分子力对大豆蛋白透明凝胶作用机理研究

通过对大豆分离蛋白／大豆7S球蛋白凝胶光学和流变学性质与溶剂、牛血清白蛋白、脂肪酸盐浓度关系的深入研究,探讨了分子力对大豆蛋白透明凝胶的作用机理。结果表明：氢键、静电力和疏水作用对大豆蛋白透明凝胶的形成具有重要的影响。这为进一步研究大豆蛋白凝胶的光学性质和研制透明的大豆蛋白产品提供理论依据。     

大豆7S球蛋白凝胶光学性质的研究

本文深入地研究了大豆7S球蛋白凝胶光学和流变学性质与蛋白质浓度、加热温度和加热时间的关系。结果表明在形成蛋白质凝胶(蛋白质浓度≥7.5%)的前提下,低的蛋白质浓度有利于大豆7S球蛋白形成透明性凝胶,但凝胶强度较低;温度＞85℃有利于蛋白凝胶透明性和强度的提高;加热60min.较为适宜。扫描电子显微镜(SEM)观察显示大豆7S球蛋白透明凝胶具有有序微观结构;探讨了大豆7S球蛋白形成透明凝胶机理。可为进一步研究大豆蛋白凝胶的光学性质和研制透明的大豆蛋白产品提供理论依据。     

大豆7S球蛋白凝胶光学性质的研究 注

本文深入地研究了大豆7S球蛋白凝胶光学和流变学性质与蛋白质浓度,加热温度和加热时间的关系,结果表明,在形成蛋白质凝胶（蛋白质浓度≥7．5％）的前提下,低的蛋白质浓度有利于大豆7S球蛋白形成透明性凝胶,但凝胶强度较低,温度＞85℃有利于蛋白凝胶透明性和强度的提高,加热60min,较为适宜,扫描电子显微镜（SEM）观察显示,大豆7S球蛋白透明凝胶具有有序微观结构,探讨了大豆7S球蛋白形成透明凝胶机理,可为进一步研究大豆蛋白凝胶的光学性质和研制透明的大豆蛋白产品提供理论依据。     

鸡蛋品质与蛋白凝胶性的相关性研究

为探索贮藏过程中鸡蛋品质与蛋白凝胶质构性质的关系,试验研究了不同贮藏条件下,鸡蛋失重率、哈夫单位、浓蛋白含量、蛋白pH等品质变化及其对蛋白凝胶的质构性质、微观结构的影响。结果表明鸡蛋品质与贮藏时间呈负相关,且温度越高,品质下降速度越快,蛋白凝胶质构性质与贮藏时间呈正相关。鸡蛋品质与蛋白凝胶质构性质之间有显著的相关性:失重率和pH与凝胶质构性质呈正相关,哈夫单位和浓蛋白含量与凝胶质构性质呈负相关。由蛋白凝胶的微结构变化推断,鸡蛋品质变化引起蛋白质分子间作用力的变化,改变了蛋白凝胶的微观结构和质构性质。鸡蛋贮藏过程中可以使用品质指标表征蛋白凝胶的质构性质变化规律。     

大豆7S球蛋白透明凝胶形成机理研究

深入研究了大豆７Ｓ球蛋白凝胶透明性和流变学性质与ＰＨ值、加热温度、蛋白质浓度、ＮａＣｌ浓度的关系。结果表明：在ＰＨ〈３．５或ＰＨ〉６．５,蛋白质浓度〉７．５％,低ＮａＣｌ浓度有地大豆７Ｓ球蛋白形成透明性凝胶,但凝胶强度较低;温度〉８５℃有地蛋白凝胶透明性和强度的提高。电子显微镜观察显示：大豆７Ｓ球蛋白透明凝胶具有序微观结构;探讨了大豆＆Ｓ球蛋白形成透明凝胶机理。可为进一步研究大豆蛋白凝胶的光学性质     

