影响猪血浆蛋白热诱导凝胶质构特性及持水性因素的研究

本实验研究在一定的加热条件下猪血浆蛋白质量浓度、加热温度、加热时间、离子种类、离子强度和pH 值对猪血浆蛋白热诱导凝胶的质构、持水性等性质的影响。利用质构仪测定猪血浆蛋白热诱导凝胶的硬度和黏附性,利用离心的方法测定凝胶的持水性。结果表明,在80℃下加热45min,猪血浆蛋白质量浓度超过6g/100mL可以形成凝胶,并且随蛋白质量浓度的增大,凝胶强度和持水性也增大;凝胶强度随pH 值(3～9)增加而增大,pH5 时凝胶的持水性最小,pH3 时最大;NaCl 浓度0.2mol/L,CaCl2 浓度0.6mol/L 时,凝胶硬度最大。实验得出,猪血浆蛋白热诱导凝胶的质构特性及持水性受许多因素影响,在实际生产中应该控制加热条件,以获得高质量的凝胶。     

食用胶对虾蛄中磷酸化肌原纤维蛋白凝胶特性的影响

将魔芋胶、卡拉胶、黄原胶分别添加到虾蛄磷酸化肌原纤维蛋白中,在不同食用胶、三聚磷酸钠添加量及不同温度下形成凝胶,研究食用胶对磷酸化蛋白凝胶特性的影响。结果表明：随着三聚磷酸钠添加量的增加,3 种食用胶形成的蛋白凝胶强度和保水性均提高;随着食用胶添加量的增加,卡拉胶与黄原胶形成的蛋白凝胶强度和保水性提高,魔芋胶添加量为0.1%时,其蛋白凝胶强度最高;随着温度的升高,魔芋胶与卡拉胶均对蛋白凝胶强度和保水性有显著性影响（P＜0.05）,但黄原胶对凝胶强度和保水性无显著影响（P＞0.05）。     

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。     

Rheological and Microstructural Properties of Porcine Myofibrillar Protein–Lipid Emulsion Composite Gels

ABSTRACT:  The objective of the study was to investigate the role of emulsified fat (lard) and oil (peanut oil) in the rheology and microstructure of porcine myofibrillar protein (MP) gels. Heat-induced composite gels were prepared from 2% MP with 0% to 15% pre-emulsified lipids at 0.6 M NaCl, pH 6.2. Dynamic rheological testing upon temperature sweeping (20 to 80 °C at 2 °C/min) showed substantial increases in G ' (an elastic modulus) of MP sols/gels with the addition of emulsions. Gel hardness was markedly enhanced ( P < 0.05) by incorporating ≥10% emulsions, and the composite gel with 15% lard was 33% more rigid ( P < 0.05) than that with 15% peanut oil. Incorporation of both emulsions at 10% or higher levels improved the water holding capacity of the gels by 28% to 44% ( P < 0.05). Light microscopy revealed a compact gel structure filled with protein-coated fat/oil globules that interacted with the protein matrix via disulfide bonds. The results indicated that both physical and chemical forces contributed to the enhancements in the rheology, moisture retention, and lipid stabilization in the MP–emulsion composite gels.     

Heat-induced Gels of Rice Globulin: Comparison of Gel Properties with Soybean and Sesame Globulins

The hardness and water-holding ability of rice globulin gels were intermediate between those of gels of soybean and sesame globulins. Scanning electron micrographs showed that rice globulin gel had a rough network structure composed of small globular particles of protein aggregates. Effects of various reagents on solubilization of proteins from the three gel types were compared. Disulfide bonds and hydrophobic interactions contributed mainly to the stability of rice globulin gels. The contributions of disulfide bonds to both the formation and stability of rice globulin gels were greater than for sesame globulin gels.     

