电渗析脱盐对咸鸭蛋蛋清理化性质的影响

目的：为评估电渗析脱盐是否对鸭蛋清的功能性质和营养性有影响,研究经电渗析脱盐后鸭蛋清的部分理化性质变化。结果：脱盐后鸭蛋清的凝胶硬度在蛋白质量浓度较低时(5～8g/100mL)与鲜鸭蛋清相比无显著差异;当蛋白质量浓度为3～9g/100mL时,脱盐鸭蛋清的乳化活性及起泡性较咸鸭蛋清均有所提高,与鲜鸭蛋清相比,两者乳化活性相当,但其起泡性优于鲜鸭蛋清;SDS-PAGE、DSC及氨基酸分析表明,咸鸭蛋清脱盐前后蛋白质相对分子质量无明显变化;脱盐后的鸭蛋清与鲜鸭蛋清的氨基酸组成、热变性温度及颜色均十分接近。结论：经电渗析脱盐处理,鸭蛋清的理化性质影响不大,可作为良好的食品原辅料。     

Production and characterisation of duck albumen hydrolysate using enzymatic process

Influences of different ultrasound treatments combined with heat pretreatment on enzymatic hydrolysis, emulsifying properties and antioxidant activities of hydrolysates from duck egg albumen were studied. Heat pretreatment at 95 °C for 30 min inhibited both serine and cysteine protease inhibitors effectively. Ultrasonication of heated duck albumen at 60% amplitude for 10 min yielded the highest surface hydrophobicity. Coincidentally, aforementioned pretreatment rendered the hydrolysate with highest degree of hydrolysis (DH) than other pretreatments when Alcalase was used. The resulting hydrolysate showed the highest antioxidant activities including DPPH radical and ABTS radical cation scavenging activities and ferric reducing antioxidant power as well as emulsifying properties when hydrolysis time of 90 min was used. The hydrolysate possessed the peptides with molecular weight of 219–255 Da with the highest ABTS radical scavenging activity. Thus, heat pretreatment, followed by ultrasonication of duck albumen under appropriate condition could increase DH, antioxidant activities and emulsifying properties of duck albumen hydrolysate.     

FUNCTIONAL PROPERTIES OF HIGH HYDROSTATIC PRESSURE-TREATED WHEY PROTEIN

Surface hydrophobicity, solubility, gelation and emulsifying properties of high hydrostatic pressure (HHP)‐treated whey protein were evaluated. HHP treatment of whey protein buffer or salt solutions were performed at 690 MPa and initial ambient temperature for 5, 10, 20 or 30 min. Untreated whey protein was used as a control. The surface hydrophobicity of whey protein in 0.1 M phosphate buffers treated at pH 7.0 increased with an increase in HHP treatment time from 10 to 30 min. HHP treatments of whey protein in salt solutions at pH 7.0 for 5, 10, 20 or 30 min decreased the solubility of whey proteins. A significant correlation was observed between the surface hydrophobicity and solubility of untreated and HHP‐treated whey protein with r = ?0.946. Hardness of HHP‐induced 20, 25 or 30% whey protein gels increased with an increase in HHP treatment time from 5 to 30 min. An increase in the hardness of whey protein gels was observed as whey protein concentration increased. Whey proteins treated in phosphate buffer at pH 5.8 and 690 MPa for 5 min exhibited increased emulsifying activity. Whey proteins treated in phosphate buffer at pH 7.0 and 690 MPa for 10, 20 or 30 min exhibited decreased emulsifying activity. HHP‐treated whey proteins in phosphate buffer at pH 5.8 or 7.0 contributed to an increase in emulsion stability of model oil‐in‐water emulsions. This study demonstrates that HHP treatment of whey protein in phosphate buffer or salt solutions leads to whey protein unfolding observed as increased surface hydrophobicity. Whey proteins treated in phosphate buffers at pH 5.8 and 690 MPa for 5 min may potentially be used to enhance emulsion stability in foods such as salad dressings, sausage and processed cheese.     

