棕榈酰化大豆蛋白的制备及其乳化性能的研究

棕榈酰基通过碱催化的酯交换反应与大豆蛋白的ε-NH2共价结合，以棕榈酸N-羟琥珀酰亚胺酯为酰化试剂。在pH9．0，温度25℃条件下，棕榈酰基与大豆蛋白结合得到不同改性程度的棕榈酰化蛋白。测定了改性对大豆蛋白表面疏水性和乳化性的影响。随着酰化程度的增加，大豆蛋白表面疏水性增加，溶解性下降。改性程度迭30．21％的棕榈酰化蛋白具有较原料蛋白明显改善的乳化性能，其表面疏水性较高，而溶解性又没有明显降低。     

琥珀酰化调控大豆分离蛋白电荷密度对其构象及乳化性的影响

通过加入琥珀酸酐对大豆分离蛋白(soybean protein isolate,SPI)进行改性,探究琥珀酰化调控SPI电荷密度引起的构象改变和乳化性改善之间的关系.通过荧光光谱、紫外光谱、傅里叶变换红外光谱分析不同酰化程度SPI的构象变化,采用扫描电子显微镜、电位、表面疏水性、分子柔性及乳化性等手段表征琥珀酰化对SP...     

酰化对大豆蛋白结构和功能性质影响

酰化改性是现代食品蛋白质化学的研究热点。通过对大豆蛋白质乙酰化和琥珀酰化的改 性研究发现,随酰化试剂用量的增大,酰化程度不断提高,在相同酰化试剂用量下,乙酰化 程度高于琥珀酰化。随酰化程度增大,大豆蛋白质表面疏水性,分子柔性和溶性粘度不断 增大,这表明酰化改变了大豆蛋白的结构;在低于原大豆蛋白等电点的ｐＨ范围内,酰化 对其功能性质影响不大,而在高于或等于原大豆蛋白等电点的ｐＨ范围内,酰化可显著地 提高大豆蛋白的水溶性,乳化活性和乳化稳定性,琥珀酰化对大豆蛋白结构和功能性质的 影响均大于乙酰化。研究还发现酰化可使大豆蛋白质的等电点降低。     

酰化对大豆分离蛋白发泡性能的影响

采用乙酸酐和琥珀酸酐对大豆分离蛋白(SPI)进行化学改性.研究了酰基化程度、pH和离子强度对SPI发泡性能的影响.结果表明,随酰化试剂用量的增大,酰基化程度不断提高,在相同酰化试剂用量的条件下,乙酰化程度高于琥珀酰化.SPI的发泡性经酰化改性后得到明显改善,且随酰基化程度的增大而逐步提高,琥珀酰化的作用更突出;但酰化不利于SPI的泡沫稳定性,其随酰基化程度的增大而不断下降,琥珀酰化的下降更显著.     

琥珀酰化改性对米糠蛋白功能性质的影响

为了改变米糠蛋白的功能性质,扩大米糠蛋白在食品工业的应用范围,利用琥珀酸酐对米糠蛋白进行酰化改性处理。通过单因素反应,确定了琥珀酸酐酰化改性米糠蛋白的最适反应条件为:米糠蛋白浓度为10%,反应温度为35℃,琥珀酸酐/蛋白质用量为15%。在最适反应条件下,分别反应40 min、80 min,制得酰化度分别为46.8%、69.2%的琥珀酰化米糠蛋白。评价了上述两种琥珀酰化米糠蛋白制品的溶解性、乳化性、起泡性等功能性质,结果表明,琥珀酰化改性对米糠蛋白的溶解性、乳化稳定性以及起泡性均有一定改善,而酰化米糠蛋白的乳化活性、泡沫稳定性随着酰化程度的提高有所下降。     

酰化对大豆分离蛋白乳化性能的影响

目的:研究化学改性对大豆分离蛋白(SPI)乳化性能的影响;方法:采用乙酸酐和琥珀酸酐对SPI进行化学改性;结果:随酰化试剂用量的增大,酰化程度不断提高,在相同酰化试剂用量的条件下,乙酰化程度高于琥珀酰化.SPI的乳化活性指数(EAI)和乳化稳定性(ES)都随酰化程度的增大而增大.在中性和弱碱性(pH 5.0～9.0)范围内,酰化明显提高了SPI的EAI和ES.琥珀酰化的改性效果优于乙酰化;不过离子强度削弱了SPI的EAI和Es;结论:酰化可有效提高SPI的乳化性能,其中琥珀酰化的改性效果优于乙酰化.     