Mechanisms of gelation of sardine proteins: influence of thermal processing and of various additives on the texture and protein solubility of kamaboko gels

Surimi prepared from freshly caught sardines was mixed with NaCl and other additives and used to prepare kamaboko gels. Protein-protein interactions involved in the setting (at 4 or 37°C) and/or the cooking (at 90°C) gelation steps were investigated (i) by assessment of kamaboko texture as a result of the type and concentration of additive added; (ii) by partial solubilization of kamaboko gels in buffers containing mercaptoethanol, sodium dodecyl sulphate (SDS) and/or urea, followed by determination of the soluble protein constituents by polyacrylamide gel electrophoresis. Cooked gels of high elasticity and of varying rigidity and gel strength were obtained in the 73–80% water range. Adequate gel texture required a NaCl content of 1.7–3.5% and a pH range of 6.4–8.4. Low concentrations of reducing agents (mercaptoethanol, dithiothreitol, cysteine) or of divalent cations (Ca²⁺, Mg²⁺) improved the texture of gels obtained by setting at 37°C with and without subsequent cooking at 90°C. On the other hand, the addition of N -ethyl maleimide or of ethylene diamine tetra-acetate led to texture deterioration after cooking. These data demonstrate the involvement of disulphide bonds and of electrostatic interactions in surimi gelation. Gel solubilization experiments indicate that the aggregation of myosin heavy chains through various types of protein-protein interactions may be responsible for the elastic gel network formed during setting at 37°C (30 min) or 4°C (24h). Strengthening of the gel network after cooking appears to be due to additional disulphide and hydrophobic interactions.     

Crayfish protein isolated gels. A study of pH influence

Z-potential measurements of aqueous crayfish protein isolate (CFPI) dispersions were carried out to determinate isoelectric point. Gels were prepared by heating CFPI dispersions at 90 °C for 30 min. Solubility and electrophoresis of CFPI and CFPI gels, extracted using different extraction media, were studied. Gels were characterised by linear viscoelasticity, water-holding capacity and SEM techniques. Results confirm that myofibrillar proteins play an important role, where a matrix is stabilized mainly by disulfide bonds, hydrophobic interactions and hydrogen bonds. Similar pH profiles obtained for CFPI dispersions (solubility and Z-potential measurements) and CFPI gels (solubility, linear viscoelasticity and water holding capacity) were obtained. SEM images provide information consistent with those pH profiles.     

Thermal Gelation of Previously Cooked Minced Meat from Jonah Crab (Cancer borealis)

ABSTRACT:  Crab processing typically involves picking meat from whole cooked product. Remaining meat can be recovered as mince and potentially processed into value-added products. This study focused on gelation of commercially processed crab mince. Objectives of the research were to determine the effects of cryoprotectants, freezing, and various heat treatments on gel formation of washed mince from previously cooked crab. Previously frozen minced meat from thermally processed Jonah crab was washed to remove soluble components. Four different treatments were applied to the washed mince: (1) freezing with cryoprotectants, (2) freezing with no cryoprotectants, (3) no freezing with cryoprotectants, and (4) no freezing with no cryoprotectants. Unwashed mince was used as a control treatment. Sodium chloride (2.5%) was mixed into the mince prior to stuffing into sausage casings and heating at 35 °C/30 min, 90 °C/30 min, or 35 °C/30 min followed by 90 °C/30 min. Gels were tested for proximate composition, color, water-holding capacity, and gel strength. All mince samples formed gels except for the unwashed control. Gels with no cryoprotectants had 10% to 20% greater water holding capacity, lower L* values, and greater gel strength than those with cryoprotectants. Freezing of washed mince resulted in lower water-holding capacity of gels and higher a* values. A 2-stage heating treatment resulted in gels with the greatest gel strength, whereas gels cooked at 35 °C had the greatest distance to fracture. Results indicate that protein gels can be formed using previously cooked crab meat, which may be useful in the development of value-added products.     

Combination of high pressure and heat on the gelation of chicken myofibrillar proteins

The effects of combinations of high pressure and heat on chicken myofibrillar gels were investigated. High pressure was either applied simultaneously with heating (heating under pressure, HUP), before heating (PBH) or no high pressure with heat-only (HT). PBH treatment induced many similar properties in gels as did by HT treatment, except that PBH treatment promoted secondary structure transformation and formed more covalent bonds. HUP treatment resulted in less heat denaturation of the protein, induced fewer hydrophobic interactions and covalent bonds, hindered secondary and tertiary structural transformation, and formed a gel with a more porous microstructure. The gels induced by HUP treatment had softer texture and higher water holding capacity than gels induced by PBH or HT treatments. These findings suggest that high pressure with HUP treatment changes gel properties by resisting the heat-induced denaturation and gelation of myofibrillar proteins, while high pressure with PBH treatment alters gel properties by promoting denaturation of myofibrillar proteins.Industrial relevanceThe main constituents in meat are myofibrillar proteins, which are responsible for the functional properties of processed meat products. The gelation of myofibrillar proteins differs according to the sequence in which pressure/temperature combinations are applied. The pressure-modified protein interactions should be considered when adopting high pressure in meat product processing since the microstructure of the meat gel is affected by pressure, which would further affect water holding capacity and textural properties. HUP treatment showed its advantages in forming a fine microstructure and improving water-holding capacity.     

