不同聚合度菊粉对乳清蛋白基乳液结构和氧化稳定性的影响

该文探究了不同聚合度下不同浓度菊粉对乳清分离蛋白(whey isolate protein, WPI)乳化体系的结构稳定性和氧化稳定性机制。通过连续相Zeta电位、内源荧光光谱;Mastersizer 3000型激光粒度仪、激光共聚焦等设备对WPI乳液的平均粒径、乳化性质、界面蛋白吸附率、微观结构以及氧化稳定性等进行表征,研究不同质量分数(0%、2%、4%、6%、8%)的短链菊粉、中链菊粉对WPI乳液结构稳定性以及氧化稳定性的影响。实验结果表明,随着菊粉质量分数的增大,乳液的平均粒径呈上升趋势。界面吸附蛋白、乳化活性指数(emulsifying activity index, EAI)和乳剂稳定性指数(emulsion stability index, ESI)呈现减小的趋势。乳液初级氧化产物值、次级氧化产物呈现增大趋势,质量分数为2%中链菊粉乳液在15 d内表现出良好的氧化稳定性。低浓度菊粉(质量分数为2%)表现出最小的粒径以及更高的EAI和ESI,较单独使用WPI乳液增加了9.59%以及8.55%。     

乳清分离蛋白-南极磷虾油乳液理化稳定性和流变特性

比较分析不同质量分数（0%、1.5%、3%、6%）乳清分离蛋白（whey protein isolate,WPI）对水包油型南极磷虾油（Antarctic krill oil,AKO）(30%,m/m)乳液理化特性、物理稳定性、流变学特性和微观结构的影响。结果表明,不添加WPI的AKO乳液平均粒径和Zeta电位值分别为516.67 nm和-14.03 mV;随着WPI质量分数从0%增加到6%,乳液平均粒径显著降低了42.28%(P<0.05),而Zeta电位绝对值显著增加了18.05%(P<0.05),乳液物理稳定性明显提高。剪切流变学测试显示,随着WPI质量分数的增加,乳液表观黏度逐渐增大。微流变学测试显示,乳液体系中WPI引入使脂滴运动速率减慢、弹性行为增加,而流动性降低。微观结构观察发现,WPI添加能够使乳液网络结构趋于完整且均一,进而束缚更多脂滴以维持乳液体系稳定;WPI质量分数达到6%时,过多的蛋白会使乳液发生絮凝,进而削弱乳液体系稳定性。因此,适量WPI添加能够减小乳液粒径、增加脂滴电斥力、提高乳液黏弹性、增强蛋白网络结构束缚等,从而有效改善AKO乳液的稳定性。...     

热处理对金枪鱼蛋白乳液稳定性的影响

热处理是影响蛋白乳液稳定性的重要因素,本文研究了不同热处理温度（30、50、70、80、90℃,30 min）对金枪鱼蛋白乳液理化性能的影响。结果表明,与未进行热处理的样品相比,经过热处理的蛋白乳液乳化性能发生显著变化（P<0.05）。随着热处理温度的上升,金枪鱼蛋白乳液的表面疏水性、黏度、Zeta电位、乳化活性和乳化稳定性均呈现先增大再减小的趋势。加热温度在30～70℃范围内,蛋白二级结构展开,疏水性基团暴露,乳液黏度增大,液滴粒径减小,乳液稳定性增加;加热温度超过70℃后,蛋白分子重新聚集,与油滴结合的氨基酸残基重新进入蛋白质内部,液滴出现絮凝现象,乳液也变得不稳定。SDS-PAGE图谱显示70℃热处理30 min能够提升油-水界面蛋白质吸附量,液滴分布均匀,粒径达到最小值102.6 nm,黏度达到最大为43.87 Pa·s,贮藏28 d后没有出现乳析现象,乳液状态最稳定。综上,适当的热处理能提升金枪鱼蛋白乳液的稳定性。     

