复合米糠蛋白-卵白蛋白的起泡特性及相关机理分析

考察复合米糠蛋白（rice bran protein,RBP）-卵白蛋白（ovalbumin,OVA）的起泡特性,并分析在特定pH值与NaCl浓度下溶液与泡沫中不同蛋白质的物化性质,以阐述两种蛋白之间相互作用对起泡特性的影响。结果表明,在pH 4.0条件下,两种蛋白质在起泡能力上可以产生协同作用,且当RBP-OVA质量比为3:1时,添加1% NaCl后RBP-OVA复合蛋白的起泡能力和泡沫稳定性均显著增加;而在pH 7.0、无NaCl的情况下两种蛋白在起泡特性上没有表现出特别明显的协同作用,当添加1% NaCl后二者在起泡能力方面反而表现出一定的拮抗作用。通过对pH 4.0、1% NaCl条件下溶液与泡沫中蛋白质的物化性质进行分析可知,因两种蛋白质在物化性质方面具有一定的互补性,可通过蛋白质之间的相互作用从不同的物化性质角度改善RBP-OVA复合蛋白的起泡能力与泡沫稳定性。     

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。     

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。     

pH值碱性偏移结合热处理对米糠蛋白结构和功能性质的影响

研究pH值碱性偏移（pH 11）结合热处理（50、60 ℃）对米糠蛋白结构和功能性质的影响。结果表明,pH值碱性偏移促使米糠蛋白二级结构由有序向无序转化,pH值碱性偏移结合热处理使得米糠蛋白二级结构呈现折叠-去折叠-复折叠的复杂变化,并伴随巯基氧化。pH值碱性偏移促使米糠蛋白展开,随着处理时间的延长,米糠蛋白重新聚集,热处理会加剧聚集程度。pH值碱性偏移使得米糠蛋白持水性、起泡性、泡沫稳定性、乳化性和乳化稳定性显著下降,仅持油性显著改善;随着处理时间的延长,米糠蛋白持水性、起泡性、乳化性和乳化稳定性逐渐上升,其中乳化性上升幅度最大。pH值碱性偏移结合热处理可显著改善米糠蛋白的持水性、起泡性、泡沫稳定性和乳化稳定性,同时也会降低米糠蛋白的持油性和乳化性。     

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%。     

酱油沉淀控制酶解制备高起泡蛋白的研究

研究了pH值、蛋白浓度、水解度对酱油沉淀蛋白控制酶解制备起泡蛋白的影响,并探讨了黄原胶的添加对酱油沉淀蛋白泡沫性质的改善效果。结果表明:酱油沉淀蛋白的起泡性随着pH值的升高而提高,但沉淀蛋白水解物的起泡性呈现相反的变化趋势,其在pH 5时起泡性和泡沫稳定性最佳,酶解3h水解物的起泡性和泡沫稳定性分别达到59.00%和43.55%;当黄原胶添加量为0.05%～0.1%时,能显著提高沉淀蛋白水解物的泡沫稳定性,但添加量过大会影响起泡性。在pH 5时,添加0.05%的黄原胶,3h水解物的起泡性和泡沫稳定性可达到54.00%和81.81%。以粘度、表面疏水性、ζ-电位为指标探讨了影响酱油沉淀蛋白泡沫性质的机理,蛋白泡沫性质的呈现与它们的综合效应有关。     

响应曲面法优化木瓜蛋白酶改善蛋清蛋白起泡性能工艺

优化木瓜蛋白酶改善蛋清蛋白起泡性能的工艺。在单因素试验基础上,确定自变量酶解时间、木瓜蛋白酶添加量、酶解温度、pH值的试验水平,以起泡性和泡沫稳定性为响应值,采用Box-Behnken试验设计方法,研究各自变量及其交互作用对蛋清蛋白起泡性和泡沫稳定性的影响。然后利用Design Expert软件进行响应面分析,模拟得到二次多项式回归方程的预测模型,并确定蛋清蛋白酶改性的最佳条件组合。结果表明：蛋清蛋白泡沫稳定性酶解模型不显著,而起泡性酶解模型显著,在最佳工艺参数酶解时间45min、酶添加量38.2mg/5mL蛋清、酶解温度47.5℃、pH6.3的条件下,蛋白起泡性可达2.09,此条件下可使蛋清蛋白起泡性提高140%左右。     

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。     

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.     

