米黑毛酶提高大豆分离蛋白泡沫稳定性的研究

通过测定不同水解pH条件、不同水解时间、不同搅打起泡pH条件下大豆分离蛋白(SPI)的泡沫稳定性,结合SDS-PAGE分析,水解度分析及蛋白分子表面疏水性分析,为利用米黑毛酶水解大豆分离蛋白制备高泡沫稳定性大豆蛋白制品提供一定的理论依据。显示结果表明:SPI经米黑毛酶在pH 3.5处水解45~60 min后,回调pH至5.0搅打起泡的泡沫稳定性最优;随水解时间增长,SPI的泡沫稳定性有不同程度提高。通过酶解作用,伴随SPI的蛋白分子量减小,蛋白分子表面疏水性增加,泡沫的稳定性显著提高。     

Alcalase蛋白酶酶解高温豆粕制备水溶性大豆多肽

以氮溶指数为指标,应用Alcalase蛋白酶酶促降解高温豆粕,以获得高得率的水溶性大豆肽。酶促降解的优化实验结果表明:在加酶量1750U/g、底物浓度4%(w/w)、温度60℃、pH9.0的条件下酶促降解3h所得到的水解产物其氮溶指数达到了62.97%,比水解前提高了47.87%;酶解前后大豆蛋白的SDS-PAGE图谱表明:Alcalase蛋白酶可以催化大豆蛋白迅速地降解,水解1h后,7S蛋白的α-亚基,α’-亚基,β-亚基以及11S的酸性亚基已经完全消失,水解3h后,11S的碱性亚基也基本消失,且大多数的肽类分子量在20ku以下;与以大豆分离蛋白为原料制备的多肽相比,以高温豆粕为原料制备的多肽苦味值较低。     

极端pH处理对大豆分离蛋白、β-伴大豆球蛋白、大豆球蛋白结构和功能特性的影响

为丰富大豆蛋白柔性改性技术,采用极端pH条件(pH 1,2,3,4,10,11,12,13)处理大豆分离蛋白(SPI)、β-伴大豆球蛋白(7S)和大豆球蛋白(11S)。通过对SPI、7S和11S蛋白进行凝胶电泳分析、氨基分析、巯基分析和色氨酸荧光分析,并测定大豆蛋白表面疏水性、溶解性、乳化性和起泡性,探讨极端pH处理对SPI、7S和11S结构和性质的影响。结果表明:极端pH处理可导致SPI、7S和11S游离氨基和内源色氨酸荧光强度增加,蛋白表面疏水性提高,三级结构部分展开。此外,极端pH处理可诱导SPI与11S亚基部分解离,而对7S亚基影响较小。极端pH处理能够提高SPI、7S和11S蛋白溶解性、乳化性和起泡性。11S球蛋白可能是SPI结构变化和功能特性改善的主要贡献者。由此可见,极端酸碱处理通过诱导大豆蛋白高级结构的展开,改善其功能特性。     

富硒发芽对大豆蛋白凝胶性质的影响

以10 mg/L Na2SeO3溶液浸泡的大豆为材料,采用碱提酸沉法制备大豆分离蛋白(soybean protein isolate,SPI),以葡萄糖酸-δ-内酯(GDL)为凝固剂制备大豆蛋白凝胶,系统研究了富硒处理及发芽时长对大豆蛋白凝胶性质的影响。结果发现:发芽48 h内大豆GDL凝胶与SPI凝胶的硬度快速下降,分别由25.25 g和27.73 g降至10.77 g和13.37 g,持水性从61.42%和62.64%分别降至51.55%和55.54%。SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)图谱显示,富硒大豆与对照SPI谱带变化基本一致,其中7S球蛋白的β亚基与11S球蛋白的碱性亚基B较稳定,而7S球蛋白的α'亚基和α亚基与11S球蛋白的酸性亚基A3和A则被内源蛋白酶逐渐降解为相对分子质量较小的组成,从而影响发芽大豆凝胶性质。而富硒处理对发芽大豆蛋白凝胶性质影响较小。     

干热处理对大豆分离蛋白乳化与起泡性能的影响

研究了60℃、80℃和90℃下干热处理对大豆分离蛋白乳化和起泡性能的影响.研究发现,干热处理4 d使大豆分离蛋白的乳化活性增加到最大值,其乳化稳定性也增加到接近最大值的水平,长时间的热处理降低大豆分离蛋白的乳化活性;60℃干热处理1 d使大豆蛋白的膨胀率增加到最大值880%,此后随热处理时间的延长而持续下降,80℃和90℃热处理降低了大豆分离蛋白的泡沫稳定性;干热处理使大豆分离蛋白7S亚基各组分和部分11S酸挂亚基发生共价聚合形成高分子量的聚合物.     