低酰基结冷胶-乳清蛋白混合凝胶的凝胶特性

研究了离子种类、离子浓度和基体浓度对低酰基结冷胶/乳清蛋白混合凝胶力学性质、保水性质、光学性质和网络孔径的影响。研究发现,乳清蛋白浓度对混合凝胶凝胶特性影响较小。混合凝胶的断裂应力、断裂应变、不透明性和保水性随着低酰基结冷胶浓度的增大而增大,混合凝胶网络孔径则随着低酰基结冷胶浓度的增大而减小。离子种类和离子浓度对混合凝胶凝胶特性影响显著,混合凝胶的断裂应力和孔径随着离子浓度的增加出现了先增大后降低的变化趋势,断裂应变和保水性则随着离子浓度的增大而减小。离子浓度增大,混合凝胶的不透明指数随之升高,当离子浓度超过某一定值后,不透明指数则基本保持恒定。相对于钠离子而言,钙离子形成的凝胶更强且用量更少。钠离子和钙离子在诱导凝胶形成上不存在协同效应。     

大豆分离蛋白热变性程度对肌纤维蛋白凝胶性质的影响

研究大豆分离蛋白(SPI)热变性程度对肌肉纤维蛋白(MPI)凝胶性质的影响.将SPI在80,90,100℃分别热处理0,15,30,60,100,180 min,得到一系列不同热变性程度的SPI,将其与MPI按1:3(V:W,总蛋白浓度为4%)的比例混合,热诱导得到混合蛋白凝胶.分别研究这些混合蛋白的流变学性质、凝胶性质以及凝胶持水性.结果表明:热变性的SPI有利于混合凝胶的性质提高,经过100℃热处理180 min的SPI与MPI形成的混合蛋白的弹性模量G'值最大,凝胶强度和弹性也最接近纯MP凝胶性质,持水性甚至好于纯MP凝胶性质.     

植物蛋白质凝胶光学性质研究的进展(二)

2 3大豆 7S和 11S球蛋白混合体系凝胶光学性质的研究 　　在 7S和 11S大豆球蛋白混合体凝胶的形成过程中, 7S和 11S大豆球蛋白非共价键相互反应,形成在凝胶化过程中由 7S和 11S大豆球蛋白组成的可溶性聚集。大豆 7S球蛋白其凝胶特性和凝胶化机理是不同于 11S球蛋白的 [10],大豆 7S球蛋白能够形成透明的凝胶,但是凝胶强度较低;而大豆 11S球蛋白能够形成强度较高的凝胶,但是凝胶的透明性较低。在 7S和 11S大豆球蛋白混合体凝胶的形成过程中,大豆 7S球蛋白能够抑制 11S大豆球蛋白分解出不溶解的碱性亚单位,因此, 7S和 11S大…     

葡聚糖对大豆7S蛋白凝胶流变性质及微观结构的影响

采用小变形振荡流变及激光共聚焦技术研究葡聚糖分子质量对热致大豆7S蛋白凝胶的微观结构及动态黏弹性质的影响作用.结果表明:热致大豆7S蛋白凝胶的黏弹性质随添加葡聚糖分子质量的增加而增加,主要由于大分子质量的葡聚糖可以扩大其在葡聚糖/大豆7S蛋白混合体系中的空间占有体积和降低大豆7S蛋白的临界凝胶浓度所致.同时提高变温速率和葡聚糖分子质量对大豆7S蛋白凝胶黏弹性质有协同增加效应.增加葡聚糖分子质量7S蛋白凝胶结构逐步由相分离结构转变为互穿型蛋白-多糖双连续结构.     

木瓜蛋白酶促使大豆蛋白胶凝的研究--7S/11S比例对胶凝性质的影响

适量的木瓜蛋白酶可以促使大豆分离蛋白形成凝胶.大豆分离蛋白的两种主要组分是7S和11S蛋白.本文就木瓜蛋白酶作用于大豆分离蛋白、7S和11S蛋白溶液形成凝胶过程的流变性质进行了研究.结果表明,酶的水解速度和凝胶的形成速度成正比.大豆分离蛋白中的7S和11S蛋白为形成酶促凝胶的关键组分,11S蛋白的浓度对凝胶的强度起决定作用,其他蛋白成分的存在会降低对7S和11S蛋白的有效酶活力.7S凝胶的δ值最小,弹性成分比例最大;11S凝胶的G′值最大,弹性最强.     

