丝素的功能性质

丝素在pH3～10范围内具有较好的乳化能力和优良的乳化稳定性;氯化钠的添加使丝素的乳化能力和乳化稳定性略微下降;随着丝素质量浓度的增加,丝素的乳化能力和乳化稳定性均增强,当丝素质量浓度高于0.5g/dL时,乳化能力的增幅变缓。丝素的表面疏水性低于酪蛋白酸钠,经高速剪切作用后,表面疏水性显著增加。以丝素为壁材的微胶囊化薄荷油缓释性能良好。     

高酰基结冷胶/酪蛋白酸钠复合凝胶粘弹行为的研究

本文研究了酪蛋白酸钠浓度、结冷胶浓度、离子和测试条件对高酰基结冷胶/酪蛋白酸钠复合凝胶粘弹性的影响。结果表明:高酰基结冷胶/酪蛋白酸钠共混体系为典型的切力变稀流体,表观粘度随着酪蛋白酸钠浓度的升高而降低,而随着阳离子浓度的增大出现先增大后减小的变化趋势。压缩速度对复合凝胶硬度几乎无影响,而内聚性和弹性则随着压缩速度的增加而增大。内聚性随着压缩应变的增大出现先增大后减小的变化趋势。复合凝胶的硬度和弹性随着酪蛋白酸钠浓度的增加而下降,但复合凝胶的内聚性对酪蛋白酸钠浓度不敏感。高酰基结冷胶浓度越高,复合凝胶的硬度和弹性越大。相对于一价离子而言,二价离子形成的凝胶更强且用量更少。钾离子的添加对复合凝胶保水性影响较弱,而钙离子的添加则可以提高复合凝胶的保水性。     

可溶性丝素蛋白的流变性质和胶凝性质

研究了可溶性丝素蛋白的流变性质和胶凝性质。丝素蛋白溶液的黏度随质量浓度的增加而增加;随着温度的升高,丝素蛋白溶液的黏度不断的降低;在剪切速率为0～30S-1的范围内,丝素蛋白溶液是剪切变稀的假塑性流体,剪切速率大于30S-1时,丝素蛋白溶液是牛顿流体;动态流变性质的研究表明,丝素蛋白溶液是典型的粘性流体;随着丝素蛋白质量浓度的增大,凝胶强度增大;丝素蛋白溶液的质量浓度大于100g/L时,丝素蛋白溶液在加热后的冷却过程中会形成凝胶,丝素蛋白溶液的质量浓度越高,则其胶凝点也越高。     

丝素蛋白结构的研究 2.探讨丝素形成凝胶的机理

采用拉曼光谱、红外光谱和X-射线衍射法测定可溶性丝素形成凝胶时的结构,结果表明可溶性丝素形成凝胶时p-折叠和结晶区明显增加.丝素凝胶的形成涉及疏水相互作用和β-折叠的形成,并通过聚集作用形成了网状结构,氢键和静电相互作用对此网状结构起了稳定作用.     

乳清组分的波动对牛乳体系及其酶凝胶特性的影响

为探讨牛乳乳清的组成成分对酪蛋白胶束酶凝胶特性的影响,采用超滤浓缩技术去除渗透液,并分别用去离子水、乳清蛋白和酪蛋白酸钠溶液取代所除掉的渗透液,进而改变乳清相的蛋白质组成和离子强度。研究表明,添加乳清蛋白和酪蛋白酸钠虽未对酪蛋白胶束的结构和电荷特性产生影响,但能显著阻碍蛋白质凝胶结构的形成。研究发现添加酪蛋白酸钠能够完全阻止酪蛋白凝胶结构的形成,主要是它通过疏水作用与酪蛋白胶束相结合,从而提高酪蛋白胶束间的静电和空间排斥作用。另外,添加去离子水的样品显著降低了体系的钙离子浓度。酪蛋白胶束的Zeta电势值从-20 mV增到-33 mV,同时粒径从163 nm降到153 nm。钙离子浓度的降低显著减缓了酶凝胶的形成过程,凝胶时间延长到93 min,所得凝胶的弹性模量仅为1.5 Pa。本研究发现乳清中的钙离子含量、蛋白质含量及种类都能显著影响酪蛋白胶束的酶凝集过程。酪蛋白酸钠具有强大的阻碍酪蛋白胶束聚集的能力。此外,钙离子浓度的降低也会对酪蛋白凝胶结构的形成及特性产生影响,乳清中足量的钙离子浓度(330 mg/L)是获得良好凝胶结构的必要条件。     

