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。     

响应面法优化微波加热制备肌原纤维蛋白凝胶工艺

以鸡胸肉为原料,利用响应面分析法优化微波加热改善肌原纤维蛋白（myofibrillar protein,MP）凝胶特性和结构的工艺条件。在单因素试验基础上,以微波加热功率、微波时间和MP溶液pH值为影响因子,以MP凝胶硬度、弹性和保水性为响应值建立数学模型,进行响应面优化试验,研究各变量及其交互作用对MP凝胶品质的影响。结果表明,微波加热制备MP凝胶的最佳条件为微波功率400 W、微波时间15 s、MP溶液pH值6.0,该条件下MP凝胶的硬度为45.48 g,弹性为0.82,保水性为88.86%。优化结果表明,低功率、长时间的微波加热能够使MP凝胶获得更好的质构特性和较高的保水性。     

热处理温度及时间对镜鲤鱼肌原纤维蛋白热聚集行为的影响

通过测定蛋白溶解度、浊度、表面疏水性、巯基含量、破碎力等指标并结合傅里叶变换红外光谱分析,探究热处理温度（30～90 ℃）和保温时间（0～60 min）对镜鲤鱼肌原纤维蛋白热聚集行为的影响。结果表明,镜鲤鱼肌原纤维蛋白热诱导聚集具有高度的温度依赖性。30 ℃处理条件下,蛋白变性程度较小,活性巯基含量增加,总巯基含量不变,二硫键未形成,此时蛋白聚集主要依靠表面疏水相互作用。随着温度的升高,蛋白具有高的表面疏水性、β-折叠结构含量、浊度、破碎力和低的巯基含量、α-螺旋结构含量、溶解度。这表明热处理温度的升高导致蛋白具有较高的热诱导聚集性。在0～15 min保温处理过程中,蛋白各指标水平变化显著（P＜0.05）,并在30 min后基本保持稳定。另外,在70 ℃、30 min时蛋白热诱导凝胶强度最大（1.07 N）。综上,热处理条件对蛋白热聚集行为具有显著影响,控制热处理条件可以调节蛋白热聚集行为。     

从质构学角度研究肌原纤维蛋白凝胶形成的作用力

通过研究有关试剂对肌原纤维蛋白(MP)凝胶质构特性的影响,探讨了维持凝胶形成的作用力。结果表明:改变pH和离子强度影响了静电相互作用,从而改变了肌源纤维蛋白(MP)凝胶的质构特性;添加二硫苏糖醇(DTT)、N-乙基顺丁烯二酰亚胺(NEM)、溴酸钾能影响二硫键的形成,但MP凝胶质构特性变化不明显,说明二硫键对MP凝胶形成的影响不大;添加微量的十二烷基硫酸钠(SDS)可明显影响凝胶的硬度和弹性,说明疏水相互作用在MP凝胶形成中具有显著作用;添加尿素和盐酸胍能明显降低MP凝胶的硬度和弹性,说明氢键对MP凝胶的形成也具有重要的影响。     

预热变性程度对大豆蛋白凝胶性质的影响

以非还原SDS-PAGE表征大豆蛋白的预热变性程度,并采用质构分析、流变分析研究预热变性程度对大豆蛋白凝胶性质的影响。SDS-PAGE结果表明,随着加热温度的升高蛋白质变性速率逐渐增大,相同加热时间条件下,蛋白质变性程度随加热温度升高呈S型曲线上升。质构、流变分析结果表明:随着预热变性程度的增大,大豆蛋白凝胶硬度先增大后减小,变性程度为86.11%时凝胶硬度最大,是未经预热变性的大豆蛋白凝胶硬度的2.15倍;凝胶弹性则随预热变性程度的增大持续增大;变性程度在22.28%以上时大豆蛋白形成凝胶更快,但完全变性大豆蛋白在形成凝胶时的降温阶段不能形成很好的凝胶结构。粒径分析结果表明,预热变性程度对大豆蛋白凝胶性质的影响与蛋白质预热变性时形成的聚集体尺寸及形态有关。     

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.     

Effects of β‐glucans on properties of soya bean protein isolate thermal gels

The effects of concentration and molecular weight of oat β‐glucans on properties of soya bean protein isolate (SPI) thermal gels prepared by heating at 90℃for 30 min were investigated. Compared with control (free of β‐glucan) formulations, the presence of β‐glucans (0.5–1.5%, w/v) largely enhanced storage modulus (G′) and texture properties of SPI (12%, w/v) thermal gels measured by dynamic oscillatory rheometry and texture profile analysis, which were developed as increasing β‐glucan concentration and molecular weight. It is possible that β‐glucans could cause the formation of protein aggregates to produce gels through hydrophobic interactions. Mixed gel systems at low ionic strength showed higher G′ resulting from the lower denaturation temperature of SPI, which was beneficial to the formation of gel structure. In addition, although adding a certain amount of β‐glucan into SPI reduced water‐holding capacity of mixed gels, high molecular weight of β‐glucan improved their water‐holding capacity compared to control formulations attributed to the improvement of the structural integrity of the mixed gel network.     