Solubility, Hydrophobicity and Net Charge of Succinylated Canola Protein Isolate

Effects of succinylation (54% and 84% modification of free amino groups), pH (3.5–11.0) and NaCl concentration (0.0–0.7M) on solubility, hydrophobicity and zeta potential (net charge) of canola protein isolate were examined. Succinylation markedly enhanced protein solubility at alkaline and slightly acidic pH while effect of NaCl depended on pH. Surface hydrophobicity (S₀) decreased as level of succinylation increased. Effect of NaCl varied with pH but in general, S₀ decreased in a curvilinear manner as pH increased. Zeta potential became more electronegative as both succinylation and pH increased, but decreased with addition of NaCl. Hydrophobicity and zeta potential were closely related in a nonlinear inverse manner demonstrating that ionic environment had opposing influences on number of hydrophobic and charged groups on the surface of protein molecules in solution.     

磷酸盐对巴氏杀菌全蛋液理化及功能性质的影响

为保护并改善巴氏杀菌全蛋液的功能特性,探究在巴氏杀菌条件下添加不同类型磷酸盐（磷酸氢二钠、焦磷酸钠和六偏磷酸钠）对全蛋液理化功能特性的影响,包括pH值、表面疏水性、色度、游离巯基、溶解度、起泡特性、乳化特性和凝胶特性。结果表明：相比巴氏杀菌后的全蛋液,3 种磷酸盐会降低全蛋液的表面疏水性和游离巯基含量,相对较高浓度的磷酸氢二钠（10、20 mmol/L）和焦磷酸钠（9、12 mmol/L）能够显著提高全蛋液pH值。另外,3 种磷酸盐都能显著改善全蛋液的溶解度、起泡特性和乳化能力,且达到巴氏杀菌前水平。其中添加12 mmol/L焦磷酸钠改善效果较为突出,全蛋液乳化能力和起泡能力分别提高了19.74%和30.49%,并显著改善了全蛋液凝胶的持水性,但会使乳化稳定性降低41.41%。色度结果表明,添加3 种磷酸盐都会提高全蛋液的黄度和红度。综合来看,3 种磷酸盐都表现出了很大的应用潜力,研究结果将为巴氏杀菌全蛋液功能性质的稳态化提供理论依据。     

Effect of NaCl on thermal aggregation of egg white proteins from duck egg

Thermal aggregation of duck egg white solution (1 mg protein/ml, pH 7) was monitored in the presence of different NaCl concentrations (0–6%, w/w) across the temperature range of 20–90 °C. Duck egg white solution exhibited higher turbidity with coincidental increases in surface hydrophobicity and decreases in sulfhydryl group content as temperatures increased from 70 to 90 °C (p < 0.05). As NaCl concentration increased, the negative charge decreased, with coincidental increases in particle size of aggregate after heating to 90 °C. As visualised by confocal laser scanning microscopy, larger clusters of protein aggregates were observed with increasing NaCl concentrations. Major duck egg white protein with molecular mass of 45 kDa disappeared in the presence of 2–6% NaCl after heating above 80 °C, regardless of concentrations. Therefore, NaCl, especially at high concentrations, could induce thermal aggregation of duck egg white protein, which could determine the characteristics of salted egg white after heating.     

Influence of Enzymatic Hydrolysis on Structure and Emulsifying Properties of Sardine (Sardina pilchardus) Protein Hydrolysates

The influence of enzymatic modification with Alcalase was studied on surface hydrophobicity, molecular weight distribution and emulsifying properties of ten hydrolysates from sardine differing in degree of hydrolysis. Surface hydrophobicity was evaluated fluorometrically using 1 anilino-8-naphthalenesulfonate (ANS); molecular weight distribution was determined by gel chromatography on a Superfine Sephadex G50. Emulsifying capacity and stability were evaluated as functions of pH values and product concentration, in comparison with sodium caseinate. Results showed emulsifying properties, surface hydrophobicity and the high molecular weight fraction decreased as degree of hydrolysis increased. Thus production of hydrolysates with desired molecular structures and emulsifying properties is possible.     

