不同大麦籽粒品质及发芽后蛋白质含量和主要水解酶活力变化的研究

研究了12种国内外大麦籽粒的外观和基本理化品质,检测其发芽前后清蛋白、球蛋白、醇溶蛋白和谷蛋白4种蛋白质亚组分的含量及主要水解酶活力的变化,探讨了部分蛋白亚组分与总蛋白、酶与蛋白及酶与酶之间的相关性.结果表明:1号和3号大麦籽粒品质较好,具有开发啤酒大麦的潜力;发芽后大麦总蛋白含量基本不变,清蛋白大幅增加,球蛋白略降低,贮存蛋白(醇溶蛋白与谷蛋白)总体降低.相关性分析表明:大麦和麦芽中贮存蛋白的含量反映了其总蛋白的含量;α-淀粉酶与清蛋白呈负相关性,蛋白酶与清蛋白呈正相关性,β-淀粉酶与总蛋白、蛋白亚组分及蛋白酶之间存在显著正相关性.     

挤压处理对薏米蛋白组分结构及功能性质的影响

以脱脂薏米粉为原料进行挤压,采用Osborne分级法提取清蛋白、球蛋白、醇溶蛋白与谷蛋白,探讨挤压处理对4种蛋白组分结构与功能性质的影响。结果表明,挤压后4种蛋白组分的粒径均呈下降趋势（低至3 nm）。挤压导致清蛋白、球蛋白与谷蛋白发生不同程度的聚集融合,游离巯基含量分别降低了72.37%,40.64%和51.71%,蛋白的最大荧光吸收波长蓝移,电泳图谱中高分子质量区域分布的条带逐渐消失,亚基种类减少,而醇溶蛋白无明显变化。除球蛋白外,挤压后清蛋白、醇溶蛋白与谷蛋白中有序结构,即α-螺旋与β-折叠结构的含量明显下降（P <0.05）,分别减小了1.58%,22.88%和7.75%。此外,挤压后清蛋白、球蛋白与谷蛋白的持水性分别提高了1.74,3.18倍和4.89倍,持油性分别增长了2.00,2.23倍和1.67倍。结论：挤压处理诱导清蛋白、球蛋白与谷蛋白的结构性质发生明显改变,而醇溶蛋白具有较高的结构稳定性与抗热剪切能力。研究结果为薏米蛋白组分的工业化制备及在多种食品配方中的应用提供参考。     

甜荞蛋白质组分的物化特性研究

研究甜荞不同蛋白组分的物化特性.采用分步提取法分离收集甜荞清蛋白、球蛋白、醇溶蛋白和谷蛋白.结果表明甜荞清蛋白、球蛋白、醇溶蛋白和谷蛋白的含量分别占总蛋白的21.91%、19.36%、2.26%和19.95%,等电点分别为pH4.40、5.00、4.80和4.60,变性温度分别为79.39℃、70.36℃、80.04℃和83.09℃,前三种蛋白白色略偏黄,而谷蛋白偏红色.甜荞清蛋白、球蛋白和谷蛋白的必需氨基酸含量丰富.甜荞清蛋白含铁量高,醇溶蛋白含锌量高,球蛋白含镁量高,而铅、锡、砷在各蛋白质组分中的含量均很低.     

萌发大麦种子蛋白组分含量变化研究

采用蛋白质组分连续累进提取分析法，检测了垦啤8号、甘啤4号、Harrington、Es．terel四个品种大麦种子萌发前后各蛋白组分的含量变化。结果表明：大麦种子中清蛋白含量较低，占总蛋白含量的3％～5％，种子萌发后，清蛋白含量迅速升高，发芽第四天达到最大值，含量占10％左右，绿麦芽焙焦后，含量略有下降；球蛋白含量变化较为复杂，在种子发芽2天后达到最大值，由3％升至6％左右；醇溶蛋白在种子萌发过程中明显减少，Esterel品种变化最大，减少了总蛋白质的7．14％，其它三个品种减少了4到6个百分点；谷蛋白含量在萌发过程中略呈升高趋势，但变化不大。     

萌发荞麦种子蛋白质组分含量变化的研究

研究了荞麦种子萌发后总蛋白质和各蛋白组分如清蛋白、球蛋白、醇溶蛋白和谷蛋白的含量变化，结果表明：本试验条件下，山西甜荞和四川苦荞萌发后总蛋白质含量呈逐渐下降趋势。山西甜荞经过72h的萌发，其蛋白质总量由最初的11．90％下降到5．44％，下降了6．5个百分点。四川苦荞由萌发初的6．53％下降到0．96％，下降了5．6个百分点。荞麦清蛋白和球蛋白在萌发后均呈现下降趋势，与总蛋白质含量变化相一致。谷蛋白在萌发后至36h内含量下降，之后又快速增加。四川苦荞醇溶蛋白含量在萌发后逐渐增加．而山西甜荞则有逐渐下降趋势。     