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。     

不同乳化剂对大豆基搅打稀奶油的影响

本研究以大豆油体为原料,探究了不同乳化剂(大豆皂苷、大豆卵磷脂、大豆多糖、吐温80)对大豆基搅打稀奶油的粒径分布、粘度、乳状液稳定性、搅打起泡率、泡沫稳定性的影响。结果表明,不同乳化剂对大豆基搅打奶油的乳状液特性和搅打特性有一定影响。添加吐温80的大豆基搅打稀奶油有较小的粒径分布,ζ-电位为-30.3 mV,粘度比加其他大豆乳化剂的小,而且搅打起泡性最高,达到112.4%,但是泡沫稳定性只有2.1%。添加大豆乳化剂的大豆基搅打稀奶油具有类似的乳状液特性,但是添加大豆卵磷脂的大豆基搅打稀奶油比其他两种大豆乳化剂具有更高的膨胀率(134.5%),而添加大豆多糖的大豆基搅打稀奶油具有更好的泡沫稳定性(1.2%)。     

糖含量对大豆蛋白起泡性的影响

采用美拉德反应协同β-淀粉酶定向断裂共聚糖链，获得具有不同糖含量的大豆蛋白(SPI)，分析糖含量对SPI起泡性及其相关特性的调控作用。通过美拉德反应制备糖基化产物，随后利用β-淀粉酶对糖基化大豆蛋白的侧链糖基进行水解，得到糖含量分别为8.10，4.88，2.21 g/100 g大豆蛋白的糖基化修饰产物，并对其起泡性及相关特性分析。SDS-PAGE电泳图谱证实SPI与麦芽糊精发生糖基化反应。内源荧光光谱分析结果表明，糖基化产物的三级结构变得更加疏松；美拉德反应提高了SPI(pH 7.0)的起泡性及泡沫稳定性，即:起泡性从83.48%提高到132.63%，泡沫稳定性从57.95%提高到71.56%。糖含量的变化对SPI的起泡性影响显著，随糖含量的增加，起泡性逐渐增大；而(4.88~8.10 g/100 g大豆蛋白)对SPI的泡沫稳定性影响不显著。随着糖含量的下降，糖基化产物的水合粒径、Zeta电位的绝对值、溶解性逐渐减小，表观黏度逐渐降低。研究结果为定向开发特定功能的大豆蛋白提供理论参考。     

大豆蛋白亚基组成对其功能特性影响的研究现状

综述了大豆蛋白亚基组分的研究现状,并从大豆分离蛋白(SPI)功能特性,豆腐、豆乳品质及特异种质大豆品种的蛋白功能性评价3个方面介绍了亚基组成对大豆蛋白功能特性影响研究的最新进展.结果表明,大豆蛋白7S和11S组分及其亚基组成,11S/7S比值与大豆蛋白的功能特性及加工特性密切相关.     

发芽对大豆分离蛋白功能性质的影响

研究发芽对大豆分离蛋白(SPI)功能性质的影响。采用碱提酸沉法制备不同发芽阶段的SPI,研究大豆蛋白功能性质变化。结果表明：发芽使大豆SPI溶解性、吸水性、起泡性和乳化性均有所增加,其中芽长1cm大豆SPI具有最佳的蛋白功能性质。SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)结果表明：大豆发芽过程中7S球蛋白更易受蛋白酶影响而发生降解,使其内部疏水性氨基酸残基暴露,从而使大豆SPI的功能性质不能持续改善。     

抗坏血酸对大豆分离蛋白酶解产物功能特性影响研究

采用木瓜蛋白酶水解不同浓度的大豆分离蛋白,研究了抗坏血酸对较低水解度（DH为3.7%）和较高水解度（DH为8.9%）酶解产物黏度、发泡性、发泡稳定性、乳化性和乳化稳定性的影响.结果表明：在水解度为3.7%的、浓度为7%的大豆分离蛋白酶解液中添加0.3%抗坏血酸,体系的黏度最大、乳化性最强、乳化稳定性最高;在水解度为8.9%的、浓度为3%的大豆分离蛋白酶解液中添加0.3%抗坏血酸,体系的发泡性最大;在水解度为3.7%的、浓度为7%的大豆分离蛋白酶解液中添加0.5%抗坏血酸,体系的泡沫体积比最大.     