Structural Characterization of Amaranth Protein Gels

ABSTRACT: Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix.     

Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

Fish sarcoplasmic protein (SP) could be exploited in the water‐holding agent for fish protein gels, except that the gel strength is reduced. The adjustment of pH could modify protein interactions to overcome the inferior effect. Fish SP solutions were adjusted to pH 3 or 12, neutralised to pH 7 and lyophilised to be pH‐treated SPs. These SPs along with lyophilised untreated SP (Normal SP) were incorporated into fish myofibrillar protein (MP) with microbial transglutaminase (MTG). The denaturation temperature (T_d) of MP mixed with normal SP was 66 °C with the lowest shear stress value. The denaturation of MP mixed with pH‐treated SP reduced to be 57 °C, resulting in increased shear stress. The cooking loss of MP gel was reduced by adding pH‐treated SPs, while the breaking forces were similar to control. The result indicated that pH‐treated SPs could be used to reduce cooking loss of MTG‐mediated MP gels without affecting the gelling properties.     

Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels

The molecular forces involved in the gelation of heat-induced pea protein gel were studied by monitoring changes in gelation properties in the presence of different chemicals. At 0.3 M concentration, sodium thiocyanate (NaSCN) and sodium chloride (NaCl) showed more chaotropic characteristic and enhanced the gel stiffness, whereas sodium sulfate (Na₂SO₄) and sodium acetate (CH₃COONa) stabilized protein structure as noted by increasing denaturation temperatures (T_d) resulting in reduced storage moduli (G′). To determine the involvement of non-covalent bonds in pea protein gelation, guanidine hydrochloride (GuHCl), propylene glycol (PG), and urea were employed. The significant decrease in G′ of pea protein gels with the addition of 3 M GuHCl and 5 M urea indicated that hydrophobic interactions and hydrogen bonds are probably involved in pea protein gel formation. The increase in G′ with increasing PG concentration (5–20%), demonstrated hydrogen bonds and electrostatic interaction involvement. No significant influence was observed on G′ with addition of different concentrations of β-mercaptoethanol (2-ME), low levels of dithiothreitol (DTT), and up to 25 mM N-ethylmaleimide (NEM), which indicated that disulfide bonds are not required for gel formation, but data at higher DTT and NEM concentrations and slow cooling rates showed a minor contribution by disulfide bonds. Reheating and recooling demonstrated that gel strengthening during the cooling phase was thermally reversible but not all the hydrogen bonds disrupted in the reheating stage were recovered when recooled.     

加热时间和葡萄糖酸内酯对猪肌原纤维蛋白凝胶性的影响

研究不同加热时间和不同质量分数的葡萄糖酸内酯(GDL)添加量对猪肉肌原纤维蛋白凝胶特性的影响.结果表明:GDL质量分数1.5％～2.0％,加热时间30min时凝胶的保水性、硬度、黏聚性和回弹性最好(P＜0.05);同时,加热30min后凝胶的白度值降到了最低值;加热时间对凝胶弹性的影响不显著(P＞0.05),但随着GDL质量分数的增加,凝胶弹性逐渐增加,当GDL质量分数为1.5％时凝胶弹性最好并趋于平稳.     

β-Lactoglobulin Gelation and Modification: Effect of Selected Acidulants and Heating Conditions

ABSTRACT: The effect of acidulant selection, heating temperature, and heating rate on the properties of low-pH β-lactoglobulin (β-Lg) gels and powders derived from these gels was investigated by rheological and microscopic techniques. As isothermal gelation temperature was increased from 75 to 85 °C, gels made with hydrochloric and lactic acid showed more rapid gel formation and increased stress at gel fracture. Thickening and water-holding properties of powders derived from these gels also increased with temperature. Increases in gel strength and derivatized powder functionality appeared to plateau above 85 °C. Gels and derivatized powders prepared with phosphoric acid exhibited attributes similar to samples prepared with HCl and lactic acid at lower temperatures. The ion-specific ability of phosphate to increase denaturation temperature was responsible for the shift in properties of gels made with phosphoric acid. Microscopy revealed temperature effects on network building block size, but variations in rheological properties could not be linked to changes in gel micrographs. Alteration of heating rates from 2.0 to 0.2 °C/min during gelation affected the observed gelation temperature, but had little effect on final gel mechanical properties. Acid selection and gelation temperature offer alternatives to control β-Lg gel strength and the functional properties of instant thickening protein ingredients.     