Amino acid composition,foaming, emulsifying properties and surface hydrophobicity of mustard protein isolate as affected by pH and NaCl

Amino acid composition, protein hydrophobicity, foaming and emulsifying properties of mustard protein isolate at pH 3, 5, 7 and in 0.05 and 0.1 m NaCl were studied. Glutamic (19.18 ± 0.30%) and aspartic (7.49 ± 0.11%) acids were the dominants. Foaming ability was enhanced by NaCl. Time to reach 75 mL foam was 23% higher in water than in NaCl. Drained volume after 10 min was concentration dependent and was the lowest in 0.05 and 0.1 m NaCl at protein concentration of 2.5% and 5%. The emulsifying properties were pH and concentration dependent, and the best results were obtained at pH 3, corresponding to the highest positive charge density of the protein surface. The highest emulsion stability (90.22 ± 3.52%) was obtained in 0.05 m NaCl and 5% protein concentration, whereas the lowest (63.00 ± 1.06%) was in water at all protein concentrations. Protein hydrophobicity was low and depended of pH but not of NaCl.     

干燥方式对蛋清蛋白理化性质和功能特性的影响

为探究干燥方式对蛋清蛋白（egg white protein,EWP）功能特性的影响及其内在机理,分别通过喷雾干燥与真空冷冻干燥制备蛋清蛋白粉,并对其蛋白结构、理化性质与功能特性进行研究。结果表明,与蛋清液（EWP-C）相比,喷雾干燥使蛋清蛋白（EWP-P）的内源性荧光强度降低,表面疏水性和表面游离巯基含量增大。傅里叶变换红外光谱分析显示,EWP-P的α-螺旋、β-折叠和β-转角分别为16.30%、25.72%和40.23%,冷冻干燥蛋清蛋白（EWP-D）分别为20.43%、24.32%和35.69%。不同pH下,EWP-D的溶解度均高于EWP-P,表面张力小于EWP-P。此外,EWP-P的接触角为99.62°,高于EWP-D（接触角为65.97°）,表明喷雾干燥能显著提高蛋白的疏水性（P<0.05）。EWP-D在不同pH下的乳化性、乳化稳定性以及起泡性均大于EWP-P,但起泡稳定性更小,这与EWP-D较高的溶解性与较低的表明疏水性有关。荧光倒置显微镜及激光共聚焦扫描显微镜分析表明EWP-D乳液的微粒更小,分布更均匀,其稳定性高于EWP-P。综上,喷雾干燥蛋清蛋白的β-折叠结构较多,表面游离巯基含量和表面疏水性较高,具有较好的凝胶性;冷冻干燥蛋清蛋白的表面疏水性较小,且表面张力小、溶解度大,具有更好的乳化能力与起泡性。     

酶法制备不同水解度高温豆粕水解产物的理化特性研究

采用Alcalase酶和木瓜蛋白酶分别对高温大豆粕进行酶解,通过控制酶解反应得到水解度为5%、10%和15%的6种水解产物,研究两种酶对不同水解度的水解产物理化特性的影响。结果表明,Alcalase酶和木瓜蛋白酶均可产生6种不同分子量范围的水解产物,但各部分比例具有显著差异(P0.5),其平均分子量随水解度的增加逐渐减少,Alcalase酶的水解产物中小于2562 Da小分子量肽所占比例更高。豆粕蛋白的疏水基团在酶解反应中发生暴露与断裂的数量差,导致其表面疏水性随水解度增加呈现先下降再上升的变化,即水解度为10%的表面疏水性最低。zeta电势的绝对值随水解度不断上升,分子间的斥力增大,相同水解度下两种酶对zeta电势的影响并不显著。此外,在pH值为3、5、7和9时,水解产物的溶解性随着水解度的增加而逐渐增高,乳化活性和乳化稳定性则逐渐降低。     

