米糠蛋白的起泡特性及其泡沫微观形态

考察pH值和NaCl浓度对米糠蛋白起泡特性及泡沫微观形态的影响,并对二者之间的内在关系进行阐述。结果表明,当米糠蛋白溶液中不添加NaCl、pH?4时起泡能力较差,但泡沫稳定性可达最大值（88.3±7.3）%,而当溶液的pH值偏离4时起泡能力增加,在pH10和12条件下起泡能力分别可达（73.3±0）%和（168.9±10.2）%,泡沫稳定性分别为（74.7±2.5）%和（68.5±2.1）%;另外在米糠蛋白溶液pH值为4和7条件下分别添加1%的NaCl后,可显著提高起泡能力至（77.8±3.8）%和（90.0±5.8）%。米糠蛋白泡沫的微观形态随时间变化规律说明,不同pH值条件下起始阶段气泡的直径大小分布与泡沫稳定性相关,而当添加NaCl后米糠蛋白起泡能力和泡沫稳定性的改变则与气泡数量和平均面积二者的综合效应有关。     

脱酚棉籽分离蛋白功能特性研究

为拓宽棉籽蛋白在食品领域应用范围,对棉籽分离蛋白基本功能性质进行分析,结果显示,本试验条件下所得棉籽分离蛋白(CPI)属酸溶性蛋白质,在酸性条件下(pH1～4)溶解性较好(30%～50%),在近中性溶液中溶解性较差,仅20%左右;乳化性受pH值、离子强度和CPI浓度影响不显著;乳化能力较低,但所得乳状液非常稳定;起泡性受pH值、离子强度和CPI浓度等因素影响很大,在中性pH下最高;添加NaCl对CPI溶液起泡能力影响不大,但会显著影响CPI溶液泡沫稳定性,随NaCl浓度增加,溶液泡沫稳定性急剧降低。粘度分析表明,CPI溶液属典型非牛顿流体,有"剪切变稀"和"热变稀"特征。     

马铃薯淀粉废水蛋白的功能特性

以碱提酸沉法制备的马铃薯淀粉废水蛋白为原料,分别考察了pH值、NaCl浓度和温度对蛋白功能特性（溶解性、持水能力、乳化性及乳化稳定性、起泡性及泡沫稳定性）的影响。结果表明,pH值、NaCl浓度和温度对蛋白的功能特性产生不同程度的影响。在等电点（pH 4.0）时,马铃薯蛋白表现出最低的溶解性、持水性、乳化性、乳化稳定性及起泡性,而泡沫稳定性最好。在较低NaCl浓度（＜0.2 mol/L）时,蛋白溶解性、持水能力、乳化性和乳化稳定性随NaCl浓度的增加而提高,而高浓度的NaCl（＞0.2 mol/L）对上述性质具有抑制作用;蛋白的起泡性和泡沫稳定性在NaCl浓度为0.4 mol/L时具有最大值。在4～80 ℃范围内,蛋白质的各项功能性质随温度的升高均呈现先增加后降低的趋势,且溶解性、持水性、乳化稳定性、起泡性及泡沫稳定性在40 ℃时最佳,乳化性在60 ℃最佳。     

茶多酚及其单体和加工环境对蛋清蛋白起泡性能影响的研究

本实验用电动打蛋机搅拌、直接测量的方法测定了茶多酚及其单体对蛋清蛋白质起泡能力和泡沫稳定性的影响,发现茶多酚添加量为0.2% 到0.4% 之间对蛋清蛋白质起泡性有显著的改善,并且发现主要单体EGCG 和ECG的活性羟基是茶多酚提高起泡性能的主要原因。同时也初步探讨了加工环境的改变(不同的NaCl 浓度、蔗糖浓度、pH 值等)对茶多酚- 蛋白质混合溶液相互作用的影响规律。     