Gelling properties of protein fractions and protein isolate extracted from Australian canola meal

Gelling properties of canola albumin and globulin fractions, and canola protein isolate (CPI) were examined in this study. The effects of pH and salt concentration on canola protein gelling properties were studied primarily by means of dynamic oscillatory rheology and gel texture analysis. The findings were supported by confocal laser scanning microscopy (CLSM) images of the gels, isoelectric point, and solubility measurement data. All canola proteins showed typical heat-set gel protein profiles. Gels formed at higher pH had better gelling properties including higher overall resistance to deformation (G*), higher gel elasticity (low tan δ ), higher fracture stress and firmness, and denser gel microstructure. Isoelectric points of canola proteins used in this study were in the range of pH 3.0–4.7 where low protein solubility was observed. The albumin fraction was able to form a very weak gel at pH 4, whereas the globulin fraction and CPI precipitated due to loss of protein surface charge. The effects of NaCl on gelling were protein sample dependent. The presence of NaCl negatively affected gelling properties of albumin and globulin fractions, with decreases in overall resistance to deformation (G*), and fracture stress and firmness, but positively affected CPI gels in the same aspects. The elasticity (tan δ) of all canola protein gels remained constant in the presence of NaCl. Frequency sweep analysis revealed that the albumin fraction and CPI formed weak gels, whereas the globulin fraction formed a strong gel. Strain sweep analysis further confirmed that the globulin fraction formed a stronger gel with a critical strain of at least 10%. This study demonstrates the high potential of canola proteins, particularly the globulin fraction, as a prospective gelling agent.     

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.     

发芽对大豆蛋白凝胶性质的影响

研究了发芽大豆蛋白质凝胶性质的变化。采用碱提酸沉法制备大豆分离蛋白(SPI),以葡萄糖酸-δ-内酯(GDL)为凝固剂制备大豆蛋白凝胶,系统研究了不同芽长大豆蛋白凝胶强度的变化。通过SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)图谱分析了发芽过程中SPI的变化及其对大豆凝胶强度的影响。结果发现:SPI中7S球蛋白的α'、α亚基和11S球蛋白的酸性亚基A3、A发芽时发生明显降解,但11S球蛋白各亚基在发芽初期变化小,利于大豆蛋白质分子之间形成网络结构使凝胶强度增强。随着发芽时间的延长,11S球蛋白也部分发生降解,凝胶强度下降。     

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.     

Effects of partial hydrolysis on structure and gelling properties of oat globular proteins

The effects of partial hydrolysis and the environmental conditions (pH and temperature) on the gelling properties of oat protein isolate (OPI) were investigated. OPI was treated with flavourzyme, alcalase, pepsin and trypsin. The changes in protein structure were observed by SDS-PAGE, size exclusion high performance liquid chromatography (SE-HPLC) and amino acid analysis. Gel mechanical properties were evaluated by textural profile analysis (TPA). The results revealed that the acidic polypeptides (12S-A) of oat globulin exerted great influence over the gelling ability of oat protein. Partial hydrolysis by flavourzyme and trypsin could significantly improve oat protein gel strength, especially at pHs 8–9 by modulating the balance between the electrostatically repulsive force and the hydrophobic attractive force among polypeptide chains during the gelling process. The gels prepared with flavourzyme and trypsin treated oat proteins have comparable or higher mechanical strength than soy protein gels at neutral pH. At pH 9 the gel made of trypsin treated oat protein even showed comparable mechanical strength to egg white protein gels under the same pH. Both oat protein and its hydrolysate gel exhibited excellent water-holding capacity at neutral or mildly alkaline conditions. The results of this study indicate that oat protein has a promising potential to be used as new and cost-effective gelling ingredient of plant origin to provide texture and structure in food products.     

