以及离子强度等因素对MP-FS混合样品流变特性的影响.在单因素试验的基础上,以储能模量G '为响应值,采用响应面Box-Behnken试验研究MP与FS质量浓度比、pH值以及离子强度对G '的影响.结果表明:各因素影响混合样品凝胶G’的顺序为:pH＞MP与FS质量浓度比＞离子强度,MP与FS质量浓度比20∶10、pH6.0、离子强度0.6时,G’取得最佳值153Pa.     

Xanthan Enhances Water Binding and Gel Formation of Transglutaminase-Treated Porcine Myofibrillar Proteins

ABSTRACT: In this study, the effect of xanthan on dynamic rheological properties, textural profile, and water binding of transglutaminase (TG)-treated myofibrillar protein (MP) gels was investigated. In experiment 1, MP suspensions (40 mg/mL protein, 0.6 M NaCl) at pH 6.45 with or without 0.05% xanthan were treated with 0%, 0.1%, 0.2%, 0.3%, 0.4%, and 0.5% TG; in experiment 2, MP suspensions (40 mg/mL protein, 0.6 M NaCl) at pHs 6.13, 6.30, 6.45, 6.69 with or without 0.05% xanthan were treated with 0.3% TG. Treated samples were analyzed with differential scanning calorimetry for thermal stability and oscillatory rheometry and Instron penetration tests for gelation properties. The TG treatments lowered the transition temperature (T_m) of MP by as much as 6 °C (P < 0.05) but increased apparent enthalpy of denaturation. However, there was no detectable thermal stability difference between MP samples with or without xanthan. The shear storage modulus (G′) of MP gels increased markedly upon treatments with ≥0.3% TG, and the presence of xanthan further enhanced the gel strength (P < 0.05). The addition of 0.05% xanthan decreased cooking loss of TG-treated MP gels by 17% to 23% when compared with gels without xanthan at all pH levels evaluated (6.13 to 6.67). Thus, the combination of TG and xanthan offered a feasible means to promote cross-linking and gelation of MP while reducing cooking losses.     

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.     

冰温和冷鲜贮藏对鸡肉肌原纤维蛋白凝胶性能和水分状态的影响

以鸡胸肉为原料,研究4℃冷鲜和-0.7℃冰温贮藏期间鸡肉肌原纤维蛋白凝胶强度、保水性和水分分布状态变化。采用动态流变仪测定其凝胶强度,用离心法测定凝胶的保水性,用低场核磁共振分析凝胶的水分状态变化情况。结果表明:随着贮藏时间的延长,冷鲜和冰温组鸡胸肉肌原纤维蛋白凝胶强度和保水性均呈下降趋势,冰温组蛋白凝胶强度和保水性显著高于冷鲜组(P0.05);低场核磁共振分析表明持水性的下降与不易流动水比例降低和自由水比例提高有关;冰温组蛋白凝胶不易流动水下降和自由水的上升幅度显著低于冷鲜组(P0.05)。冰温贮藏可以更好地保持肌原纤维蛋白的热诱导凝胶性能,从而保证鸡肉的加工品质。     

不同超声功率处理对鲢鱼肌原纤维蛋白理化特性及凝胶品质的影响

以鲢鱼为原料,研究不同功率下超声处理对鲢鱼肌原纤维蛋白及其凝胶性质的影响。结果表明：随着超声功率的增加,肌原纤维蛋白起泡性、泡沫稳定性、乳化性和乳化稳定性均呈现先增加后降低的趋势,超声功率300 W时均达到最大值;肌原纤维蛋白热凝胶的白度和持水性也随着超声功率的增大先增加后减小,在超声功率300 W时达到最大值,较未处理样品分别提高44%和27%;肌原纤维蛋白凝胶的蒸煮损失率呈现出随着超声功率的增加一直降低的趋势,在超声功率为400 W时达到最小值,较未处理样品降低13%。上述结果表明,不同功率超声波处理对鲢鱼肌原纤维蛋白及其凝胶的改性具有一定的改善作用。     

多酚对猪肉肌原纤维蛋白氧化和凝胶特性的影响

采用羟自由基氧化体系研究添加不同质量分数多酚化合物--鞣酸（tannic acid,TA）、没食子酸（gallicacid,GA）对猪肉肌原纤维蛋白氧化和凝胶特性的影响。结果表明：与对照组相比,添加0.05% TA和0.25% GA可显著抑制肌原纤维蛋白中羰基和二聚酪氨酸含量的增加（P＜0.05）,提高肌原纤维蛋白的最大热变性温度和凝胶保水性（P＜0.05）。扫描电子显微镜观察表明,不同酚类化合物对肌原纤维蛋白凝胶微观结构影响有显著差异,添加0.05%氧化TA后形成的肌原纤维蛋白凝胶结构更加致密。结论：多酚的添加抑制了肌原纤维蛋白氧化,改善了肌原纤维蛋白的热稳定性、凝胶保水性和凝胶强度。     