茶多酚对胡麻粕蛋白表面性质的影响

采用碱溶酸沉法提取胡麻粕中的蛋白质并研究了茶多酚(TP)对此蛋白质表面性质的影响。结果表明:添加TP后胡麻粕蛋白的起泡性及泡沫稳定性有明显的提高,当TP添加量为0.08%,温度为30 ℃,pH为6的条件下起泡度和泡沫失水率分别为65.0%和51.5%,温度和pH值均对TP-胡麻粕蛋白体系的起泡性质有影响;添加TP后胡麻粕蛋白的乳化性质也有所提高,当TP添加量为0.04%,温度为40 ℃,pH值为6的条件下乳化性和乳化稳定性分别为44.5%和39.0%。     

不同因素对白果蛋白持油性、持水性和起泡性的影响

以白果蛋白为研究对象,研究温度对其持油性、持水性和pH值、NaCl、蔗糖对其起泡性的作用规律。结果表明:当温度达到40℃时,白果蛋白持油性达到最大值(3.32%),当温度达到45℃时,持水性达到最大值2.97%;当NaCl浓度为0～0.4mol/L时,白果蛋白的起泡能力和泡沫稳定性与NaCl浓度呈正相关,当NaCl浓度高于0.6mol/L时,过高的离子强度使白果蛋白的起泡能力和泡沫稳定性降低;蔗糖的加入将大幅度提高白果蛋白的泡沫稳定性,而对起泡能力提高幅度较小;pH值对白果蛋白的起泡能力和泡沫稳定性影响较大,当pH值为3～11时,起泡性较差,当pH值小于3时,起泡能力和泡沫稳定性与pH值呈负相关,当pH值大于11时,起泡能力和泡沫稳定性与pH值呈正相关,当pH值等于13时达到最高值。     

胡麻籽分离蛋白的溶解性与起泡性研究

为促进胡麻籽分离蛋白在食品工业中的应用,研究了pH值、盐浓度、蛋白质浓度等因素对其水溶性、起泡性和泡沫稳定性的影响。pH值对胡麻籽分离蛋白溶解度的影响呈典型的V形曲线。NaCl浓度为0.4mol/L前后胡麻籽分离蛋白表现出明显的盐溶与盐析效应。在0.1%～0.8%范围内,提高蛋白质浓度能增强起泡性与泡沫稳定性。在等电点附近,胡麻籽分离蛋白的起泡性最差但却具有最强的泡沫稳定性。NaCl对胡麻籽分离蛋白的起泡性的影响与其对溶解性的影响有相同的趋势。蔗糖能提高胡麻籽分离蛋白的泡沫稳定性,但当浓度高于5%时,对起泡性有负面影响。     

谷氨酰胺转氨酶介导的荞麦蛋白-花生蛋白交联及其功能特性研究

该文以谷氨酰胺转氨酶（TGase）为交联酶制剂,对荞麦蛋白与花生蛋白进行交联,通过单因素试验对两种蛋白的比例、总蛋白质浓度、TG酶添加量、交联温度、交联时间和pH进行了参数优化,并研究了最佳交联工艺条件下制备得到的交联产物的功能特性。结果表明,荞麦蛋白与花生蛋白的质量比1:1 (g:g)、总蛋白浓度4%、加酶量1.25%、反应温度40℃、反应时间120 min、pH 8.0时的交联反应效果最佳,交联度为63.1%。功能特性测定结果表明,与未交联的蛋白质相比,交联后的蛋白质的持水性、持油性和乳化稳定性有所提高,但乳化性、起泡性和起泡稳定性降低;在pH 3~12范围,交联蛋白质的溶解度逐渐升高,尤其在pI 4.0处,溶解度提高最为显著。     

绿豆分离蛋白功能特性研究

研究了绿豆分离蛋白的功能特性,探讨了pH值、温度、离子强度、蛋白质质量分数诸因素对绿豆分离蛋白溶解性、吸水性与吸油性、起泡性与起泡稳定性、乳化性与乳化稳定性、黏度的影响.结果表明,在pH=8的溶液中,绿豆分离蛋白的乳化性最好(45.2);在c(NaCl)=0.6 mol/L的溶液中,绿豆分离蛋白表现出较好的起泡性(160%);当w(绿豆分离蛋白)=9%时,起泡性和起泡稳定性最佳(分别为270%,77.8%～100%);当w(绿豆分离蛋白)=10%时,绿豆分离蛋白溶液的黏度可达7050 mPa·s.     