罗非鱼蛋白-乳清蛋白复合乳液负载β-胡萝卜素的研究

为了提高β-胡萝卜素的稳定性和生物利用率,充分利用双蛋白的营养和功能特性优势,以罗非鱼分离蛋白（tilapia protein isolate,TPI）和乳清分离蛋白（whey protein isolate,WPI）混合液作为乳化剂,通过高压均质结合热处理制备负载β-胡萝卜素的TPI-WPI复合乳液,探讨两种蛋白的质量比（2∶1、1∶1、1∶2）对乳液稳定性、抗氧化活性及体外消化特性的影响。结果表明,与单一的TPI和WPI乳液比较,TPI-WPI复合蛋白乳液的稳定性及β-胡萝卜素的生物利用率提高。当TPI与WPI质量比为1∶2时,复合蛋白乳液初始粒径为259.18 nm,zeta电位绝对值为28.23 mV,乳液的稳定性好,4℃贮藏21 d不分层;当TPI与WPI质量比为2∶1时,复合蛋白乳液贮藏21 d后β-胡萝卜素保留率达到62.36%,DPPH自由基和ABTS+自由基清除率分别为54.83%和40.11%,经体外消化后,β-胡萝卜素的生物利用率达24.76%,乳液游离脂肪酸释放率高。因此,WPI的添加可以提高复合蛋白乳液的稳定性,而TPI的添加可以提高乳液负载β-胡萝卜素的稳定性和生物利用率。研究结果可为混合蛋白构建稳定的乳液体系及活性成分的递送提供参考。     

乳清分离蛋白-葡聚糖接枝物Pickering乳液的稳定性研究

为提高蛋白基Pickering乳液稳定性,采用美拉德反应制备乳清分离蛋白(WPI)-葡聚糖(Dex)接枝物,然后利用该接枝物制得蛋白基固体颗粒,再与中链甘油三酯制备Pickering乳液,考察WPI-Dex接枝物对蛋白基固体颗粒乳化活性、乳化稳定性和蛋白基Pickering乳液乳析指数的影响,以及Pickering乳液在不同pH、加热温度、贮藏时间下粒径的变化。结果表明：扫描电镜观察到共价接枝Dex将WPI形貌结构由球状转变为片状,十二烷基硫酸钠-聚丙烯酰胺凝胶电泳证实干法美拉德反应成功制备了WPI-Dex接枝物;与WPI相比,WPI-Dex接枝物的乳化活性和乳化稳定性分别增加了57.8%和138.5%;WPI和WPI-Dex接枝物Pickering乳液贮藏30 d时的乳析指数分别为52.3%和36.0%,WPI-Dex接枝物使Pickering乳液的乳析稳定性提高了31.2%;WPI-Dex接枝物Pickering乳液具有良好的pH稳定性、热稳定性和贮藏稳定性。综上,蛋白质糖基化接枝修饰是提高天然蛋白质Pickering乳液稳定性的有效方法。     

自由基接枝改性对乳清分离蛋白乳化稳定性的影响

为研究蛋白的共价接枝改性对其乳化稳定性的影响,本文以乳清分离蛋白（whey protein isolate,WPI）和表没食子儿茶素没食子酸酯（epigallocatechingallate,EGCG）为原料,通过自由基接枝法制备WPI-EGCG复合物。利用扫描电镜（SEM）对其微观结构进行观测,通过测定界面蛋白吸附量、界面流变学特性来探究共价接枝对界面特性的影响;进而以WPI-EGCG接枝物为乳化剂构建番茄红素纳米乳液,并对其物理化学稳定性及储藏稳定性进行研究。结果表明,EGCG的自由基接枝改变了WPI的结构,使之具有更高的黏度和界面稳定性,使以接枝物为乳化剂的番茄红素纳米乳液体系具有更高的物化稳定性。WPI-EGCGE接枝物稳定的番茄红素纳米乳液在37 ℃下储藏30 d后粒径和ζ-电位绝对值分别增加了268.3 nm和17.6 mV,乳液中番茄红素的保留率仍有66.23%,呈现出更佳的番茄红素保护效果。本研究为功能活性物质纳米乳液载运体系的构建提供了参考。     