Salt, Cryoprotectants and Preheating Temperature Effects on Surimi-like Material from Beef or Pork

Gel forming ability, measured by cooked gel hardness, and water-holding capacity of surimi-like pork were enhanced by addition of NaCl at 1.5 or 3% although 4.5% or 6% NaCl did not further increase hardness. Cooked gel strength was unaffected by freezing of beef or pork surimi-like materials for 48 hr. Addition of cryoprotectants (3% or 6% sorbitol, 3% glycerol, or 3% sucrose) before freezing had no effect on gel forming ability. Gel hardness was not increased by preheating prior to cooking. Preheating surimi-like pork at 50°C resulted in formation of weaker gels which corresponded to myosin proteolysis. Myosin heavy chain (mw 200 kD) decreased, and new peptide fragments of mw about 138 kD, 128 kD, 120 kD, 86 kD, 77 kD, and 64 kD appeared. Proteolysis was salt-dependent and occurred at pH 6.8–7.5.     

淀粉对磷酸化的虾蛄肌原纤维蛋白凝胶特性的影响

将马铃薯、木薯和玉米淀粉分别添加到磷酸化的虾蛄肌原纤维蛋白中,探讨在不同淀粉添加量、不同三聚磷酸钠添加量及不同温度下对磷酸化蛋白所形成凝胶特性的影响。结果表明：随着三聚磷酸钠添加量的增加,3 种淀粉形成的复合蛋白凝胶强度和保水性均提高;随着淀粉添加量的增加,马铃薯、木薯淀粉对复合蛋白的凝胶特性有显著影响（P＜0.05）,玉米淀粉对蛋白凝胶特性没有显著影响（P＞0.05）;随着温度的升高,3 种淀粉均能使蛋白的凝胶强度升高,但保水性下降。本研究结果为进一步研究虾蛄中肌原纤维蛋白凝胶特性以及淀粉的利用提供了一定的基础。     

离子强度和温度对乳清蛋白凝胶的影响

本实验主要研究凝胶温度和CaCl2 浓度对乳清蛋白冷凝胶的影响。结果表明：较低的凝胶温度和增加CaCl2浓度能够致使乳清蛋白形成清亮的凝胶;在0、10、20℃凝胶温度条件下,增加CaCl2 浓度使得凝胶硬度有所增加;乳清蛋白凝胶的持水性在凝胶温度为0、10℃,CaCl2 浓度为20、40mmol/L 时受到影响;除了0℃ 和20mmol/LCaCl2 条件下,低温能够使乳清蛋白形成较高的凝胶硬度和持水性。凝胶温度和CaCl2 浓度是影响乳清蛋白冷凝胶的关键因素。     

油茶籽油对鱼糜凝胶特性及凝胶结构的影响

为探讨脂质对鱼糜蛋白凝胶功能特性的影响及其机理,研究不同油茶籽油添加量对鱼糜凝胶特性、水分分布、脂质及蛋白质结构等的影响。结果表明:随着油茶籽油添加量的增加,鱼糜凝胶强度、乳化稳定性和持水性显著增加(P0.05),当油茶籽油添加量增加到8%时各指标基本稳定,此时鱼糜凝胶强度为225.1 g·cm,游离出来的液体质量分数为2.60%。拉曼光谱分析发现,油茶籽油的添加改变了鱼糜凝胶体系中脂质和蛋白质的化学结构,主要表现为C—H谱带峰宽的增加、O—H谱带相对强度的下降,以及鱼糜蛋白中β-折叠、β-转角和无规卷曲结构相对含量的增加和α-螺旋结构相对含量的降低。同时,随着油脂质量分数的增加,水分以更加细小的状态分布在鱼糜凝胶体系之中。以上结果进一步揭示了油茶籽油的添加可增加鱼糜凝胶强度、乳化稳定性和持水性的内在原因。     