Interaction and Functionality of Mixed Myofibrillar and Enzyme-hydrolyzed Soy Proteins

ABSTRACT Native and briefly heated (85 °C for 3 min) soy protein isolates (SPI) were partially hydrolyzed (4% DH) by Alcalase® and Flavourzyme™ before incorporation into a pork myofibril isolate (MPI) system. The hydrolysis of soy protein enhanced its interaction with MPI, leading to a decreased thermal stability of both soy and muscle proteins. Alcalase SPI hydrolysates, when compared with nonhydrolyzed SPI, improved viscoelastic properties and hardness of MPI gels, while Flavourzyme SPI hydrolysates had an adverse effect. Hydrolyzed SPI augmented emulsifying properties of MPI; the specific efficacy depended upon the type of enzymes used, the SPI:MPI ratio, and whether SPI was heated before hydrolysis.     

Linear Heating Rate Affects Gelation of Alaska Pollock and Pacific Whiting Surimi

Shear stress of Alaska pollock surimi gels with and without beef plasma protein (BPP) increased as heating rate decreased, but shear strain was unaffected. An increase in shear stress was accompanied by an increase of cross-linked myosin heavy chain. Slow heating rates increased proteolysis in Pacific whiting surimi as shown by degradation of myosin heavy chain and low shear stress and shear strain. Proteolysis of whiting surimi was lessened by BPP to a greater extent at rapid heating rates (20 and 30°C/min) than at slow heating rates (1 and 5°C/min).     

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。     

Physicochemical Changes in Alaska Pollock Surimi and Surimi Gel as Affected by Electron Beam

ABSTRACT: Alaska pollock surimi and surimi gels (cooked) were subjected to various doses of electron beam (e-beam). Shear stress of surimi gels increased as the dose increased up to 6 to 8 kGy and then decreased. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed gradual degradation of myosin heavy chain as the dose increased. The degradation was slower for frozen samples. The integrity of actin was slightly affected by high doses (25 kGy). The amount of sulfhydryl groups and the level of surface hydrophobicity of Alaska pollock surimi decreased as the dose increased, suggesting formation of disulfide bonds and hydrophobic interactions. The sulfhydryl groups and hydrophobicity of surimi gels increased as the dose increased up to 6 kGy and then decreased.     

Hydroxyl Radical and Ferryl-Generating Systems Promote Gel Network Formation of Myofibrillar Protein

ABSTRACT: The objective of the study was to examine how oxidatively induced protein cross-linking would influence the gelation properties of myofibrillar protein (MP) under meat processing conditions. MP suspensions in 0.6 M NaCl at pH 6 were treated with an iron-catalyzed oxidizing system (IOS: 10 μM FeCl₃, 0.1 mM ascorbic acid, 0.05 to 5 mM H₂O₂) or a H₂O₂-activated metmyoglobin oxidizing system (MOS: 0.01 to 0.1 mM metmyoglobin/H₂O₂) that produced hydroxyl radical and ferryl species, respectively. Both oxidizing systems promoted MP thermal gelation, which was evidenced by rapid protein–protein interaction and the enhancement in storage modulus (elasticity) of the gel network as revealed by dynamic rheological testing in the 20 to 74 °C temperature range. This gelation-enhancing effect was attributed to the shift of myosin aggregation in the early stage of heating from predominantly head–head association (nonoxidized control samples) to prevalently tail–tail cross-linking through disulfide bonds. However, both hardness and water-holding capacity of chilled gels tended to decline when MP was exposed to ≥1 mM H₂O₂ in IOS and to all concentrations of metmyoglobin in MOS. Microscopic examination confirmed a more porous structure in oxidized gels when compared with nonoxidized protein gels. The results demonstrated that mild oxidation altered the mode of myosin aggregation in favor of an elastic gel network formation, but it did not improve or had a negative effect on water-binding properties of MP gels. Practical Application: Mild oxidation promotes protein network formation and enhances gelation of myofibrillar protein under normal salt and pH conditions used in meat processing. This oxidative effect, which involves disulfide linkages, is somewhat similar to that in bakery product processing where oxidants are used to improve dough performance through gluten protein interaction.     