微生物转谷氨酰胺酶催化酪蛋白酸钠聚合物的功能特性研究

研究了微生物转谷氨酰胺酶(TGase)催化酪蛋白酸钠聚合对其功能特性的影响。结果显示,随着催化时间的增加,其各组份含量不断减少,同时生成的聚合物含量不断增加,比较了TGase催化不同酪蛋白的聚合速率,结果显示转谷氨酰胺酶较易催化α-和β-酪蛋白,而不易催化κ-酪蛋白TGase催化聚合酪蛋白酸钠能明显改善其乳化性能,聚合时间越长,乳化指数越高,而乳化稳定性随聚合时间先升后降,4h时最高TGase催化酪蛋白酸钠还可提高其热稳定性,然而对其起泡性影响不大     

剪切稀化效应对肌原纤维蛋白凝胶特性的影响

将肌原纤维蛋白充分剪切后,以不同放置时间下的黏度来评价剪切稀化程度,分析剪切稀化效应对肌原纤维蛋白凝胶特性的影响,并设置对照组排除无关因素的影响。结果表明,实验组中,剪切稀化程度随着放置时间的延长逐渐降低,同时肌原纤维蛋白凝胶的储能模量逐渐增加,凝胶持水性、凝胶强度、化学作用力显著提高(P<0.05),凝胶孔径逐渐减小,结构变得质密均匀,二级结构中β-折叠含量显著增加(P<0.05),β-转角含量显著降低(P<0.05);而对照组在剪切稀化程度一致的情况下,凝胶特性不随放置时间发生明显变化。这表明是剪切稀化效应影响了肌原纤维蛋白的凝胶特性,即剪切稀化效应的减小有利于形成稳定的凝胶结构,提升肌原纤维蛋白的凝胶特性。     

酪蛋白凝胶颗粒对水包油型乳液稳定性及体外消化的影响

研究酪蛋白凝胶颗粒对水包油型乳液的稳定性及体外消化特性的影响,并与商业乳化剂酪蛋白酸钠和吐温20作对比。采用马尔文激光粒度仪、纳米粒度电位仪及稳定性分析仪分别测定水包油乳液的粒径、电位和稳定性;通过模拟体外消化,研究酪蛋白凝胶颗粒稳定的乳液的消化情况并比较不同种类乳化剂对乳液体外消化特性的影响。结果表明,酪蛋白凝胶颗粒稳定的乳液不稳定性指数为0.71±0.09,显著低于酪蛋白酸钠和吐温稳定乳液的不稳定性指数(分别为1.43±0.09,1.62±0.15),稳定性最好。这与酪蛋白软颗粒能以完整的颗粒结构存在于油水界面后形成较强的空间位阻和静电作用有关。体外消化结果表明,酪蛋白凝胶颗粒稳定的乳液脂肪酸的释放量为(86.13±3.91)%,而酪蛋白酸钠和吐温20稳定的乳液脂肪酸释放量分别为(86.79±3.61)%,(91.62±1.31)%,三者并没有显著性差异,表明酪蛋白凝胶颗粒对乳液消化不产生抑制作用。乳化剂种类虽对初始消化速率有影响,但不影响消化终点。结论:酪蛋白凝胶颗粒能够较好地稳定水包油乳液且不影响其消化。     

剪切作用下高浓度再生丝素蛋白水溶液性质的研究

研究了不同剪切作用下高浓度再生丝素蛋白水溶液的性质,并利用拉曼光谱分析了丝素蛋白分子受剪切作用后的构象变化。结果发现：浓度和剪切作用是影响再生丝素蛋白水溶液性质的两个重要因素。高浓度再生丝素蛋白水溶液经过一定的剪切作用后将呈现各向异性的性质,且随着溶液中丝素蛋白浓度的增加,溶液出现各向异性现象所需要的临界剪切作用力减小;而在相同浓度下,剪切作用越大,再生丝素蛋白水溶液中丝素蛋白分子沿剪切作用方向的有序程度也随之增加。在一定的剪切作用下,高浓度再生丝素蛋白水溶液中部分丝素蛋白分子可由原来的无规线团和(或)α螺旋结构转变成β折叠结构。     