酰化对大豆分离蛋白水合性质的影响

采用乙酸酐和琥珀酸酐对大豆分离蛋白（SPI）进行化学改性。研究了不同改性程度下SPI水合性质的变化。结果表明：随酰化试剂用量的增大，酰化程度不断提高，在相同酰化试剂用量的条件下，乙酰化程度高于琥珀酰化，5．0～8．0的中性与弱碱性范围内，酰化明显提高了蛋白质的溶解性，持水性和粘度也均得到改善，其中琥珀酰化的作用比乙酰化显著。     

小麦面筋蛋白琥珀酰化修饰研究

采用琥珀酸酐对小麦面筋蛋白进行改性修饰，系统研究了底物浓度、改性剂用量和反应温度对反应程度、溶解性、乳化性、起泡性和泡沫稳定性等蛋白功能特性的影响。优化出小麦面筋蛋白琥珀酰化的最佳条件：琥珀酰化底物浓度10％，琥珀酸酐用量15％，反应温度45℃。应用红外光谱对最优条件下改性的面筋蛋白结构进行了表征。将琥珀酰化改性后的小麦面筋蛋白添加至小麦粉中，面团粘着性提高32％。     

改性对玉米蛋白质功能性质和结构的影响(II)酰化

通过乙酰化和琥珀酰化对玉米蛋白质功能性质和结构的影响研究发现 ,随酰化试剂用量的增大 ,蛋白质的酰化程度提高 ,且在相同摩尔酰化试剂剂量下 ,乙酰化程度高于琥珀酰化 :随酰化程度的增大 ,玉米蛋白质的溶液粘度 ,表面疏水性和分子柔性不断增大 ,蛋白质的等电点向酸性方向漂移 ,水溶性 ,乳化活性和乳化稳定性在等于或高于原蛋白质等电点的pH范围内增大 ,而在低于原蛋白质等电点的pH范围内降低 ;酰化程度越高对蛋白质功能性质和结构的影响越大 ,相同摩尔酰化试剂剂量下 ,琥珀酰化的影响大于乙酰化。     

大豆球蛋白吸附在油—水界面上的膨胀流变特性

采用动态滴形分析法研究了大豆球蛋白(soy glycinin)吸附在油-水界面上的膨胀流变特性,主要检测了不同初始体相蛋白浓度(C0)和pH值条件下,大豆球蛋白吸附在纯的花生油-水界面上的界面张力(σ)和界面膨胀流变特征参数(界面膨胀模量E、界面膨胀弹性Ed、界面膨胀黏性Ev以及相角θ)随时间的变化.结果表明:随着吸附时间的延长,σ降低,E和Ed增大而减小,大豆球蛋白分子吸附到油-水界面上形成界面蛋白吸附膜;随着C0的增加,吸附速率加快,吸附膜的界面膨胀黏弹性增大,受pH值的影响更为明显;在试验时间(0～120 min)和频率(0.01～0.5 Hz)范围内,吸附膜的Ed明显大于Ev,从流变学的角度分析,大豆球蛋白吸附到花生油-水界面上形成弹性的吸附膜.     

大豆球蛋白吸附在空气-水和油-水界面上的比较研究

采用动态滴形分析法研究了大豆球蛋白在空气-水和油-水界面上的吸附特性,主要检测了大豆球蛋白吸附在空气-水、纯的花生油-水和正十四烷-水界面上的界面张力和膨胀流变特征参数随吸附时间的变化.结果表明:吸附速率随着初始体相蛋白浓度的增加而加快,受界面类型的影响比较明显;大豆球蛋白在三种界面上吸附的速率顺序为:正十四烷-水界面>空气-水界面>花生油-水界面;在空气-水和花生油-水界面上,大豆球蛋白的吸附及其吸附膜的形成机制基本类似;而在花生油-水和正十四烷-水界面上,吸附膜的膨胀流变特性差别较大.     

大豆蛋白乳化性能比较及机理探讨

以大豆浓缩蛋白、改性大豆浓缩蛋白、大豆分离蛋白、商业大豆分离蛋白和酪蛋白钠为原料,比较了它们的乳化性、界面张力、NSI、表面疏水性、分子量分布等方面的差异.结果表明,不同大豆蛋白乳化能力差别很大,但界面张力无显著差异;NSI较好的大豆蛋白乳化能力较强,疏水性和分子量的增大也有利于乳化能力的提高;同时将NSI、表面疏水性和分子量分布等综合考虑,将能更好地解释和预测大豆蛋白的乳化性能.     