大豆种子萌发后油脂体乳液稳定性的研究

以大豆为原料,大豆种子经萌发处理后的油脂体乳液为研究对象,通过测量乳化稳定性、过氧化值、硫代巴比妥酸值（TBARS值）及酸价等指标,比较了大豆种子不同萌发时间油脂体乳液的稳定性,研究了不同处理条件（NaCl浓度、pH、贮藏温度）对大豆种子萌发后油脂体乳液稳定性的影响。实验结果表明,大豆种子萌发后油脂体提取率逐渐降低,20 h（12.36%±0.21%）至27 h（10.89%±0.28%）油脂体提取率呈逐渐下降趋势,且27 h后提取率下降显著（P<0.05）。室温下贮藏14 d样品出现不同程度的絮凝。不同萌发时间油脂体乳液稳定性也不同,27 h表面疏水性（99.78±0.88）最大,且乳化稳定性（23.49±0.39）最好。经不同NaCl浓度、pH、贮藏温度处理后,随NaCl浓度的增加,萌发后的大豆油脂体乳液乳化活性无显著变化（P>0.05）,乳化稳定性在NaCl浓度为0~150 mmol/L时呈下降趋势,大于150 mmol/L时无显著变化,150与200 mmol/L时分别为（4.75±0.12）和（4.74±0.14）min,但过氧化值在贮藏0~6 d时显著增加（P<0.05）;pH越高,萌发大豆油脂体乳液的ζ-电势及乳化活性越小,pH为4时乳化活性为（19.13±0.23）m2/g,过氧化值和TBARS值变化显著（P<0.05）;贮藏温度上升,萌发大豆油脂体乳液过氧化值升高,酸价无显著性变化（P>0.05）。不同萌发时间大豆种子油脂体乳液稳定性均存在差异,且萌发27 h后的大豆油脂体较其他萌发时间更稳定。NaCl浓度和pH都对萌发大豆油脂体乳液稳定性有较大影响,且贮藏温度对其影响相对较小。可为今后萌发大豆油脂体的应用提供理论基础。     

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.     

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。     

Enzymatic Hydrolysis of Casein: Effect of Degree of Hydrolysis on Antigenicity and Physical Properties

Casein was enzymatically hydrolyzed for potential use in a hypoallergenic infant formula. Samples from the digest at different hydrolysis time (HT) intervals were tested for antigenicity, hydrophobicity, net charge (zeta potential), and emulsifying activity. Casein antigenicity loss could be approximated by three-phased first-order kinetics. Extensive antigenicity loss occurred during the first 10% of HT and relatively small changes occurred during the remaining 90% of HT. Hydrophobicity and emulsifying activity decreased, while the magnitude of the net charge increased (P <0.01) with increasing degree of hydrolysis. Strong correlations (r²≥ 0.89) were found among hydrophobicity, emulsifying activity and zeta potential.     

Modified Soy Proteins with Improved Foaming and Water Hydration Properties

Soy proteins were modified by alkali treatment at pH 10.0, followed by papain hydrolysis. Solubility, water hydration capacity (WHC), surface hydrophobicity, foaming and emulsifying properties of unmodified, alkali-treated, and papain-modified soy protein (PMSP) were compared. PMSP exhibited higher solubility (100% at pH > 7.0), WHC (3.13) and hydrophobicity (40.8) than unmodified soy protein which had solubility 68.5%, WHC 0.21, and hydrophobicity 8.1. The PMSP had foaming capacity (22.0 mL) similar to egg white (21.2 mL) at pH 7.0; and enhanced foam stability (36.4) compared to the unmodified control (32.9). In general, alkali-treated soy had lower functional properties. Emulsifying properties of PMSP and alkali treated soy were unchanged by the modification. PMSP could be used as an egg white substitute in foaming applications at neutral pH.     

不同水解度猪骨蛋白水解物对水包油型乳状液乳化特性的影响

摘 要：研究不同水解度的猪骨蛋白水解物（porcine bone protein hydrolysates,PBPH）对水包油乳状液的乳化特性的影响。采用碱性蛋白酶对猪骨蛋白进行水解0、1、2、3、4、5?h得到水解度分别为0%、5.6%、7.8%、11.1%、14.3%、17.2%的样品,分别测定PBPH的乳化活性、乳化稳定性、Zeta电位、乳状液微观结构的变化以及活性肽的分子质量分布。PBPH乳化性研究表明,随着水解度的增加,乳状液的乳化活性和乳化稳定性呈现先增加后降低的趋势（P＜0.05）,水解度为11.1%时的PBPH所形成的乳状液稳定性最高,这可能与其具有最高的表面疏水性、最高的Zeta电位、最小的体积平均粒径和最均匀的液滴分布有关。分子排阻色谱测定结果表明,随着水解度的增加,酶解产物的分子质量分布表现出大分子肽含量逐渐减少,小分子肽含量逐渐增多,水解过程中伴有多肽链的断裂和蛋白质的聚集,结构变化影响不同水解度的PBPH功能性质的变化,这进一步解释了乳化性变化的原因。由此可以得出,PBPH在水解时间为3?h?（水解度为11.1%）的适度水解的条件下,其乳化性最好,可以用于制备高物理稳定性的乳状液。     