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.     

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。     

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.     

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.     

提取方法对银杏蛋白功能特性及抗氧化活性的影响

研究水提酸沉法（water extraction and acid precipitation, WEAP）、碱提酸沉法（alkali extraction and acid precipitation, AEAP）和超声辅助碱提酸沉法（ultrasound-assisted alkali extraction and acid precipitation, UA-AEAP）三种方法对银杏蛋白功能特性和抗氧化活性的影响。以溶解度、起泡性、起泡稳定性、乳化性和乳化稳定性为指标,考察不同提取方法对银杏蛋白功能特性的影响;以亚铁离子螯合能力、1,1-二苯基-2-三硝基苯肼（1,1-diphenyl-2-picrylhydrazyl, DPPH）自由基清除能力和羟基自由基清除能力为指标,评价不同提取方法对银杏蛋白抗氧化活性的影响。结果表明,不同提取方法对银杏蛋白得率和溶解度的影响较大,其中UA-AEAP蛋白得率最高,达11.36%±0.10%;在pH2~12范围内,UA-AEAP银杏蛋白的溶解度最高;提取方法显著影响了银杏蛋白的起泡性、泡沫稳定性和乳化性等功能特性（P<0.05）,UA-AEAP蛋白的起泡性、泡沫稳定性和乳化性均优于AEAP和WEAP蛋白,而对乳化稳定性无显著性影响（P>0.05）;提取方法还影响了银杏蛋白的抗氧化活性,银杏蛋白的螯合亚铁离子能力、清除DPPH自由基能力和清除羟基自由基能力的顺序均为:UA-AEAP>WEAP>AEAP。UA-AEAP蛋白得率高、抗氧化能力和功能特性优于另外两种方法,适用于银杏蛋白的制备。     

Solubility and functional properties of sesame seed proteins as influenced by pH and/or salt concentration

The protein content, solubility and functional properties of a total protein isolate prepared from sesame seeds (Kenana 1 cultivar) as a function of pH and/or NaCl concentration were investigated. The protein content of the seed was found to be 47.70%. The minimum protein solubility was at pH 5 and the maximum was at pH 3. The emulsifying capacity, activity and emulsion stability as well as foaming capacity and foam stability were greatly affected by pH levels and salt concentrations. Lower values were observed at acidic pH and high salt concentration. The protein isolate was highly viscous and dispersable at pH 9 with water holding capacity of 2.10 ml H₂O/g protein, oil holding capacity of 1.50 ml oil/g protein and bulk density of 0.71 gm/ml.     

Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration

The content, fractionation, solubility and functional properties of wheat bran proteins as well as the effects of pH and/or NaCl concentration on some of these functional properties were investigated. The protein content of the bran was found to be 16.80%. Albumin and glutelin are the major fractions of wheat bran proteins. The minimal protein solubility was observed at pH 5.5, the maximum at pH 11.5. The emulsifying capacity, activity and emulsion stability as well as foaming capacity and foam stability were greatly affected by pH and salt concentrations. Lower values were observed at acidic pH and high salt concentration. The least gelation concentration of wheat bran proteins was found to be 16% when the proteins were dissolved in 1.0 M NaCl. The total protein was highly viscous and dispersable with water-holding capacity of 4.20 mL H2O/g protein, oil-holding capacity of 1.70 mL oil/g protein and bulk density of 0.29 g/mL while dispensability was found to be 77.30%.