羟自由基氧化对鲢鱼肌原纤维蛋白凝胶特性的影响

采用含不同浓度H₂O₂(0.0～10.0 mmol/L)的Fenton体系(H₂O₂-VC-FeCl₃)模拟氧化应激环境对鲢鱼肌原纤维蛋白进行氧化,测定蛋白的巯基含量,以及蛋白凝胶的凝胶强度、白度、持水性、水分分布状态及微观结构,探究氧化度对蛋白凝胶特性的影响。结果表明：随着H₂O₂浓度的增加,蛋白的总巯基含量和白度、持水性呈先升高后降低的趋势。当体系中H₂O₂浓度较低(0.1～0.5 mmol/L)时,蛋白凝胶强度增大,白度得到改善;凝胶的三维结构孔洞的面积较小,且分布较为均匀,凝胶的持水力有所增强。但是当体系中的H₂O₂浓度较高(5.0～10.0 mmol/L)时,蛋白凝胶的白度下降,凝胶结构的有序性降低,孔洞面积变大,分布变得不均匀,凝胶的持水力下降,凝胶品质发生劣变。因此,适度氧化(0.1～0.5 mmol/L H₂O...     

L-组氨酸修饰乳清蛋白结构及其热诱导凝胶特性

采用L-组氨酸（L-His）作为蛋白凝胶功能性的增强剂,将其加入乳清分离蛋白溶液中制备热诱导凝胶,研究L-His对乳清蛋白结构及其凝胶特性的影响。结果表明：在乳清蛋白等电点（pI 5.2）时蛋白形成尺度约1 700 nm、具有极小比表面积且几乎不带电的蛋白聚集体,远离蛋白等电点时则所形成的聚集体大小约为400 nm;L-His抑制蛋白聚集体的形成而减小粒径、显著提高聚集体比表面积,促进蛋白分子结构展开并提高其带电量。在经历热诱导后,乳清蛋白在其等电点时形成持水性差的白色凝胶,而在其他pH值时则形成持水性高的黄色凝胶且越远离等电点,胶体黄度值越大;L-His的加入对凝胶颜色变化无显著影响,但能够显著提高凝胶的持水性（P＜0.05）;有效提高凝胶的质地特性,特别是在pH 7.59和pH 9.74时显著提高乳清蛋白凝胶的弹性及咀嚼性（P＜0.05）。这些质构变化可能主要归结于L-His改变了凝胶内的氢键、二硫键和疏水作用力的重排。总之,L-His修饰乳清蛋白结构而改变其凝胶性能且同时受到pH值的影响。     

Gelation Behavior of Protein Isolates Extracted from 5 Cultivars of Pisum sativum L.

ABSTRACT: Protein isolates were extracted from 5 pea ( Pisum ) cultivars and their gelation behaviors were compared at pH 7.6. Gel formation and development was monitored via constant oscillation dynamic measurements. The standard heating and cooling rate was 1.0°/min, but samples were also heated at 0.5°C (and cooled at 1.0°C/min), and others were heated at 1.0°C/min and cooled slowly at 0.2°C/min. When heating more slowly, no changes in gel formation were detected for any of the cultivars. When cooling slowly, the cultivar Solara, with the highest legumin content, formed a stronger gel than all the other cultivars. It did the same when the thiol-blocking agent N -ethylmaleimide (NEM) was added to the system. This indicated that the strengthened gel system formed independently of any disulfide bonds formed by the legumin. The cultivars Supra and Classic formed stronger gels only when cooled slowly in the presence of NEM, and so disulfide bond formation in their gel systems was apparently a factor that prevented gel network strengthening. The cultivars Finale and Espace were unable to form strong and self-supporting gels. This was believed to be because of the repulsive forces on the α-subunits of vicilin, which were at their highest level in the cultivars Finale and Espace. The contribution of legumin to the pea protein isolate gels was shown to be cultivar specific and related to its disulfide bonding ability rather than the absolute amount of legumin protein present.     