尿素对肌原纤维蛋白热诱导凝胶非共价键作用力及特性的影响

研究尿素对肌原纤维蛋白凝胶非共价键作用力和特性的影响及其调控机制,揭示凝胶作用力和特性之间的关系,并探讨通过添加尿素研究凝胶氢键和疏水作用方法的科学性。分别用0.0~0.4 mol/L尿素处理肌原纤维蛋白并加热制成凝胶,用Zeta电位仪测定其静电相互作用;利用拉曼光谱仪测定其疏水相互作用与氢键;用离心法和质构仪测定相应尿素浓度条件下热诱导凝胶的保水性、硬度和弹性。结果表明,随着尿素浓度增大,热诱导凝胶的Zeta电位绝对值由7.83 m V下降到5.55 m V;S_0-ANS从698.5逐渐增大到885.3;I_(760 cm~(-1))/I_(1 003 cm~(-1))由0.957 1降到0.849 3;I_(850 cm~(-1))/I_(830 cm~(-1))先下降后上升;随着尿素浓度增大,凝胶保水性、硬度和弹性都存在下降的现象。相关性分析表明静电相互作用、表面疏水性和疏水相互作用显著影响肌原纤维蛋白热诱导凝胶保水性和质构特性。     

APPLICATION OF SURFACE FRICTION MEASUREMENTS FOR SURFACE CHARACTERIZATION OF HEAT-SET WHEY PROTEIN GELS

The surface properties of heat‐set whey protein gels (14 wt %) was studied by measuring the friction at the gel's surface. A simple device was constructed that can be conveniently attached to a Texture Analyzer. Surface friction forces of gels with and without addition of salt were measured as a function of sliding speed and surface load. Surface friction strongly depended on the sliding speed for all three gel systems over the speed range 0.01 mm/s to 10 mm/s. The gel without salt addition showed the highest speed dependency, while the gel containing 200 mM NaCl had the lowest speed dependency. Surface load tests showed nearly linear relationships for both protein gels (with and without salt addition). Unlike solid materials, both protein gels exhibited a surface friction even as the surface load approached zero. Possible contributions of surface attraction and viscous flow to the measured forces are discussed. Results from surface friction tests were further confirmed by optical observation of the surface using a confocal laser scanning microscope (CLSM), where a very smooth surface was observed for the whey protein gel without salt addition, but a much rougher surface was observed for the gel containing 200 mM NaCl.     

pH值对11S球蛋白结构与凝胶性的影响

研究了豫豆-25 11S球蛋白凝胶质构特性与pH值的关系。结果表明:pH值对豫豆-25 11S球蛋白凝胶的形成及质构特性影响较大,酸性条件下的凝胶与碱性条件下的有较大的差异。扫描电子显微镜(SEM)观察及傅立叶交换红外光谱(FTIR)分析显示:在远离等电点的碱性条件下,11S球蛋白凝胶具有较高有序性的微观结构,它们的微观结构均匀,只有少量的聚合物;酸性条件下的凝胶的微观结构有序性低于碱性条件下的凝胶,离等电点较近pH的凝胶聚合物较多,微观结构有序性低;pH4.15的凝胶要比pH7.5的含有更多的无规则卷曲结构。凝胶蛋白二级结构中无规则卷曲向有序结构的转化,微观结构趋于有序。     

Effects of combined high-pressure and heat treatment on the textural properties of soya gels

SPI, 7S, and 11S globulin at 12% (w/v) protein concentration, at neutral pH, did not form gels when heat-treated (90 °C, 15 min) or when high pressure-treated (300–700 MPa), except for the 11S, which formed a gel when heat-treated. The combination of heat and pressure (that is heating the solutions in a water bath and then pressure-treating at room temperature or the reverse sequence), led to differences: when heat-treatment was before high-pressure treatment, only the 11S fraction formed a self-standing gel; however, when the solutions were pressurised before heat treatment, all the proteins formed self-standing gels. The textural and water-holding properties were measured on the gels formed with the three different soy proteins.