葡萄籽油/大米水解蛋白复合乳液工艺优化及稳定性研究

以葡萄籽油和大米水解蛋白为原料,制备水包油型乳液。选择大米水解蛋白质量分数、油相占比、pH值、高压均质时间、高压均质压力做单因素实验。在此基础上采用Box-Behnken试验设计,以乳液粒径及乳化稳定性为响应值做响应面分析试验,确定最优工艺参数是：大米水解蛋白质量分数2%,油相占比10%,pH 7,均质时间5 min,均质压力50 MPa,此时测定平均粒径为（0.894±0.013）μm,乳化稳定性为（18 157.7±137）min。在上述最优工艺条件下,制备葡萄籽油/大米水解蛋白复合乳液,分别于储藏1,7,15,30 d,考察乳液粒径、乳化指数、乳液微观结构的变化,并对乳液的储藏稳定性进行评估。结果表明,该乳液为水包油型,油相于水相中分散均匀,储藏30 d内乳液外观无明显变化,乳液粒径随储藏时间的增加略有增大,乳化指数逐渐下降,总体稳定性较好。     

预加热处理对甘薯蛋白乳化特性的影响

为探究预加热处理对甘薯蛋白乳化特性的影响,本研究以预加热处理(90℃)后的甘薯蛋白制备蛋白乳液,对蛋白乳化稳定性指数(ESI)、蛋白乳化活性指数(EAI)、乳液液滴粒径、Zeta电位和流变学特性进行测定。采用远紫外圆二色光谱法表征甘薯蛋白经预加热处理后的二级结构变化。随着预加热处理时间延长至10 min, ESI值提高约80%,Zeta电位绝对值增大约50%,EAI值降低约30%,乳液液滴粒径下降约20%;稳态流变学结果表明乳液表观黏度逐渐增大;动态流变学结果表明乳液结构强度逐步增强;远紫外圆二色光谱实验表明,预加热处理后甘薯蛋白的α-螺旋、β-折叠含量下降,而β-转角、无规则卷曲含量有所上升。研究结果表明,适度时间预加热处理(5～10 min, 90℃)能改善甘薯蛋白的乳化稳定性,但会弱化乳化活性,归因于甘薯蛋白结构的改变以及蛋白表面净电荷的改变,为预加热处理调控蛋白乳液特性提供参考。     

小麦醇溶蛋白/卵磷脂复合纳米粒子制备Pickering乳液研究

以小麦醇溶蛋白和卵磷脂为原料,利用pH循环法制备小麦醇溶蛋白/卵磷脂复合纳米粒子,并以此为稳定剂制备Pickering乳液。探究了纳米粒子质量分数、油相体积分数对Pickering乳液的粒径、微观形貌、乳析稳定性、储藏稳定性及流变学特性的影响。结果表明：制备的Pickering乳液为水包油型乳液。当小麦醇溶蛋白/卵磷脂质量比为2∶1时,Pickering乳液的乳化活性和乳化稳定性分别为9.33 m²/g和93.33%。固定油相体积分数为50%,当纳米粒子质量分数由0.1%增加到2.0%时,Pickering乳液的粒径由56.19μm减小到36.57μm,乳析指数由46.5%增加到91.0%;固定纳米粒子质量分数为1.5%,当油相体积分数由20%增加到60%时,Pickering乳液的粒径由31.43μm增大到38.79μm,乳析指数由54%增加到93%。流变学结果表明,乳液的表观黏度和弹性性能随着纳米粒子质量分数以及油相体积分数的增加而增加,且都具有剪切稀化的现象,形成了凝胶网络结构;环境应力稳定性实验表明,Pickering乳液具有良好的NaCl离子稳定性。     

花生蛋白肽对核桃乳贮藏稳定性的影响

以核桃乳质量为基准,添加0.1%、0.2%、0.3%的花生蛋白肽添加到核桃乳中,探索花生蛋白肽对核桃乳乳化稳定性以及氧化稳定性的影响,测定了核桃乳的脂肪上浮率、离心沉淀率、黏度、分层指数、粒径以及脂质氧化程度.结果表明:随着储藏时间的增加,核桃乳的稳定性下降,添加花生蛋白肽能够显著降低核桃乳的脂肪上浮率和离心沉淀率、增加核桃乳的黏度、减小核桃乳的粒径、改善分层现象.不同添加量的花生蛋白肽均能够显著地降低核桃乳的TBARS值,起到抑制脂肪氧化的作用.因此,花生蛋白肽可以显著改善核桃乳的乳化稳定性和氧化稳定性.     