不同花生品种籽仁发育过程中蛋白质组分分析

采用蛋白质组分的连续累进提取法提取4个花生品种籽仁的清蛋白、球蛋白、醇溶蛋白和谷蛋白。利用聚丙烯酰胺凝胶电泳(SDS-PAGE)技术,对各蛋白组分的亚基组成进行分析。结果表明,花生籽仁发育过程中,清蛋白始终占绝对优势,占花生蛋白质总量的70%以上,最高达95%;球蛋白含量较低,仅占花生蛋白质总量的3%~5%,谷蛋白含量最低,其不足3%,醇溶蛋白痕量;在4种组分中,品种之间球蛋白含量差异最大。SDS-PAGE图谱显示,染色后清蛋白、球蛋白条带清晰可见,谷蛋白条带较为模糊,清蛋白含量高,清蛋白和球蛋白成分较丰富。花生蛋白亚基分子质量在14.4~97.4 ku之间,清蛋白有10~12个亚基,球蛋白有9~10个亚基。采用连续累进提取法可将花生蛋白组分分离,利用SDS-PAGE方法可以得到花生籽仁清蛋白、球蛋白的清晰条带且多态性高,而谷蛋白条带模糊。     

脱除不同溶解性内源蛋白质对早籼米粉理化性质的影响

为通过利用内源蛋白质调控早籼米粉理化性质提高其制品品质，本文研究脱除不同溶解性内源蛋白质（清蛋白、球蛋白、醇溶蛋白和谷蛋白）对早籼米粉溶解度、膨胀度、成糊特性及其糊化后水分结合状态、流变学特性和冻融稳定性的影响。结果表明，脱除球蛋白和谷蛋白可提高早籼米粉的溶解度，而脱除醇溶蛋白和谷蛋白均可在高温下提高其膨胀度。脱除清蛋白使早籼米粉成糊的峰值粘度、终值粘度、崩解值和回生值分别降低16%、21%、50%和43%；脱除球蛋白可提高其糊化温度并降低其峰值粘度，脱除醇溶蛋白则相反；脱除谷蛋白使其峰值粘度和终值粘度分别降低22%和12%，并使其崩解值和回生值分别提高49%和53%。脱除谷蛋白使早籼米粉糊化后的弱结合水含量降低14%；脱除球蛋白和谷蛋白均可提高其糊化后与水结合的强度，脱除醇溶蛋白则相反。脱除醇溶蛋白使早籼米粉糊化后的似固状态增强20%；脱除球蛋白和谷蛋白均可降低其糊化后的弹性，脱除醇溶蛋白则相反。脱除球蛋白和谷蛋白使早籼米粉糊化后的冻融稳定性分别降低121%和56%。该研究工作为利用不同溶解性内源蛋白质提高早籼米粉制品品质提供了重要的参考依据。     

大麦蛋白的组成

蛋白是大麦的主要组成之一，它对啤酒酿造有着重要的意义。本文就国外研究者对大麦蛋白的概况、醇溶蛋白、谷蛋白、清蛋白和球蛋白的相关研究进行介绍。     

未成熟蚕豆蛋白组分的分析

通过分析5个未成熟蚕豆品种在3个可食用阶段的蛋白质组分,探索未成熟蚕豆种子蛋白质组分的变化规律。采用分级提取的方法分别提取清蛋白、球蛋白、醇溶蛋白和谷蛋白组分,并利用考马斯亮蓝法和SDS-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate polyacrylamide gel electrophoresis,SDS-PAGE)对其含量和组分进行测定。结果表明,5个蚕豆品种最主要的蛋白组分为谷蛋白,其次为清蛋白和球蛋白,醇溶蛋白含量最低;随着蚕豆种子的不断成熟,清蛋白和球蛋白的含量明显增加;醇溶蛋白含量明显减少;谷蛋白含量因品种的不同,而表现出多样性;同一可食阶段,不同品种蛋白组分含量具有差异;随着可食阶段的延后,清蛋白和球蛋白的SDS-PAGE电泳条带逐渐增多。随着蚕豆种子的不断成熟,其蛋白各组分的含量发生变化:从S1到S2阶段,清蛋白的40 kDa的条带变浅,新增15 kDa至35 kDa的条带,球蛋白中的40 kDa的条带变浅甚至消失,新增20 kDa至35 kDa以及55 kDa的条带;从S2到S3阶段,清蛋白的15 k Da至35 k Da的小分子量条带颜色变浅,其含量减少,出现了60 kDa～65 kDa和70 kDa～85 kDa,甚至更大分子量的条带,而球蛋白的15 kDa至35 k Da的小分子量条带颜色变浅,40 kDa条带再次出现且加深,出现了60 kDa～65 kDa和70 kDa～85 k Da,甚至更大分子量的条带。这些表明在蚕豆成熟过程中,一些蛋白到一定阶段被降解,一些新的蛋白又被合成。     