热处理辅助木瓜蛋白酶改善蛋清蛋白的起泡特性

为获得起泡特性优良的蛋清蛋白制品,试验以新鲜鸡蛋蛋清为原料,采用热处理辅助木瓜蛋白酶有限酶解的方法来改性蛋清蛋白,通过单因素实验,分析了底物浓度、酶的添加量、酶解时间、酶解温度、酶解pH等因素对起泡能力、泡沫稳定性的影响,并在单因素实验的基础上,以起泡能力和泡沫稳定性为响应值,通过响应面分析和方差分析得出热处理辅助木瓜蛋白酶改性蛋清蛋白的最佳工艺条件:底物质量分数3%、热处理温度90℃、热处理时间10 min、酶的添加量3 500 u/g、酶解时间2.5 h、酶解温度55℃、酶解pH 7。在此条件下,蛋清蛋白的起泡力为1741.38%,泡沫稳定性为93.38%。与未改性的蛋清蛋白相比,起泡力提高了112.97%,泡沫稳定性提高了93.27%。泡沫流变学特性结果表明改性蛋白的泡沫储存模量G′是未改性蛋白的1.5倍,泡沫更加稳定。     

Acid-thermal-induced formation of rice bran protein nano-particles: foaming properties and physicochemical characteristics

The purpose of this study was to expound on the correlation between foaming properties and physicochemical characteristics of rice bran protein (RBP) samples. RBP nano-particles (RBPNs) were prepared by acidic–thermal treatment under different RBP solution concentrations and treated times at 90 °C, and then the foaming properties were measured at pH 7.0 and pH 2.0. Compared to RBP, the foaming properties of RBPNs were increased at pH 7.0, and RBPNs could have better foam capacity but have no obvious changes in foam stability at pH 2.0. The results of Pearson correlation showed that the foaming properties were closely correlated with ζ potential, contact angle, and surface hydrophobicity for RBP and RBPNs, and a strong correlation between foaming capacity and surface hydrophobicity was shown for RBPNs. Additionally, the result of TEM images confirmed that RBPNs were inclined to form associated aggregates which may affect the physicochemical characteristics of RBPNs.     

Proteose Peptones and Physical Factors Affect Foaming Properties of Whey Protein Isolate

Effects of peptides and nonprotein components of whey on whey protein isolate (WPI) were studied using a differential pressure method. Decay of WPI foam followed biphasic first-order kinetics, but was affected by solution conditions. WPI foam stability exhibited two pH optima (5.0 and 8.5). Addition of 0.02–0.15M NaCl progressively decreased foaming capacity and foam stability. Addition of 0.01–0.2% proteose-peptones caused a sharp decrease in foam stability, but did not affect WPI foaming capacity. Foam stability was increased by addition of up to 20% lactose. Removal of proteose-peptones should greatly improve foaming properties of whey proteins.     

Functional Properties of Pork Liver Protein Fractions

The functional (emulsifying, gelling and foaming) properties of liver protein fractions as well as their molecular weight distribution and surface hydrophobicity were investigated and compared to commercial proteins. Two protein fractions were characterized: water soluble (WSLP) and WSLP combined with salt soluble liver proteins (W?+?SSLP). The effect of salt concentrations was also investigated (0, 1.8 and 3.4 % NaCl). Both WSLP and W?+?SSLP displayed good emulsifying properties and foam stability. However, their gelling properties were rather poor. An increase in salt concentration decreased the emulsifying properties of WSLP while the effect on W?+?SSLP was less pronounced. Addition of 1.8 % NaCl increased foaming ability of WSLP and W?+?SSLP while foam stability was not affected. Further increase of NaCl (3.4 %) decreased both foaming ability and foam stability and is probably attributed to refolding of the protein molecules because of the higher level of hydrophobic groups with 3.4 % NaCl. Gel forming ability of WSLP and W?+?SSLP containing 0 % was higher compared to high salt concentrations. However, higher salt concentrations shifted onset gelation temperature of WSLP and W?+?SSLP to lower temperatures probably due to partial unfolding of the proteins as indicated by an increase of the surface hydrophobicity.     