可溶性丝素蛋白的功能性质

研究了可溶性丝素蛋白的功能性质。结果表明,丝素蛋白具有表面活性,能降低溶液的表面张力;经高速剪切作用后,丝素蛋白的表面疏水性显著增强;随着丝素蛋白质量浓度的增加,丝素蛋白溶液的乳化性、起泡性均增强,当丝素蛋白质量浓度大于5g/L时乳化能力增幅不明显,当丝素蛋白质量浓度为15g/L时,它的起泡能力最高,质量浓度继续增加至20g/L时其起泡能力下降,当丝素蛋白质量浓度高于15g/L时,泡沫稳定性的增幅变缓;丝素蛋白在pH3～10范围内具有较好的乳化性、起泡性,在pH4时最强。     

RHEOLOGY OF ACID-INDUCED SODIUM CASEINATE STABILIZED EMULSION GELS

The storage modulus G', loss modulus G", and phase angle δ of acidinduced sodium caseinate emulsion gels were measured at 25C for a certain period of time after the addition of glucono-δ-lactone (GDL). Comparison between pure protein gels and emulsion gels revealed that the presence of emulsion droplets greatly enhanced the gel strength. Acidification by mixing an emulsion with a GDL solution caused immediate gelation but the emulsion gel had similar mechanical properties to the gel formed by direct addition of GDL granules. The viscoelasticity of the gel was strongly related to the pH value of the system. There was no evidence for a three-dimensional network when the pH value was higher than 5.8 or lower than 3.2. The largest storage and loss moduli were observed for gels formed at pH values near the isoelectric point of sodium caseinate (pH 4.6). Rheological differences for gels made at different pH values became distinguishable at low frequencies, where a much smaller phase angle was determined for a gel made at a pH value below the isoelectric point. Partial recovery of the three-dimensional gel network was observed for disrupted gels formed at a pH near the isoelectric point.     

Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels

The aim of this work was to study the potential of tyrosinase enzymes in structural engineering of acid-induced milk protein gels. Fat free raw milk, heated milk or a sodium caseinate solution were treated with tyrosinases from Trichoderma reesei (TrTyr) and Agaricus bisporus (AbTyr) and the reference enzyme transglutaminase (TG) prior to acid-induced gelation. TrTyr treatment increased the firmness of raw milk and sodium caseinate gels, but not that of heated milk gels, even though protein cross-linking was detected in heated milk. AbTyr did not cross-link proteins in any of the studied milk protein systems. TG was superior to TrTyr in gels prepared of heated milk. In acidified heated milk and sodium caseinate, TrTyr and TG treatment resulted in a decrease of the pore size. Scanning electron microscopy revealed more extensive particle interactions in the heated milk gels with TG than with TrTyr.     

Formation of two types of gels from bovine myosin

Myosin was isolated from bovine m. semimembranosus and gels were formed by heat treatment at different pH values and ionic strengths. The gels were subjected to rigidity measurements and their microstructure was studied by scanning electron microscopy. This article provides evidence that myosin can form two completely different gel structures in the pH range 5.5–6.0, depending on ionic strength. Fine stranded gel structures were formed at low ionic strength (0.25M KCl), whereas coarsely aggregated gel structures were formed at high ionic strength (0.6M KCl). The fine stranded structure had a higher rigidity than the coarsely aggregated structure. It was found that all fine strand myosin gels were formed from turbid solutions and the aggregate gels from clear solutions. When the pH was lowered to 4 in 0.6M KCl a strand-type gel structure formed spontaneously on dialysis, even without heat treatment. This structure did not change in character on heating. It was concluded that the conditions required for the formation of strand-type myosin gels were already present before the heat treatment and that the strands were made up of myosin filaments at certain pH and ionic strength combinations, which produced a turbid solution. The strand-type structures were considered specific with regard to myosin interactions which was not the case for the aggregated structures. Variation of the heating temperature in the range 55 to 65°C had no major effect on the type of structure formed.     

