大豆分离蛋白起泡性和乳化性影响因素的研究

大豆分离蛋白的乳化性和起泡性与蛋白质、NaCl、卡拉胶、蔗糖和山梨酸钾含量、pH值、加热温度等密切相关。蛋白质质量浓度分别为2.0g/100mL和2.5g/100mL时,大豆分离蛋白乳化性和起泡性分别达到最大值;远离pH4.5,大豆分离蛋白起泡性和乳化性增加;加热温度45℃时起泡性最好,而乳化性最差;氯化钠、卡拉胶、山梨酸钾添加量分别为1.00g/100mL、0.20g/100mL、0.08g/100mL时,起泡性和乳化性好;添加蔗糖会使蛋白质的起泡性下降,而蔗糖添加量6.0g/100mL时乳化性好。     

不同酶切方式对乳清蛋白疏水性和乳化性的影响

采用不同的蛋白酶对乳清蛋白进行水解,考察了肽键断裂方式对乳清蛋白肽疏水性和乳化性的影响,以及乳清蛋白不同酶解产物的疏水性和乳化性的关系。结果表明:不同蛋白酶作用于乳清蛋白得到的水解产物疏水性不同,6种蛋白酶解液的疏水性均随水解度的增大而降低,其中以胰凝乳蛋白酶酶解液的疏水性下降的最慢。研究还发现,乳化性随着水解度增加而先升高后下降,以双酶复合酶解液最差。不同蛋白酶水解液的乳化性指数随疏水性指数的降低而升高,乳化性指数与疏水性氨基酸质量分数成正相关。     

烘烤对核桃蛋白二级结构、表面疏水性及乳化性的影响

研究了烘烤增香过程对核桃蛋白的二级结构、表面疏水性以及乳化性的影响,采用扫描电镜、圆二色谱等仪器进行分析。结果表明,烘烤处理的蛋白微结构成片状,α-螺旋结构从42.7%降低至27.6%,β-转角从17.3%增加到25.3%,无规则卷曲从24.7%增加到32.7%,β折叠比例不变。界面张力从20.98减少为18.49,表面疏水性从316.14降低为297.55。使用turbiscan多重光散射仪对蛋白与三种植物油形成的乳化液进行分析,其中烘烤处理的蛋白与花生油形成乳化液稳定性指数为15.98,与大豆油形成的乳化液稳定性指数为14.53,与葵花籽油形成的乳化液稳定性指数为14.55,相比较于未处理蛋白形成的乳化液稳定性均显著下降。      

酶解对蛋清蛋白液起泡性能和乳化性能的影响

利用碱性蛋白酶水解蛋清蛋白,主要研究了酶用量、底物浓度和酶解时间对蛋清蛋白液起泡性能和乳化性能的影响。实验结果表明,酶解条件对蛋清蛋白液的起泡性能和乳化性能有一定程度的影响,当碱性蛋白酶酶解温度为45~50℃,pH6~8.5时,其最佳酶解条件为酶用量4%,底物浓度3%,酶解时间6h。在此最佳酶解条件下获得的蛋清蛋白酶解液起泡性为27.65%,发泡能力178.26,泡沫稳定性60.33%,乳化容量37.86%,乳化稳定性127.23,乳化活性指数134.53,乳状液稳定指数1.83。      

Influence of enzymatic hydrolysis,pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

The aim of this work was to enhance emulsification properties of canola proteins through enzymatic proteolysis and pH variaton. Canola protein isolate (CPI) and hydrolysates (CPHs) were used to form emulsions at pH 4.0, 7.0 and 9.0 followed by storage at 4 or 25 °C for 7 days. Controlled enzymatic hydrolysis led to increased peptide bond cleavage with time (0.23 g/100 g in CPI to 7.18 g/100 g after 24‐h Alcalase hydrolysis). Generally, oil droplet sizes were smaller for emulsions made at pH 9.0, which suggest better quality than those made at pH 4.0 and 7.0. Trypsin hydrolysate emulsions were the most physically stable at pH 7.0 and 9.0; in contrast, the pepsin hydrolysate emulsions were unstable at all conditions. The results suggest that selective enzymatic hydrolysis could play an important role in enhancing successful incorporation of canola proteins and peptides into food systems as protein emulsifiers.     

Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation

The application of mung bean protein in foods is limited due to its poor functionality. Acylation with succinic anhydride could be used to improve the functionalities of protein. In this study, the influence of the weight ratio of succinic anhydride to protein (0–0.10) on the degree of N-acylation, physicochemical properties and protein functionalities including emulsifying properties of mung bean protein isolates (MPI) were investigated. The extent of N-acylation of MPI increased as the succinic anhydride:protein ratio increased, while the ζ-potential at neutral pH decreased. In addition, succinylation had an impact on the average particle size of MPI depending on the succinic anhydride:protein ratio. Succinylation had no impact on the total and exposed free sulfhydryl groups. Moreover, the isoelectric point (pI) of the succinylated proteins shifted from pH 5 to lower pH. Succinylation increased the emulsifying activity index (EAI), while the impact on the emulsion stability index depended on the succinic anhydride:protein ratio. Thus, succinylation at low succinic anhydride:protein ratio can alter mung bean protein charge and affect physicochemical and functional properties especially emulsifying properties that could be used to increase its utilization.     

The amino acid composition,solubility and emulsifying properties of sweet potato protein

A protein was purified from the high-protein type sweet potato variety 55-2 available in China. The amino acid composition, solubility and emulsifying properties of the sweet potato protein (SPP) were studied. The SPP was rich in aspartic acid (18.5%) and glutamic acid (9.30%) while essential acid amino acids made up approximately 40.7% of the SPP. The SPP was highly soluble in distilled water over a wide range of pH. However, solubility of the SPP in 1.0 M NaCl and 1.0 M CaCl₂ solutions was low especially at pH below the pI of the SPP. The SPP in CaCl₂ demonstrated emulsifying activity index (EAI) and emulsion stability index (ESI) many folds higher than those in distilled water and NaCl solution (P < 0.05).     

pH及离子强度对燕麦分离蛋白功能特性及亚基特性的影响

以燕麦籽粒为原料提取燕麦分离蛋白(OPI),研究不同pH及盐离子强度下燕麦分离蛋白溶解性、起泡性、乳化活性及亚基特性。结果表明:①燕麦分离蛋白在pH 5.0～6.0时溶解度最低,起泡性最低,泡沫稳定性最高,在碱性条件下乳化性及乳化稳定性较高;pH 2.0,3.0的酸性条件造成了可溶性燕麦分离蛋白肽链的部分水解,形成了相对分子质量为31.0～43.0kDa的亚基条带,碱性条件下无明显区别。②NaCl浓度为0.05mol/L时溶解度最低,在0.6～0.9mol/L时,起泡性、泡沫稳定性及乳化性均较高;溶解度最低时,可溶性蛋白主要是由相对分子质量为43.0kDa的亚基组成,NaCl的加入,造成了可溶性燕麦分离蛋白肽链的断裂,形成了相对分子质量分别为43.0,66.2kDa的多肽链。     

玉米胚芽分离蛋白溶解性和乳化性质的研究

以湿法脱胚的玉米胚芽为原料,采用碱溶酸沉法制备了玉米胚芽分离蛋白。探讨了不同实验条件如温度、pH、盐浓度等对玉米胚芽分离蛋白的溶解性和乳化性的影响,并解释了乳化性和溶解性在实验条件下的变化规律。研究结果表明,玉米胚芽分离蛋白在碱性条件下溶解度较好,55℃时溶解度最大;在pH 7.0~8.5范围内乳化活性明显增加,提高温度可以增加蛋白质的乳化活性。     

低pH条件下大豆蛋白7S和11S组分的表面特性

本文采用7S形成纤维聚合结构的制备条件,研究低p H条件下长时间热处理对大豆蛋白7S和11S(包括酸性亚基和碱性亚基)乳化性和起泡性的影响。结果发现,低p H条件下长时间热处理的聚合手段,可以显著(p<0.05)改善不同大豆蛋白组分的起泡性,但对乳化性没有明显的改善作用,甚至对乳化稳定性有降低作用,这种改善程度与是否形成纤维聚合结构无关。与p H7.0条件下的热处理手段相比,低p H条件下长时间热处理的聚合手段能够使大豆蛋白7S和11S表面疏水性显著增加,这种特殊的结构变化更有力于提高起泡性能。因此,在低p H条件下长时间热处理后,7S和11S具有较高的表面疏水性和较好的起泡性能。      