胶束化和碱溶酸沉提取羽扇豆蛋白的物化特性

利用胶束化和碱溶酸沉2 种提取方法从羽扇豆中提取羽扇豆蛋白,并对2 种方法提取羽扇豆蛋白的物化特性进行研究。结果表明：羽扇豆蛋白分子质量主要集中在18～90 kDa之间,是由多种分子质量的蛋白组成。碱溶酸沉提取羽扇豆蛋白的氨基酸总含量（66.2%）显著（P＜0.05）高于胶束化提取羽扇豆蛋白的氨基酸总含量（27.8%）。2 种提取方法提取羽扇豆蛋白的等电点pI接近5.0。胶束化提取羽扇豆蛋白的持水性显著（P＜0.05）高于碱溶液酸沉法提取的羽扇豆蛋白,而持油性无显著差异（P＞0.05）。碱溶酸沉法提取羽扇豆蛋白的起泡性在pH 2.0～6.0之间显著减小,在pH 6.0时起泡性最低,其泡沫稳定性的变化趋势与其起泡性类似。而胶束化提取羽扇豆蛋白的起泡性受pH值的影响不显著（P＞0.05）。胶束化提取的羽扇豆蛋白在pH 4.0时乳化性最小,然后随pH值的升高蛋白乳化活性也随之增加,2 种提取方法所提羽扇豆蛋白在pH 10.0时乳化活性最高。碱溶酸沉法提取的羽扇豆蛋白在pH 4.0时溶解度最小,而随着pH 4.0～10.0的增加,蛋白溶解度迅速增加。而胶束化提取羽扇豆蛋白的溶解度随pH 2.0～10.0的升高也逐渐增大。该研究为羽扇豆蛋白在食品工业中的开发与应用提供一定理论支持。     

羊肝蛋白稳定性及NaCl质量分数对其功能特性的影响

采用差式扫描量热法、激光粒径分布仪等仪器分析法研究了羊肝蛋白的稳定性,同时研究了NaCl质量分数(0.0%,1.8%,3.6%)对羊肝蛋白的乳化性与起泡性等功能特性及分子量分布和表面疏水性的影响。结果表明:随着NaCl质量分数的增加,水溶性羊肝蛋白(Water soluble liver proteins,WSLP)和盐溶性羊肝蛋白(Salt soluble liver proteins,SSLP)的表面疏水性也增加;SSLP的变性温度为87.9℃,高于WSLP的变性温度(74.4℃),表现出较好的热稳定性;WSLP的粒径分布较为集中,且电位绝对值小于SSLP;WSLP和SSLP均显示出良好的乳化性能和泡沫稳定性,NaCl质量分数的增加降低了WSLP的乳化性能,而对SSLP的乳化性能则没有明显影响。NaCl质量分数为1.8%时可提高WSLP和SSLP的起泡能力,而且不会影响其泡沫稳定性;而NaCl质量分数(3.6%)的进一步增加会降低起泡能力和泡沫稳定性。     

Combined effect of dynamic heat treatment and ionic strength on the properties of whey protein foams – Part II

The aim was to investigate the effect of dynamic thermal treatment in a tubular heat exchanger on the denaturation and foaming properties of whey proteins, such as overrun, foam stability and texture. A 2% w/v WPI solution (pH 7.0), with and without NaCl addition (100 mM), was submitted to heat treatment at 100 °C. The results demonstrated that heat treatment slightly reduced overrun, whereas NaCl and heat treatment improved foam stability, enhanced texture and provided smaller bubble diameters with more homogeneous bubble size distributions in foams. The foaming properties of proteins, especially stability, were shown to depend not only on the amount of protein aggregates, but also on their size. While insoluble aggregates (larger than 1 μm diameter) accelerated drainage, soluble aggregates (about 200 nm diameter) played a key role on the stabilization of gas–liquid interfaces.     