Interfacial and foaming properties of soy protein and their hydrolysates

The objective of the work was to study the impact of soy protein hydrolysis on foaming and interfacial properties and to analyze the relationship between them. As starting material a sample of commercial soy protein isolate was used (SP) and hydrolysates were produced by an enzymatic reaction, giving hydrolysates from 0.4% to 5.35% degree of hydrolysis (DH).In this contribution we have determined foam overrun (FO), stability against liquid drainage and foam collapse, and the apparent viscosity of foams produced by a whipping method. The surface properties determined were the adsorption isotherm and surface dilatational properties of two hydrolysates (2 and 5.35% DH, H1 and H2 respectively).The hydrolysis of soy proteins increased the surface activity at bulk concentrations where SP adopts a condensed conformation at the monolayer. At concentrations where it adopts a more expanded conformation a very low degree of hydrolysis (H1) also promoted the enhancement of surface activity. However, at 5.35% degree of hydrolysis (H2) the surface activity decreased. Moreover, H2 presented lower surface activity than H1 at every bulk concentration.The hydrolysis increased the elastic component of the dilatational modulus and decreased phase angle of films at bulk concentrations below that corresponding to the collapse of SP monolayer (2% bulk protein).SP hydrolysis increased foam overrun and the stability against drainage that could be related to increased surface activity of protein hydrolysates. However, the collapse of foams was promoted by hydrolysis and could be ascribed to a decrease of the relative viscoelasticity (higher phase angle) of surface films.The results point out that a low degree of hydrolysis (2–5%) would be enough to improve the surface activity of SP, decrease foam drainage and maintaining a considerable viscoelasticity of the surface films to retard foam collapse.     

大豆分离蛋白发泡剂的泡沫染色

采用搅打发泡的方法研究了大豆分离蛋白浓度、pH值、表面活性剂对大豆分离蛋白泡沫性能的影响;选取多个有利于泡沫性能的因素,以大豆蛋白泡沫作为染料载体,选用活性黄染料对纯棉织物进行了泡沫染色的探究,测试了染色织物的匀染性、拉伸性和色牢度。结果表明,在pH值为7,大豆分离蛋白质量分数2%,十二烷基硫酸钠(SDS)质量浓度1g/L,Tween-80质量浓度2g/L的条件下,泡沫性能最优。泡沫染色织物的匀染性、色牢度均优于常规水浴染色,织物强力提高。     

Influence of the presence of monoglyceride on the interfacial properties of soy protein isolate

BACKGROUND: This study focused on the contribution of soy protein isolate (SPI), in the absence or presence of monostearin (ME), to surface and interfacial properties as a function of protein concentration and pH, which is relevant to the physical stability of a variety of food systems. RESULTS: An increase in protein content always yielded a rapid decrease in surface tension followed by an evolution towards an asymptotic value. Addition of ME gave rise to mixed SPI/ME films, although the interface became dominated by SPI above the concentration for interfacial saturation. The relative interfacial shear viscosity of SPI films showed a marked dependence on: aging time, which may be attributed to a reorganisation of protein species at the interface with some penetration of hydrophobic parts into the oil phase; shear forces, which may partially reverse this reorganisation, leading to shear‐thickening behaviour; and pH, which is the key factor controlling which SPI species is predominant at the interface. The effect of adding ME also depends on pH, favouring a reinforcement of SPI/ME films only at low pH, at which 3S and 7S fractions are dominant. CONCLUSION: The results obtained indicate that SPI shows excellent potential to favour stabilisation of air/water and oil/water interfaces in food systems. Copyright © 2012 Society of Chemical Industry     

Alcalase酶解制备大豆肽工艺条件的优化

以大豆分离蛋白为原料,研究了用Alcalase碱性蛋白酶水解制备大豆肽。以蛋白水解度和蛋白水解液等电点溶解度为指标,通过单因素试验及正交试验得出最佳水解条件为：料液比1：20,酶解pH8．5,酶解温度60℃,加酶量5400U／g蛋白。此条件下,蛋白水解度为18．79％,等电点溶解度是86．32％。     

Interfacial and foaming properties of enzyme-induced hydrolysis of sunflower protein isolate