Labile protein reserves and protein turnover.

The concept of a labile protein reserve is based on the relatively slow establishment of a new equilibrium in the rate of nitrogen excretion after an abrupt change in dietary supply. The evidence reviewed shows that a majority of this nitrogen is derived from or deposited in skeletal muscle proteins. The rates of synthesis and degradation of total body protein are rapid in large animals (man and swine) and are correlated with heat production. The rate of protein synthesis in skeletal muscle greatly exceeds the rate of growth and is sensitive to nutritional status. The rate exceeds the rate of degradation in response to the ingestion of an adequate diet so that tissue proteins are accumulated, but it decreases below the rate of degradation under conditions of deprivation. In this latter state, proteins of skeletal muscle supply amino acids for energy or for the synthesis of other more essential proteins, e.g., milk proteins during lactation. Thus, we conclude that the labile protein reserve is a product of the normal, dynamic metabolism of protein.     

Fermentation modifies protein/protein and protein/starch interactions in sorghum dough

A study was made on the molecular and structural changes occurring in the protein and starch components of sorghum flour when fermented to prepare typical non-malted Sudanese foods. Protein solubility and SDS-PAGE studies indicated that water-soluble proteins are the main target of hydrolysis during fermentation. Proteolysis products are taken up for bacterial growth. Kafirins are among the proteins left intact by proteolytic events in the fermentation step. Upon cooking in boiling water kafirins are converted into protein aggregates almost insoluble even in the presence of 8 M urea and of disulphide-reducing agents. Viscoamylographic and microstructural studies indicate that fermentation leads to the release of starch granules from very compact structures in the original sorghum flour, in which proteolysis-sensitive, water-soluble proteins form an essential part of the outermost shell of large structures, where starch granules are embedded into a kafirin-rich protein matrix that is not affected by proteolytic events during fermentation.     

肌原纤维蛋白双蛋白乳饮料的研制

介绍了肌原纤维蛋白双蛋白乳饮料生产所需的材料、设备、工艺流程、操作要点、质量指标,确定了产品所需肌原纤维蛋白的种类、甜味剂的种类、乳化稳定剂的添加量,通过正交试验和极差分析得出肌原纤维蛋白双蛋白乳饮料的较优配方为:全脂乳粉3.5%、肌原纤维蛋白0.3%、复合甜味剂(以蔗糖计)9%、酸含量(以柠檬酸计)0.4%、复合乳化稳定剂0.40%、柠檬酸钠0.1%、食用香精0.03%。     

Perspectives of lupine wholemeal protein and protein isolates biodegradation

Lupine (Lupinus angustifolius L.) protein (in wholemeal and protein isolates) was biodegraded using Pediococcus acidilactici in submerged and solid-state fermentation conditions. The changes in the molecular weight of lupine protein fractions, amino acid (AA) profile, biogenic amine formation, antimicrobial and antioxidant properties, and protein digestibility in vitro and in vivo (in Wistar rats) were evaluated. After biotreatment, lower molecular weight peptides (from 10 to 20 kDa) were established, and the free AA content increased. Biodegradation improved the antioxidant properties, modulated the antimicrobial properties, and led to higher in vitro and in vivo digestibility and functionality of the lupine in treated rats (significant increase in body weight of Wistar rats, and increased acetic acid concentration and lowered Escherichia coli count in the caecum). Overall, the biodegradation of lupine protein can transform the plant protein, producing enhanced functionality and bioavailable products.     