沙蒿胶对虾蛄肌原纤维蛋白凝胶特性的影响

为了提高虾蛄中肌原纤维蛋白凝胶的品质,从虾蛄中提取肌原纤维蛋白,分别添加质量分数0%、0.2%、0.4%、0.6%、0.8%、1.0%的沙蒿胶,研究沙蒿胶在不同Na Cl浓度(0.1、0.2、0.3、0.4、0.5 mol/L)和不同加热温度(60、70、80、90℃)条件下对肌原纤维蛋白凝胶特性的影响。结果表明:相同沙蒿胶添加量条件下,90℃时肌原纤维蛋白凝胶保水性显著高于60℃和70℃(P0.05);80℃时凝胶硬度和弹性最大且显著高于60℃和70℃(P0.05);但对凝胶白度的影响差异并不显著。随着Na Cl浓度的增加,凝胶保水性和硬度呈先上升后下降趋势,在0.3 mol/L时达到最大值;凝胶的弹性和白度呈现上升趋势。在90℃时添加1.0%沙蒿胶的凝胶保水性最佳;在同一温度条件下,随着沙蒿胶添加量增加,凝胶弹性增强,添加0.6%沙蒿胶的凝胶硬度最大,白度呈下降趋势。本研究结果为进一步研究沙蒿胶在虾蛄制品中的应用提供了一定的理论依据。     

加热模式对添加葡萄糖氧化酶鲢鱼糜凝胶特性的影响

研究两段法加热模式对添加葡萄糖氧化酶鲢鱼糜凝胶特性的影响。结果表明,在凝胶化阶段,高温短时（40 ℃、1 h）模式下,鱼糜凝胶强度、持水性、白度和不易流动水含量最高,且自由水含量最低,凝胶网络结构最致密;十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE）图谱显示,在高温短时（40 ℃、1 h）模式下,肌球蛋白重链（myosin heavy china,MHC）条带强度降低,说明此时蛋白降解较多。在熟化阶段时,微波加热鱼糜凝胶的凝胶强度、持水性和白度最高,三氯乙酸-溶解肽含量、自由水含量和孔隙当量直径最小,形成了有序致密的三维网络结构;SDS-PAGE图谱显示,相比水浴加热,微波加热下MHC条带强度更高,说明微波加热促进了二硫键的形成。因此,适宜的加热模式能改善鱼糜凝胶的品质。     

脱乙酰魔芋葡甘聚糖对猪肉肌原纤维蛋白结构及凝胶特性的影响

研究添加不同质量分数（0%、0.125%、0.25%、0.5%和1%）的脱乙酰魔芋葡甘聚糖（deacetylated konjac glucomannan,DKGM）对猪肉肌原纤维蛋白（myofibrillar protein,MP）结构和凝胶性能的影响,通过分析其凝胶强度、保水性、水分分布、微观结构和凝胶分子力的变化,探究DKGM对MP凝胶特性的影响机制。结果表明,MP凝胶强度随着DKGM质量分数的增加而增大,添加量为0.25%时达到峰值,是对照组的1.55倍;DKGM的加入可以减缓水的流动性,从而提高凝胶持水力;冷场扫描电子显微镜观察发现添加DKGM可以促进凝胶形成更为均匀致密的网络结构;结构和作用力分析表明适量添加DKGM可以促进MP分子的展开和疏水基团的暴露,增加活性巯基的含量,诱导更多α-螺旋向β-折叠转变,增强MP凝胶的疏水相互作用和二硫键,从而改善MP凝胶强度和持水力。     

马铃薯蛋白与蛋清蛋白混合凝胶特性分析

以马铃薯蛋白（potato protein,PP）和蛋清蛋白（egg white protein,EWP）为原料制备热诱导混合凝胶,分析不同比例PP-EWP混合凝胶的质构、蛋白质二级结构、分子间作用力、游离巯基及流变性质的变化规律。结果表明,随着PP含量的增加,混合凝胶的保水性由（73.5±0.71）%升高至（97.5±0.71）%（P＜0.05）,粗糙程度逐渐减弱;随着EWP含量的增加,混合凝胶的硬度由（460.5±4.4） g升高至（1 614.9±126.4） g（P＜0.05）,2 种蛋白在保水性和硬度方面形成互补;当PP-EWP混合比例趋于1时,凝胶的二级结构由β-折叠和α-螺旋向无规卷曲转变,氢键作用力逐渐减弱;疏水相互作用和游离巯基含量随EWP含量的增加而增加;混合凝胶储能模量在PP-EWP比例为1∶0、9∶1和0∶1时较高。混合蛋白凝胶强度与疏水相互作用和游离巯基含量呈极显著正相关（P＜0.01）,与保水性呈极显著负相关（P＜0.01）,与储能模量无显著相关性（P＞0.05）。