Plant proteins are increasingly being used as an alternative to proteins from animal sources in human nutrition. In this contribution we are concerned with the analysis of interfacial (adsorption isotherm, rate of adsorption, and surface dilatational properties) and foaming characteristics (foaming power and foam stability) of a sunflower protein isolate (SPI) and its hydrolysates with different degrees of hydrolysis (DH), as a function of the protein concentration in aqueous solution. Caseinate has been utilized as a protein of reference. We have observed that the adsorption and foaming power (foam capacity, gas and liquid retention in the foam, and foam density) increases with the protein concentration in the aqueous phase, depending on the DH. The adsorption kinetic at short adsorption time is diffusion controlled. However, the controlling mechanism at long-term adsorption is the penetration of the protein at the interface. A close relationship was observed between foaming and the rate of diffusion of the protein to the air–water interface. The foam stability—quantified by the relaxation time due to drainage (t_d) and disproportionation/coalescence (t_dc)—correlates with the equilibrium surface pressure (π_e) of the film adsorbed from aqueous solutions of the protein.     

Improving the functional properties of soy glycinin by enzymatic treatment. Adsorption and foaming characteristics

In this contribution we have determined the effect of limited enzymatic hydrolysis on the interfacial (dynamics of adsorption and surface dilatational properties) and foaming (foam formation and stabilization) characteristics of a soy globulin (glycinin, fraction 11S). The degree of hydrolysis (DH=0%, 2%, and 6%), the pH of the aqueous solution (pH=5 and 7), and the protein concentration in solution (at 0.1, 0.5 and 1 wt%) were the variables studied. The temperature and the ionic strength were maintained constant at 20 °C and 0.05 M, respectively. The rate of adsorption and surface dilatational properties (surface dilatational modulus, E, and loss angle) of glycinin at the air–water interface depend on the pH and DH. The adsorption decreased drastically at pH 5.0, close to the isoelectric point of glycinin, because of the existence of a lag period and a low rate of diffusion. The interfacial characteristics of glycinin are much improved by enzymatic treatment, especially in the case of acidic aqueous solutions. Hydrolysates with a low DH have improved functional properties (mainly foaming capacity and foam stability), especially at pH close to the isoelectric point (pI), because the native protein is more difficult to convert into a film at fluid interfaces at pH≈pI. The foam capacity depends on the rate of diffusion of protein to the interface and is much improved by the enzymatic treatment. Foam stability correlates with surface pressure and, to a minor extent, with surface dilatational modulus at long-term adsorption with few exceptions.     

Interactions between Whey Protein Isolate and Soy Protein Fractions at Oil–Water Interfaces: Effects of Heat and Concentration of Protein in the Aqueous Phase

ABSTRACT:  The 2 main storage proteins of soy—glycinin (11S) and β-conglycinin (7S)—exhibit unique behaviors during processing, such as gelling, emulsifying, or foaming. The objective of this work was to observe the interactions between soy protein isolates enriched in 7S or 11S and whey protein isolate (WPI) in oil–water emulsion systems. Soy oil emulsion droplets were stabilized by either soy proteins (7S or 11S rich fractions) or whey proteins, and then whey proteins or soy proteins were added to the aqueous phase. Although the emulsifying behavior of these proteins has been studied separately, the effect of the presence of mixed protein systems at interfaces on the bulk properties of the emulsions has yet to be characterized. The particle size distribution and viscosity of the emulsions were measured before and after heating at 80 and 90 °C for 10 min. In addition, SDS-PAGE electrophoresis was carried out to determine if protein adsorption or exchanges at the interface occurred after heating. When WPI was added to soy protein emulsions, gelling occurred with heat treatment at WPI concentrations >2.5%. In addition, whey proteins were found adsorbed at the oil–water interface together with 7S or 11S proteins. When 7S or 11S fractions were added to WPI-stabilized emulsions, no gelation occurred at concentrations up to 2.5% soy protein. In this case also, 7S or 11S formed complexes at the interface with whey proteins during heating.     

大豆蛋白水解产物中巯基的热稳定性和抗氧化作用的研究

研究了大豆蛋白水解产物中巯基的热稳定性及抗氧化作用。结果表明,SPI水解不影响巯基含量;加热时大豆蛋白溶液中巯基含量下降近52%,而大豆蛋白水解产物中巯基的含量只下降4%,说明大豆蛋白水解产物中巯基的热稳定性明显提高。当巯基被封闭时,大豆蛋白水解产物的抗氧化性明显减弱,说明巯基是大豆蛋白中很重要的抗氧化成分,但较其他一些抗氧化基团更易于氧化。