Oil globule microstructure of protein/polysaccharide or protein/protein bilayer emulsions at various pH

The microstructure of oil droplets of bi-layer emulsions was studied as a function of pH (i.e. 7, 5, and 3) using scanning electron microscopy. The bi-layer emulsions consisted of a primary emulsion: 5 wt% soybean oil (SBO) in a 1% protein (nonfat dry milk) aqueous solution. The secondary layer was ι-carrageenan, high- (HMp), low (LMp)-methoxyl pectin, or gelatin. The secondary emulsions consisted of 2.5% SBO, 0.5% protein, and 0.2% polysaccharide or protein. Gelatin secondary emulsions were stable at pH 7 with defined droplets and became unstable at pH 5 and 3. The destabilization mechanisms for these emulsions at pH 5 and 3 were different as observed with the SEM: at pH 5 there is complete aggregation of protein due to their proximity to the isoelectric point; and at pH 3 the droplets are perfectly separated, suggesting that at this pH, when the net charge is positive, the destabilization is mainly due to depletion flocculation. HMp secondary emulsions shift from being stable (individual droplets) at pH 3 to being unstable at pH 7 where an extensive webbing is observed between the droplets at this pH value. The ι-carrageenan secondary emulsions are stable at each pH and the individual droplet microstructure is minimally altered as the pH changes. LMp secondary emulsions shift from being stable at pH 7 with individual droplets observed in the SEM micrographs to being unstable at pH 3 where extensive webbing is observed in the SEM micrographs.     

Nutritive value of a new protein product--dry protein mixture

A dry protein mixture (DPM) consists of dry slaughtered animal blood clarified by means of the peroxide-catalase system and dry skim milk at a ratio of 1:1. A study was made of organoleptic properties of the DPM, the composition of nutrients and biological efficacy in experiments on animals. The DPM is light yellow powder without specific taste and odor of blood, contains 58.4% of protein, 1.36% of fat, 26.71% of carbohydrates (lactose), and 8.19% of mineral substances. DPM proteins contain all the essential amino acids. As regards their biological efficacy they are not inferior to that of casein. The DPM is rich in calcium (606 mg/100 ml), phosphorus (645 mg/100 ml) and particularly in iron (106 mg/100 ml). Digestibility of iron examined on rats appeared to be high (31.2%). The new product is recommended for rational and dietetic nutrition.     

富锌豆蛋白中锌结合态含量的研究

富锌豆蛋白是一种用特殊科学方法得到的高含量锌添加剂。本文利用植物生化分离和分析方法,研究了富锌豆蛋白中锌与不同蛋白结合状态下的含量。分析结果显示,游离锌为150.7μg/g,结合于蛋白中的锌为1055.0μg/g。可以认为锌主要以有机蛋白锌的形式存在。     

Solubility of commercial milk protein concentrates and milk protein isolates

High-protein milk protein concentrate (MPC) and milk protein isolate (MPI) powders may have lower solubility than low-protein MPC powders, but information is limited on MPC solubility. Our objectives in this study were to (1) characterize the solubility of commercially available powder types with differing protein contents such as MPC40, MPC80, and MPI obtained from various manufacturers (sources), and (2) determine if such differences could be associated with differences in mineral, protein composition, and conformational changes of the powders. To examine possible predictors of solubility as measured by percent suspension stability (%SS), mineral analysis, Fourier transform infrared (FTIR) spectroscopy, and quantitative protein analysis by HPLC was performed. After accounting for overall differences between powder types, %SS was found to be strongly associated with the calcium, magnesium, phosphorus, and sodium content of the powders. The FTIR score plots were in agreement with %SS results. A principal component analysis of FTIR spectra clustered the highly soluble MPC40 separately from the rest of samples. Furthermore, 2 highly soluble MPI samples were clustered separately from the rest of the MPC80 and MPI samples. We found that the 900 to 1,200 cm⁻¹ region exhibited the highest discriminating power, with dominant bands at 1,173 and 968 cm⁻¹, associated with phosphate vibrations. The 2 highly soluble MPI powders were observed to have lower κ-casein and α-_S1-casein contents and slightly higher whey protein contents than the other powders. The differences in the solubility of MPC and MPI were associated with a difference in mineral composition, which may be attributed to differences in processing conditions. Additional studies on the role of minerals composition on MPC80 solubility are warranted. Such a study would provide a greater understanding of factors associated with differences in solubility and can provide insight on methods to improve solubility of high-protein milk protein concentrates.     

一种再生蛋白纤维--大豆蛋白纤维

主要介绍了大豆蛋白纤维的发展概况、生产工艺与设备、产品及其织物特点,从而为大豆纤维在纺织工业的应用提供技术和理论指导,同时也为纺织产品的创新开辟新的途径.