基于MP-KG凝胶体系研究微观结构影响质构特性的调控机制

以肌原纤维蛋白-魔芋胶（myofibrillar protein-konjac glucomannan,MP-KG）为模拟体系,利用质构仪、石蜡切片和扫描电镜分别测定复合凝胶质构特性、空间分布和蛋白三维凝胶网络结构,进而阐释复合凝胶微观结构对质构特性的调控机制,为KG在低脂肉制品中的应用提供一定的理论基础。质构特性结果显示：随着KG添加量增高,复合凝胶断裂形变时应力变化呈现抛物线形,说明KG对复合凝胶应力的改善具有添加量极限。复合凝胶断裂形变时应变的变化趋势和应力相似,但是两者的添加量极限不同。低场核磁结果显示：在添加1% KG时不易流动水的弛豫时间最低且其相对百分比最高,分别为274 ms和92.79%,说明KG能够促进蛋白之间的交联,进而提高蛋白基质对水分子的束缚。石蜡切片显示随着KG添加量的提高,MP-KG凝胶体系的空间分布从填充结构转变成互穿结构。扫描电镜显示：对照组的MP凝胶网络结构中布满了相互交错的水沟壑,这些沟壑的存在导致MP凝胶网络结构比较疏松。添加少量KG能够减少蛋白三维网络结构中相互交错的水沟壑,MP凝胶网络结构更加致密均一。添加过量的KG会形成KG连续相,反而破坏蛋白网络结构的整体性。因此,KG以水相稳定为主要作用时,其能够改善复合凝胶的质构;当KG以互穿结构形式存在时,其反而会劣化复合凝胶的质构。     

Physicochemical and structural changes of myofibrillar proteins in muscle foods during thawing: Occurrence,consequences, evidence,and implications

Myofibrillar protein (MP) endows muscle foods with texture and important functional properties, such as water-holding capacity (WHC) and emulsifying and gel-forming abilities. However, thawing deteriorates the physicochemical and structural properties of MPs, significantly affecting the WHC, texture, flavor, and nutritional value of muscle foods. Thawing-induced physicochemical and structural changes in MPs need further investigation and consideration in the scientific development of muscle foods. In this study, we reviewed the literature for the thawing effects on the physicochemical and structural characters of MPs to identify potential associations between MPs and the quality of muscle-based foods. Physicochemical and structural changes of MPs in muscle foods occur because of physical changes during thawing and microenvironmental changes, including heat transfer and phase transformation, moisture activation and migration, microbial activation, and alterations in pH and ionic strength. These changes are not only essential inducements for changes in spatial conformation, surface hydrophobicity, solubility, Ca²⁺-ATPase activity, intermolecular interaction, gel properties, and emulsifying properties of MPs but also factors causing MP oxidation, characterized by thiols, carbonyl compounds, free amino groups, dityrosine content, cross-linking, and MP aggregates. Additionally, the WHC, texture, flavor, and nutritional value of muscle foods are closely related to MPs. This review encourages additional work to explore the potential of tempering techniques, as well as the synergistic effects of traditional and innovative thawing technologies, in reducing the oxidation and denaturation of MPs and maintaining the quality of muscle foods.     

不同NaCl浓度条件下亚麻籽胶对肌原纤维蛋白凝胶作用力及乳化特性的影响

为改善低盐肉制品凝胶乳化品质的降低,明确亚麻籽胶（flaxseed gum,FG）添加对肉制品品质的影响,以肌原纤维蛋白（myofibrillar protein,MP）为研究对象,通过测定乳析指数、电位值、粒径、显微观察研究不同NaCl浓度条件下FG对MP乳液乳化稳定性的影响,而化学键的测定显示FG对MP凝胶化学作用力的影响。结果表明,形成MP凝胶及FG-MP凝胶体系的关键是二硫键和非二硫共价键的贡献;不同NaCl浓度对FG-MP乳液的乳析指数、ζ-电位、粒径的影响均不显著（P＞0.05）,而MP乳液随着NaCl浓度的提高,乳化稳定性、ζ-电位、粒径均显著变化（P＜0.05）。特别是在低浓度NaCl条件下,FG的加入可以显著提高MP乳液的稳定性（P＜0.05）。显微观察发现加入FG可以改善MP乳液液滴聚集的现象。因此,说明在低浓度NaCl条件下加入FG可以显著提高肌原纤维蛋白乳液的乳化稳定性,提高其抗盐能力,促进亚麻籽在肉制品中的应用。     

The relationship between breaking force and hydrophobic interactions or disulfide bonds involved in heat-induced soy protein gels as affected by heating time and temperature