不同干燥方式燕麦蛋白的性质及对肌原纤维蛋白凝胶特性的影响

为研究添加不同干燥方式处理的燕麦蛋白对肉类食品质构等特性的影响,采用4种不同干燥方法(喷雾干燥、冷冻干燥、真空干燥和微波干燥)处理燕麦蛋白,考察不同干燥方法对燕麦蛋白结构和性质的影响,以及添加不同干燥方法处理的燕麦蛋白对肌原纤维蛋白凝胶特性的影响。结果表明:不同干燥方法对燕麦蛋白的结构及性质影响不同,与喷雾干燥处理的燕麦蛋白相比较,冷冻和微波干燥处理的燕麦蛋白游离氨基和羰基含量显著下降;红外光谱分析结果显示,相比较于冷冻、真空和微波干燥,喷雾干燥处理的燕麦蛋白α-螺旋和β-转角结构含量无显著性差异,但β-折叠结构含量下降而无规则卷曲结构含量上升;荧光光谱分析结果表明,相比较于冷冻和微波干燥,喷雾和真空干燥处理的燕麦蛋白的最大发射波长出现了红移;微波干燥处理的燕麦蛋白表面疏水性最低且溶解性最好。不同干燥方法处理的燕麦蛋白对肌原纤维蛋白的凝胶性质影响不同,与肌原纤维蛋白相比,添加冷冻、真空和微波干燥处理的燕麦蛋白未改变凝胶温度,而添加喷雾干燥处理的燕麦蛋白凝胶温度降低了2℃; 添加微波、真空和喷雾干燥处理的燕麦蛋白均提高了凝胶的G′ 和G″,表明混合凝胶的弹性和黏性提高,而添加冷冻干燥处理的燕麦蛋白降低了凝胶的黏性和弹性; 扫描电子显微镜结果显示,喷雾干燥处理的燕麦蛋白与肌原纤维蛋白形成的混合凝胶网络具有更为紧密的网状结构,且孔径相对较小,而冷冻干燥处理的燕麦蛋白与肌原纤维蛋白形成的混合凝胶网络较为疏松,孔径相对较大。本研究旨在为功能型肉制品,包括谷物-肉类乳化型肉制品的开发提供一定的技术参数。     

肌原纤维蛋白凝胶形成机理及影响因素的研究进展

肌原纤维蛋白的凝胶特性是肉类制品重要的功能特性,是形成肉制品独特的质构、保水性、乳化性以及感官的决定性因素。本文介绍了蛋白质凝胶形成的机理,重点论述了肌原纤维蛋白形成良好凝胶的影响因素,为生产高质量的肉制品提供理论依据。     

大豆分离蛋白对肌原纤维蛋白加热过程中结构及流变特性的影响

大豆分离蛋白（soybean protein isolate,SPI）作为优质的植物蛋白常被用于肉制品加工中,以提高产品产量和质地。研究添加SPI对肌原纤维蛋白（myofibrillar protein,MP）凝胶特性及MP加热过程中结构和流变特性的影响。结果表明：添加10%、20% SPI能提升混合凝胶的凝胶强度及保水性（P＜0.05）;加热过程中混合蛋白凝胶二级结构发生改变,但其变化规律尚不明确;添加SPI使混合凝胶储能模量及损耗模量下降;混合凝胶上清液十二烷基硫酸钠-聚丙烯酰胺凝胶电泳图谱显示,肌球蛋白重链、肌动蛋白、SPI部分亚基均是参与凝胶形成的蛋白质。     

预热处理大豆蛋白对鲤鱼肌原纤维蛋白凝胶和流变学特性的影响

以鲤鱼肌原纤维蛋白（myofibrillar protein isolate,MPI）为研究对象,研究经过预热处理的大豆分离蛋白（soy protein isolate,SPI）对MPI凝胶和流变学特性的影响。SPI在90 ℃热处理0（天然SPI）、30 min和180 min,分别与MPI以不同的比例（0∶1、1∶1、1∶2、1∶3、1∶4）混合,所有溶液总蛋白质量浓度均为40 mg/mL。结果表明,经过预热处理的SPI与MPI混合后其凝胶硬度、弹性、白度和持水性显著高于天然SPI与MPI混合所形成的蛋白凝胶（P＜0.05）,且预热处理时间越长的大豆蛋白（180 min）与短时间处理（30 min）相比增加得更为明显（P＜0.05）。此外,随着SPI-MPI复配1∶1～1∶4,混合蛋白凝胶硬度、弹性、白度和持水性显著增大（P＜0.05）。流变学研究表明,SPI添加到MPI溶液中能增加蛋白变性温度,而经过预热处理SPI能够显著地提高储能模量（G’）。热稳定性结果表明,MPI中添加天然SPI能够显著降低Tmax3（P＜0.05）而对Tmax1和Tmax2无影响（P＞0.05）;当SPI经过热处理后添加到MPI中能够显著降低Tmax1（P＜0.05）而提高Tmax3（P＜0.05）。总之,与未经预热处理的SPI相比,经过预热处理后的SPI添加到MPI中能够改善蛋白凝胶特性和流变学特性。