Interfacial and emulsifying properties of lentil protein isolate

The dynamic interfacial tension (DIFT) at oil–water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas > LPI > WPI > BSA > Lys, while their surface hydrophobicity was in the following order: BSA > LPI > NaCas > WPI > Lys. The EAI of emulsions stabilised by the above proteins ranged from 90.3 to 123.3 m²/g and it was 93.3 ± 0.2 m²/g in LPI-stabilised emulsion. However, the stability of LPI-stabilised emulsions was slightly lower compared to that of WPI and NaCas-stabilised emulsions at the same protein concentration at pH 7.0. The ESI of LPI emulsions improved substantially with decrease in droplet size when protein concentration was increased (20–30 mg/ml). Reduction of disulphide bonds enhanced both the EAI and ESI compared to untreated samples. Heat treatment of LPI dispersions resulted in poor emulsion stability due to molecular aggregation. The stability of LPI-stabilised emulsions was found to decrease in the presence of NaCl. This study showed that LPI can be as effective emulsifiers of oil-in-water emulsions as are WPI and NaCas at ?20 mg/ml concentrations both at low and neutral pH. The emulsifying property of LPI can be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents.     

红松种子水溶性蛋白乳化性及起泡性研究

以红松种子为原料,制备红松种子水溶性蛋白,研究了pH、蛋白质量浓度、NaCl浓度对红松种子水溶性蛋白起泡性和泡沫稳定性以及乳化性和乳化稳定性的影响.结果表明:蛋白的起泡性和乳化性随蛋白质量浓度的增加而增大;pH的变化对起泡性和乳化性的影响也较大,等电点处红松种子水溶性蛋白的起泡性和乳化性最差,pH 11时起泡性和乳化性均较好;NaCl浓度对泡沫稳定性影响不大,对乳化稳定性影响较大.     

牡丹籽分离蛋白提取工艺及乳化特性

采用单因素试验及响应面试验优化盐溶法提取牡丹籽分离蛋白工艺,并测定不同p H下牡丹籽分离蛋白的乳化特性。结果表明:牡丹籽分离蛋白的最佳提取工艺条件为提取时间69 min、提取温度40℃、料液比1∶20、Na Cl浓度1.03 mol/L,在此条件下牡丹籽分离蛋白得率为(23.49±1.21)%,纯度为(90.75±0.87)%;牡丹籽分离蛋白乳液在p H为8时,乳化能力、乳液热稳定性均最高,分别为(85.27±1.23)%和(90.74±1.07)%;乳液在p H 2~5时,形成Pickering乳液,显著增加乳液热稳定性、粒径,改变乳液颜色;乳液p H 8~10,形成O/W型乳液,乳液p H越高,乳化能力、乳液热稳定性越低,乳液粒径越小,乳液颜色越深;乳液中性条件下,粒径较大,热稳定性较低。     

酱油渣中蛋白的乳化特性研究

对比分析了酱油渣中蛋白(SRP)、糖基化大豆分离蛋白(GSP)和大豆分离蛋白(SPI)的ξ-电位、疏水性以及乳化活性和乳化稳定性。发现SRP的总糖和蛋白含量比为1∶1.4,其中含有大量的糖蛋白;SRP疏水性是SPI的2.5倍。SRP等电点接近pH=3.5,在酸性环境下溶解性较好。在酸性、高盐环境下SRP乳化能力高于GSP和SPI,在pH=5时,SRP的乳化活性(EAI)是SPI的8.1倍,在NaCl浓度为0.3mol/L时,SRP的EAI是SPI的1.77倍。     

Effect of pH and NaCl/CaCl2 on the solubility and emulsifying properties of sweet potato protein

BACKGROUND: The effects of NaCl and CaCl₂ on the solubility and emulsifying properties, namely emulsifying activity index (EAI) and emulsion stability index (ESI) of sweet potato proteins (SPPs) at pH 1–10, were investigated. RESULTS: At lower NaCl (0.1 mol L^?1) and CaCl₂ (0.05 mol L^?1) concentrations, the solubility profiles of the SPPs were very similar to those in distilled water, and the lowest solubility occurred at pH 4. Increased NaCl and CaCl₂ concentration resulted in lower SPP solubility in most of the pH studied (P < 0.05). At pH < 3, NaCl improved the EAI of SPP while at pH > 7 it reduced the EAI of the SPP (P < 0.05). Moreover, addition of NaCl also resulted in reduction of ESI of the SPP in most of the pH studied (P < 0.05). On the other hand, the presence of 0.2 mol L^?1 CaCl₂ rendered the EAI and ESI of the SPPs independent of the influence of pH. CONCLUSION: The present studies show that pH and salts modified the emulsifying properties of the SPPs, and CaCl₂ at a certain concentration could be used to improve the emulsifying properties of the protein. Copyright © 2008 Society of Chemical Industry     