Textural Properties of Cold-set Gels Induced from Heat-denatured Whey Protein Isolates

A 9% whey protein (WP) isolate solution at pH 7.0 was heat-denatured at 80°C for 30 min. Size-exclusion HPLC showed that native WP formed soluble aggregates after heat-treatment. Additions of CaCl2 (10–40 mM), NaCl (50–400 mM) or glucono-delta-lactone (GDL, 0.4–2.0%, w/v) or hydrolysis by a protease from Bacillus licheniformis caused gelation of the denatured solution at 45°C. Textural parameters, hardness, adhesiveness, and cohesiveness of the gels so formed changed markedly with concentration of added salts or pH by added GDL. Maximum gel hardness occurred at 200 mM NaCl or pH 4.7. Increasing CaCl2 concentration continuously increased gel hardness. Generally, GDL-induced gels were harder than salt-induced gels, and much harder than the protease-induced gel.     

Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels

The mechanical properties and microstructure of 2.7% and 4.5% sodium caseinate gels chemically acidified by glucono-δ-lactone (GDL) and cross-linked by microbial transglutaminase (TG) were studied. The acidification was performed at different temperatures. According to SDS–PAGE TG clearly caused polymerisation of caseinate irrespective of the treatment temperature (4–50 °C), The cross-linking of the proteins was more extensive at temperatures 22–50 °C. Low amplitude viscoelastic measurements showed that 4.5% caseinate gels acidified at 50 °C were formed much faster than gels acidified at 22 °C. TG only slightly increased the time of gelling. Control gels prepared without TG at temperatures of 4, 22, 37 and 50 °C were mechanically weak. Examination of the control gels with a confocal laser scanning microscope showed that gels formed at 37 and 50 °C were coarse and porous with large cavities between particle aggregates, whereas those formed at 22 °C were much more homogeneous. The TG-treated and acidified sodium caseinate dispersions formed firm gels, indicating cross-linking of casein proteins. Interestingly, the strongest gels were formed at 22 and 37 °C. TG treatment improved the homogeneity of the gel structure at temperatures of 37 and 50 °C. The hardness of TG-treated gels acidified at 4 °C increased during 1 week of storage.     

Glycation of caseinate by fructose and fructo‐oligosaccharides during controlled heat treatment in the ‘dry’ state

This paper investigates the controlled heating of caseinate with reducing sugars to produce glycoproteins with improved functionality for use in food. Caseinate was combined with inulin, fructose and a mixture of both inulin and fructose and the lyophilisates heated at a controlled water activity for up to 48 h. Caseinate–glucose and caseinate–lactose glycoconjugates were prepared for comparison. Conjugation between caseinate and fructose occurred readily at 60 °C and 67% relative humidity, modifying up to 75% of the lysine groups of caseinate within 48 h. Moreover, when reconstituted, the caseinate–fructose glycoconjugates showed a dramatic increase in viscosity relative to caseinate ‘dry’‐heated alone. At 80% relative humidity the reaction proceeded so rapidly that gels containing darkly coloured particulate matter were formed. Incorporation of inulin prevented formation of caseinate–fructose gels, and minimised browning development while still producing moderately viscous solutions. Based on ¹³C‐NMR, SDS‐PAGE and electron microscopy techniques, mechanisms by which inulin modified the reaction have been proposed. Copyright © 2005 Society of Chemical Industry     

The effect of shear on the rheology and structure of heat‐induced whey protein gels

The influence of mechanical shearing on the small deformation properties and microstructure of heat‐induced whey protein gel has been studied. The viscoelastic properties of these gels at different concentrations of 10% and 20% (w/w) exposed to different shear rates of 0, 50, 100, 200 and 500 s^?1 during gelation were measured using dynamic oscillatory rheometry. The structure of both the shear treated and unsheared gels was then investigated using light microscopy. The results showed that the storage modulus of the gels at both concentrations was increased by increasing the shear rate exposure during gelation while the shear‐treated gels were more elastic and showed frequency‐independent behaviour. As the total protein concentration of the gel increased, the viscoelastic properties of the gels also increased significantly and the gels showed greater elasticity. The gels obtained from the higher shear rate exposure were stronger with higher elastic moduli at both protein concentrations. Images of the gels obtained using light microscopy showed that shearing resulted in phase separation and some aggregation in the structure of the gels at both concentrations. However, the shearing rates applied in this study were not enough to cause aggregation breakdown in the gel network.