添加儿茶素对喷雾干燥后的大豆分离蛋白结构、功能性和消化特性的影响

商用大豆分离蛋白（Soybean Protein Isolate,SPI）经高温喷雾干燥处理后,蛋白会发生一定程度的变性聚集,使溶解性等功能性质降低。本研究通过添加不同含量的儿茶素（Catechin,C）,探究儿茶素-大豆蛋白相互作用对喷雾干燥大豆分离蛋白结构和功能特性的影响。结果表明:随着儿茶素添加量的增加,儿茶素的荷载率和装载含量逐渐增加,SPI与儿茶素结合后其表面疏水性和巯基含量逐渐下降;添加儿茶素可有效改善喷雾干燥SPI导致的功能下降问题,在儿茶素添加量为1%时,与对照组SPI相比,溶解性提高了36.4%,乳化性、乳化稳定性分别提高了13.7%和14.3%;在儿茶素添加量为0.25%时,凝胶硬度与对照组相比提高了43.6%,进一步研究发现凝胶网络结构主要依赖于二硫键,其次是氢键、离子键,且此时凝胶流变特性中的储能模量显著高于其他各处理组（P<0.05）;通过原子力显微镜发现,添加儿茶素后凝胶的微观结构向规则均匀致密转化,当儿茶素添加量为0.25%时,复合物凝胶的聚集程度较小,但儿茶素的加入降低了喷雾干燥SPI的消化率。综上所述,在喷雾干燥过程中儿茶素能够与SPI中的基团结合,导致巯基含量和表面疏水性降低,进而干预了蛋白质分子间的热聚集,从而改善SPI的功能特性。     

巯基乙醇对大豆分离蛋白热致聚合物界面性质的影响

为探讨β-巯基乙醇对大豆分离蛋白热致聚合物界面性质的影响,以大豆分离蛋白为原料,在pH7.0、90 ℃加热添加和不添加β-巯基乙醇（2 mmol/L）浓度为10 mg/mL的大豆分离蛋白溶液0 h和10 h,制备不同大豆分离蛋白质热致聚合物。观察了大豆分离蛋白、添加β-巯基乙醇大豆分离蛋白、大豆分离蛋白热致聚合物和β-巯基乙醇大豆分离蛋白热致聚合物的微观形态、游离巯基含量的变化,同时比较了起泡能力、泡沫稳定性、乳化活性、乳化稳定性、表面疏水性和浊度的差异。结果表明,大豆分离蛋白和添加β-巯基乙醇大豆分离蛋白呈现无规则状态,大豆分离蛋白热致聚合物为有规则的球状颗粒,而β-巯基乙醇大豆分离蛋白热致聚合物部分形成球状聚合物部分形成无规则聚合物。添加β-巯基乙醇改善了大豆分离蛋白的界面性质。与大豆分离蛋白相比较,添加β-巯基乙醇大豆分离蛋白和添加β-巯基乙醇大豆分离蛋白热致聚合物的起泡能力分别提高了64.56%和95.77%,乳化活性提高的幅度分别为12.94%和14.61%。添加β-巯基乙醇大豆分离蛋白和添加β-巯基乙醇大豆分离蛋白热致聚合物在长时间储藏中表现出良好的乳化稳定性和泡沫稳定性。这种良好的界面性质源于β-巯基乙醇的加入赋予聚合物具有更高的游离巯基含量和表面疏水性。并且本实验建立了4种样品的泡沫稳定性和乳化稳定性随时间变化的Rational函数和Linear函数经验模型,为大豆分离蛋白质的实际应用奠定了理论基础。     

Subcritical Water Induced Complexation of Soy Protein and Rutin: Improved Interfacial Properties and Emulsion Stability

Rutin is a common dietary flavonoid with important antioxidant and pharmacological activities. However, its application in the food industry is limited mainly because of its poor water solubility. The subcritical water (SW) treatment provides an efficient technique to solubilize and achieve the enrichment of rutin in soy protein isolate (SPI) by inducing their complexation. The physicochemical, interfacial, and emulsifying properties of the complex were investigated and compared to the mixtures. SW treatment had much enhanced rutin‐combined capacity of SPI than that of conventional method, ascribing to the well‐contacted for higher water solubility of rutin with stronger collision‐induced hydrophobic interactions. Compared to the mixtures of rutin with proteins, the complex exhibited an excellent surface activity and improved the physical and oxidative stability of its stabilized emulsions. This improving effect could be attributed to the targeted accumulation of rutin at the oil–water interface accompanied by the adsorption of SPI resulting in the thicker interfacial layer, as evidenced by higher interfacial protein and rutin concentrations. This study provides a novel strategy for the design and enrichment of nanovehicle providing water‐insoluble hydrophobic polyphenols for interfacial delivery in food emulsified systems.     

Interfacial and emulsifying behaviour of crayfish protein isolate

The interfacial behaviour of adsorbed protein films constituted with a crayfish protein derivate that is typically produced as by-product from the food industry, has been studied at the air-water and oil-water interfaces. An analysis of the surface pressure under compression-expansion cycles of this protein was carried out as a function of time, concentration and pH (2 and 8). Besides, interfacial tension and adsorption kinetics also were determined as a function of time at different concentrations and pH values. Interfacial rheological properties were studied under dilatational deformations applied to a single droplet, either at the initial step of film formation or once the interfacial tension was at equilibrium and the film was completely formed. The contribution of the interfacial properties to the behaviour of oil-in-water emulsions stabilised with this protein derivative were also analysed. Finally, droplet size distributions obtained for concentrated emulsions stabilised by crayfish protein were analysed and related to the interfacial tension behaviour. We have demonstrated that crayfish proteins at pH 8 show higher solubility, smaller aggregates and better interfacial activity (higher surface pressure and lower interfacial tension) with higher interfacial viscoelasticity, than at pH 2. A two-dimensional model of the results showed that oil-water and air-water interfaces are clearly related to the improved stability of emulsion made with crayfish proteins at pH 8.     