苦杏仁蛋白的功能特性

采用稀盐溶液浸提及等电点盐析相结合的方法提取制备苦杏仁蛋白,研究pH值、NaCl浓度、蛋白质量浓度和温度等因素对苦杏仁蛋白功能特性(溶解性、持水性、吸油性、乳化性及乳化稳定性、起泡性及起泡稳定性)的影响。结果表明：在等电点pI附近时,苦杏仁蛋白的溶解性、持水性、乳化性及乳化稳定性、起泡性最差;在较低NaCl浓度范围内(0～0.8mol/L)提高NaCl浓度可促进蛋白溶解性、乳化性及乳化稳定性、起泡性及起泡稳定性的提高,而较高的NaCl浓度对蛋白功能特性提高具有抑制作用;当蛋白质量浓度达到一定水平时(3～4g/100mL),蛋白功能特性(乳化性及乳化稳定性、起泡性及起泡稳定性)提高趋于平缓;在适宜的温度范围内,提高温度可有效提高苦杏仁蛋白各项功能特性,但当温度继续上升,各项功能特性持续降低。     

Impact of pH on the interactions between whey and egg white proteins as assessed by the foamability of their mixtures

The impact of protein–protein interactions on foaming properties of mixtures consisting of egg white proteins (EWP) and whey proteins (WP) with total protein content of 60 g/L was examined at pH 5, 7 and 9. The ratio between EWP and WP in the mixtures was varied between 67:33, 50:50 and 33:67 (in %; w/w). The ionic strength was adjusted to that of milk (I = 176 mM). The foamability of the protein products was characterized by the foam capacity, stability and firmness. In addition, the hydrophobicity in the protein solutions was assessed as a measure for the physical behaviour and ability of proteins to adsorb at the air–water interface.The individual egg white proteins and whey proteins each showed the best foaming properties at pH 5 and pH 9, respectively. At pH 9 a synergism was observed in the capacity and stability of the foams from EWP/WP-mixtures. This effect appears to be caused by the electrostatic interactions between egg white and whey proteins which occur in the bulk solution after the pH adjustment prior to the foaming. In contrast, at pH 5 no positive influence of foaming the components in a mixture as well as no indication of intermolecular interactions was found. At pH value near the pI of ovalbumin the protein interactions occur when the proteins have adsorbed at the air–water interface. The protein systems foamed at pH 7 showed intermediate foamability compared to the values obtained at alkaline and acidic pH.     

Surface functional properties of blood plasma protein fractions

The solubility, foaming and emulsifying properties of porcine blood plasma and its main protein fractions (serum, globulins and albumin) were investigated at pH 4.5, 6.0 and 7.5 in order to clarify the contribution of each fraction and encourage the optimisation of plasma-derived products. Soluble protein contents above 85% were obtained in all samples. Plasma, serum and albumin showed good foaming capacities, reasonably similar at different pH conditions, although the highest foam stability corresponded to both albumin and plasma at pH 4.5 and 6.0. All protein fractions showed good emulsifying activities, but the stability of the formed emulsions decreased with acidification, being emulsions of albumin and globulins at pH 7.5 the most stable ones. In addition, the interaction indexes calculated to investigate protein–protein interactions revealed synergistic interactions between albumin and globulins when in co-occurrence in their foaming capacity at pH 6.0 and 7.5, and in the stability of emulsions at pH 4.5 and 6.0, but slightly negative effects in the solubility of the mixture, and a great decrease in the stability of emulsions at pH 7.5. On the other hand, the elimination of fibrinogen improved the stability of emulsions and foams at acidic conditions.