使用圆二色性光谱分析二级结构对大豆分离蛋白表面疏水性的影响

旨在采用圆二色性光谱手段研究二级结构对我国六种经常使用的大豆品种制备而成的分离蛋白的表面疏水性的影响。实验先是对六个品种的大豆进行分离蛋白的提取,并对其性质进行测定,包括溶解度和表面疏水性;再对六种大豆分离蛋白的二级结构进行测定和分析;通过SPSS软件对六种大豆分离蛋白的表面疏水性和二级结构的数值进行线性相关性分析,探究二者之间的构效关系。研究中发现六个品种的大豆分离蛋白的二级结构、溶解性、表面疏水性都差异显著（p<0.05）,表面疏水性的大小随着α-螺旋含量升高而减小,随着无规则卷曲和β-折叠含量增大而提高,因β-转角含量变化的影响不明显。SPSS线性相关性分析表明品种间的表面疏水性与β-转角含量线性关系不显著,与无规则卷曲、β-折叠含量呈正向相关,与α-螺旋含量呈负向相关。      

温度对于大豆分离蛋白起泡性的影响研究

研究了20～90℃下商业用大豆分离蛋白(SPI)的起泡性。随着溶解温度的升高,5%大豆分离蛋白的溶解性及疏水性逐渐提高,起泡能力逐渐增强,泡沫稳定性则逐渐下降;将不同温度下5%大豆分离蛋白中的可溶性蛋白采用离心方法分离后发现可溶性蛋白的起泡性表现出与5%大豆分离蛋白相反的趋势,尤其在20～40℃的溶解温度下可溶性蛋白的起泡性远远优于大豆分离蛋白的起泡性。研究结果也说明,溶液中高比例可溶性大豆蛋白的存在可能有利于蛋白质泡沫的形成,但不能对泡沫的稳定性起到良好的支撑作用,同时大豆蛋白在溶液中的构象也会影响其起泡性。     

离子强度对大豆分离蛋白结构及表面疏水性的影响

旨在采用生物化学和光谱学方法及手段,从蛋白质分子空间构象和溶液性质角度,探讨离子强度对大豆分离蛋白结构及表面疏水性的影响机制。研究表明:大豆分离蛋白表面疏水性在等电点两侧呈现显著下降趋势,而随着离子强度的增大大豆分离蛋白表现出\     

热处理对葵花籽分离蛋白结构及表面疏水性的影响

将7%葵花籽分离蛋白(SSPI)悬浮液在热处理温度分别为92、102℃(热变性温度)、112℃处理10 min,以未处理的SSPI为对照研究热处理对蛋白质结构及表面疏水性的影响。结果表明:热处理的SSPI亚基含量发生了显著变化,有聚集物生成;经过热处理的SSPI表面形貌粗糙,疏松多孔,微观结构更加没有规则;热处理后蛋白质分子伸展,SSPI发生聚集,相对荧光强度、表面疏水性下降。     

多糖类稳泡剂对大豆分离蛋白起泡性的影响

探讨了黄原胶等稳泡剂对大豆分离蛋白(SPI)起泡性的影响。黄原胶等稳泡剂可能是由于增加了连续相黏度,继而起到了稳泡作用;而由于热处理能够使蛋白质分子表面暴露的疏水性氨基酸残基增加,从而提高了起泡能力。通过响应面(RSM)分析实验,得出改善SPI起泡特性的最佳工艺条件:加热温度67℃,加热时间18 min,蛋白质浓度3.29(W/V),黄原胶添加量0.13(W/V),搅打时间4.56 min。将最终得到的SPI泡沫与蛋清白泡沫比较,发现二者具有类似的黏性和硬度,且在气泡大小和形状上也较为相近。