Emulsifying properties of canola and flaxseed protein isolates produced by isoelectric precipitation and salt extraction

The emulsifying (emulsion capacity, EC; emulsion activity/stability indices, EAI–ESI and creaming stability, CS) and physicochemical properties (surface charge/hydrophobicity, protein solubility, interfacial tension, and droplet size) of chickpea (ChPI), faba bean (FbPI), lentil (LPI), and pea (PPI) protein isolates produced by isoelectric precipitation and salt extraction were investigated relative to each other and a soy protein isolate (SPI). Both the legume source and method of isolate production showed significant effects on the emulsifying and physicochemical properties of the proteins tested. All legume proteins carried a net negative charge at neutral pH, and had surface hydrophobicity values ranging between 53.0 and 84.8 (H₀-ANS), with PPI showing the highest value. Isoelectric precipitation resulted in isolates with higher surface charge and solubility compared to those produced via salt extraction. The EC values ranged between 476 and 542 g oil/g protein with LPI showing the highest capacity. Isoelectric-precipitated ChPI and LPI had relatively high surface charges (~−22.3 mV) and formed emulsions with smaller droplet sizes (~ 1.6 μm), they also displayed high EAI (~ 46.2 m²/g), ESI (~ 84.9 min) and CS (98.6%) results, which were comparable to the SPI.     

超声处理大豆分离蛋白与壳聚糖复合物对O/W型乳液稳定性的影响

为探究超声处理大豆分离蛋白-壳聚糖（soybean protein isolate-chitosan,SPI-CS）复合物对形成O/W型乳 液性质的影响,主要研究了复合物表面疏水性、乳化活性、乳化稳定性与油-水界面张力、乳液粒径、乳液稳定性 之间的关系。结果表明：未经超声处理的SPI-CS复合物表面疏水性、乳化活性、乳化稳定性和界面吸附性较低,形 成的O/W型乳液粒径相对较大,约100 μm,乳液Zeta电位较低,乳滴有发生聚集的倾向。乳液贮存7 d后乳层析指数 最高。经超声处理后SPI-CS复合物形成的乳状液性质发生明显变化,随着超声功率的增加,形成的O/W型乳液的稳 定性有所增加：超声功率为400 W时SPI-CS复合物形成的乳液最为稳定,乳层析指数最低;当超声功率超过400 W 时,乳液的光学显微镜观察显示其粒径有所增大,同时乳液的Zeta电位、乳化活性和乳化稳定性明显下降,界面张 力降低缓慢。超声处理暴露了蛋白质分子的内部结构,使部分结构展开、柔性增加,促进了其与壳聚糖之间的静电 相互作用,说明超声处理的大豆分离蛋白与壳聚糖形成的复合物影响了O/W型乳液的稳定性及相关性质。     

Interfacial behaviour of succinylated faba bean legumin at low ionic strength

Changes in the tensio-active properties of the main storage protein from faba beans (legumin) after succinylation were studied at a low salt concentration. Surface tension, surface dilatational properties of monolayers and emulsifying activity were measured at a ionic strength of I = 0.02. The results were compared with those at a high ionic strength of I = 0.3. Parameters of the Gibbs' adsorption isotherm indicate that the most surface-active derivatives are legumins with a moderate degree of succinylation (34% and 65%). The equilibrium surface pressure, π_e, inreased from 18.47 (native legumin) to 20.72 mN/m (65% succinylation). The critical association concentration, CAC, i. e., the subphase concentration at which the plateau of π_e was reached, decreased from 15.9·10^–6 to 7.12·10^–6 g/ml after 34% succinylation. The film forming properties differed from the adsorption behaviour. Only monolayers of the 65% succinylated legumin exhibited viscoelastic behaviour. By contrast, the emulsifying activity, EAI, reached the highest values for the 65% and 95% succinylated legumins. Low salt concentrations favour the adsorption of the native legumin and reduce the surface activity of succinylated legumin. Monolayer formation and especially the ability to form elastic networks seems to be diminished by the repulsive interaction of like-charged molecules. The emulsifying properties of the higher succinylated legumins are not influenced by the ionic strength whereas those of the native and low succinylated legumin are distinctly lower at I = 0.02. This result points to different adsorption and stabilizing processes during emulsion formation.