Hydrophobic interactions and disulfide bonds involved in heat-induced soy protein gels were characterised by determining the dissolution kinetics of gels. Reducing SDS-PAGE results revealed that all proteins in gel network could be dissolved simultaneously by 1% (w/v) SDS solution, while a majority of glycinin (11S) A polypeptide and a moderate amount of 11S-B polypeptides, 7S-α′, α, γ, and β subunits were found in 2% (w/v) DTT dissolving samples. Stronger interaction force between proteins in gel network would result in lower dissolution constant rate. The breaking force of soy gels increased from 543 to 2171 g_force with increasing heating temperature from 85 to 100 °C, and denaturation of 11S globulins played an important role in the development of gel network. As increasing heating time from 30 to 120 min, the breaking force of gels increased from 1687 to 2175 g_force, then decreased to 1253 g_force when the time was prolonged to 240 min. Negative correlations were observed between breaking force and dissolution constant rate k_SDS or Δk, which suggested that the strengthening of both hydrophobic interactions and disulfide bonds.     

MECHANICAL AND WATER-HOLDING PROPERTIES OF HEAT-INDUCED SOY PROTEIN GELS AS RELATED TO THEIR STRUCTURAL ASPECTS

The dependence of mechanical and water-holding properties of soy protein gels upon their structures was examined. Gels varying in extent of network formation were prepared by heating 20% paste of the isolated soy protein (ISP) containing L-cysteine hydrochloride (CySH) which has an ability to cleave intermolecular disulfide bonds. A rapid decrease in gel hardness and cohesiveness was observed with the increase in added amount of CySH up to 2.5 times 10^-5 mole/g ISP, and then a gradual decrease to 5.0 times 10^-5 mole/g ISP. The changes in these mechanical parameters appeared to depend on the degree of the network formation interpreted from the solubility changes of gels in the phosphate buffer containing 6 M urea. The relaxation time, estimated by compression stress relaxation, was also dependent on the degree of the network formation, while the modulus of elasticity was hardly affected. On the other hand, there was an inverse correlation between the NMR line width of the water proton and expressible water by the pressure method as an index of water-holding properties of the gel; the broader the former, the lesser the latter. The change in the water-holding capacity estimated from expressible water was also associated with that in the degree of the network formation. This confirms that both mechanical and water-holding properties of the gel are qualitatively governed by the extent of the structure formation controlled by the intermolecular disulfide bonds.     

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。     

Effects of malondialdehyde-induced protein modification on water functionality and physicochemical state of fish myofibrillar protein gel

Effects of malondialdehyde (MDA)-induced modification on water distribution in fish myofibrillar proteins (MP) gels were investigated using nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI). The oxidative modifications of MP gels were evaluated by surface hydrophobicity, gel strength, water holding capacity (WHC), scanning electron microscopy (SEM) and SDS-PAGE. Influence of heating procedure on water distribution and functional properties of modified MP gels was also investigated. Results from NMR and MRI indicated that the water functionality was strongly affected by the modification level, which corresponded to the changes of water holding capacity of MP upon MDA modification. Compared with unmodified MP gels, the T₂ relaxation times of modified sample increased significantly, indicating an alteration of water-protein interaction upon MDA-induced modification. The fraction of P₂₃ declined from 7.66% to 0.15% as the MDA addition increased from 0 to 50 mM. Moreover, the relaxation components T_2b disappeared with the addition of MDA mainly due to enhanced protein flexibility and surface hydrophobicity. Besides, the P₂₃ (free water) of heated MP samples increased by 5.41 times compared with that of unheated MP samples.     

不同温度下亚麻籽胶对肌原纤维蛋白凝胶特性的影响及机制

本实验研究了不同加热温度下,添加亚麻籽胶对肌原纤维蛋白保水性、凝胶强度、流变特性、二级结构、微观结构的影响及其作用机制。结果表明,随着温度升高,肌原纤维蛋白凝胶保水性显著下降（P＜0.05）,凝胶强度显著上升（P＜0.05）,加热温度高于50 ℃时添加亚麻籽胶显著提高了肌原纤维蛋白凝胶保水性（P＜0.05）,同时显著降低了凝胶强度（P＜0.05）;拉曼光谱结果表明随着温度从30 ℃上升至80 ℃,凝胶α-螺旋含量显著下降,β-折叠含量显著上升;添加亚麻籽胶使得肌原纤维蛋白存在α-螺旋含量下降,β-折叠含量上升现象,影响凝胶的形成及性质。流变学特性结果显示高于50 ℃时添加亚麻籽胶后肌原纤维蛋白储能模量G’下降。从微观结构发现,添加亚麻籽胶后肌原纤维蛋白在50 ℃出现更多凝胶孔洞,且在70、80 ℃时形成的凝胶三维网络结构更为致密均一。