花生湿热处理对其分离蛋白的结构和功能特性的影响

本文通过还原/非还原电泳、热差示扫描、表面疏水性及等电点测定等手段,表征了花生湿热处理对其分离蛋白结构和功能特性的影响.结果表明:在105℃随着湿热处理时间延长其分离蛋白中伴球蛋白所占比例逐渐减少,球蛋白在加热75min后产生热聚集,此外通过美拉德反应生成的糖蛋白含量逐渐增加,分离蛋白等电点向酸性偏移,表面疏水性先逐渐...     

介质极性对柔性玉米醇溶蛋白乳化性的影响

为了探究介质极性对柔性玉米醇溶蛋白乳化性的影响,本研究采用扫描电镜、动态光散射仪、圆二色谱仪等技术研究了不同介质环境下（60%、70%、80%、90%、92%（v/v）乙醇水溶液）玉米醇溶蛋白的聚集状态、粒径分布、表面疏水性、结构性质和不同聚合物乳化液的性质。结果显示介质极性影响了柔性玉米醇溶蛋白的聚集形态,聚合物颗粒大小与介质极性成反比。介质极性越高,形成聚合物的乳化活性越高,但乳化稳定性越低。当乙醇浓度从60%增加至92%时,乳化稳定性从67.97%增加至86.47%,液滴从355.60 nm降至251.00 nm,乳化液的电位从?40 mV降至?42.85 mV。此外,介质极性越低,玉米醇溶蛋白α-螺旋结构和表面疏水性越大,进而诱导其形成不同形态聚合物,从而表现出不同的乳化特性。本研究结果为拓宽玉米醇溶蛋白的应用范围提供理论基础。     

Functional properties of bovine blood plasma intended for use as a functional ingredient in human food

With the aim of using bovine blood as functional ingredient in food processing, as an emulsifier or fat replacer, a study of some functional properties of blood plasma was made. The effect of pH (3.0–8.0), tryptic hydrolysis and NaCl addition (0.034 mol/L) on the solubility, hydrophobicity and emulsifying properties of bovine blood plasma were studied. The results showed that the hydrophobicity and emulsifying activity index (EAI) of bovine blood plasma reached a maximum at pH 3.0 and 7.0, respectively, while the other parameters stayed nearly constant with pH change. Tryptic hydrolysis improved hydrophobicity at certain hydrolysis times, reduced solubility and emulsifying capacity (EC) and showed no effect on EAI and emulsion stability (ES). The influence of NaCl tested at pH 5.0 and 6.0 was only positive for plasma EAI at pH 5.0 and significantly reduced solubility, hydrophobicity and EC at pH 5.0 and 6.0. For ES, NaCl addition did not produce any modification.     

Emulsifying characterization of hens egg yolk proteins in oil-in-water emulsions

Emulsifying properties of egg yolk as a function of pH and oil volume were studied. Egg yolk proteins formed larger emulsion particles at pH 3 and the mean droplet size of the emulsions was decreased with increasing pH. A linear relationship between turbidity and mean droplet size of egg yolk emulsions could not be obtained. This may be due to the floculation of the emulsions. Egg yolk proteins formed thicker multilayers at low oil volume, however total protein adsorption ratio against original proteins was 55–65%, independent to protein and oil concentration. Electrophoretic analysis of the egg yolk emulsion revealed that the main components to adsorb at the interface was glanular lipovitellins, even though its emulsifying property was lower than that of plasma because of poor solubility at low ionic strength (0.1 M NaCl) at pH 7. These results indicate that the main contributor for egg yolk emulsion is granules and it can affect the emulsifying properties of egg yolk at different pH values.