苦荞蛋白的分离及其体外抗氧化活性的研究

目的:提取苦荞蛋白并评价苦荞蛋白各组分的体外抗氧化能力。方法:采用不同溶剂分级提取苦荞中的清蛋白、球蛋白、醇溶蛋白和谷蛋白,并采用考马斯亮蓝蛋白定量法测定各组分的蛋白含量,SDS-PAGE电泳观察各蛋白组分的分子量分布情况;采用比色法测定各蛋白组分在体外抑制超氧阴离子自由基(O2-·)的能力和清除羟自由基(·OH)的能力。结果:清蛋白、球蛋白、醇溶蛋白和谷蛋白占总蛋白的百分含量分别为42.65%、14.08%、9.54%和33.73%,清蛋白含量最高,醇溶蛋白含量最少;各蛋白组分的分子量分布不一样;清蛋白和球蛋白均具有清除羟自由基(·OH)的能力和抑制超氧阴离子自由基(O2-·)的能力,且球蛋白高于清蛋白(p0.05),而醇溶蛋白和谷蛋白无抗氧化能力。结论:苦荞中的清蛋白和球蛋白具有体外抗氧化能力。     

Feed protein fractions in various solvents of ruminant feedstuffs

The classical protein fractions, ie albumins, globulins, prolamins, glutelins and insoluble (or structural) proteins were evaluated in selected feedstuffs. Solvents used for classical protein fractionation were: dilute salt (1 M NaCl) in phosphate buffer (pH 7·0), aqueous alcohol (70% ethanol) and dilute alkali (0·05 M NaOH), with the subsequent separation of albumins and globulins by dialysis. In addition, crude protein content, soluble non-protein nitrogen, total true protein and soluble true protein in McDougall's buffer from the same feedstuffs were determined. The soluble non-protein N contributed only a small portion of the total N in feedstuffs. Total true protein was approximately 8–10% for energy feeds, and then increased to 30% for plant protein sources, while the soluble true protein was about the same for energy feeds and plant protein sources. The major proportion of protein in plant protein sources was in the form of globulins, followed by albumins and lesser amounts of glutelins and prolamins. In contrast, the major proportion of protein in cereals was in the form of prolamins and glutelins, followed by globulins and albumins. © 1997 SCI.     

Effect of seed treatments on the chemical composition and properties of two amaranth species: starch and protein

The seeds of two Amaranth species were studied. The starch contents were 543 and 623 g kg^?1 while crude protein contents were 154 and 169 g kg^?1 for Amaranthus caudatus and Amaranthus cruentus seeds, respectively. The effect of several treatments, including cooking, popping and germination and flour air classification on the protein and starch properties were studied. Air classification decreased the starch content and increased the protein content, while heating increased the protein but did not affect the starch content. Germination decreased both starch and protein contents. Amylose content was increased by air classification and heating, but was not affected by germination. It was found that all treatments increased the starch swelling power and reduced the falling number. The resistant starch content was increased in the high protein flour (HPF) fraction and germinated flour compared with the raw flour, while its content decreased in the heat treated seed flours. These processes also affected the starch gelatinization temperature and peak viscosity. The thermal properties of the starch flour were not affected by air classification while gelatinization energy was decreased significantly (by 52.0 and 90.0% and by 70.0 and 95.0%) in cooked and popped A caudatus and A cruentus seed flours, respectively. The gelatinization energy was highest in germinated seeds dried at 90 °C with values of 2.67 and 3.87 J g^?1. Air classification reduced the level of all protein fractions. Thermal treatment decreased the water‐soluble fraction (albumins + globulins) and alcohol‐soluble fraction (prolamins) in both species. The levels of all fractions except the water‐soluble fraction (albumins + globulins) were reduced significantly in both species by germination, which mainly increased the amount of aspartic acid, serine and alanine, while the amounts of threonine, arginine and tyrosine decreased in both species. The polypeptide bands of the HPF in both species were unchanged compared with the raw seed flours, but more intensive coloured bands were observed. Thermal treatments eliminated major and minor bands above 35.0 KDa in both species. Copyright © 2004 Society of Chemical Industry     

Effects of Protein in Wheat Flour on Retrogradation of Wheat Starch

Albumins, globulins, gliadins, and glutenins were isolated from wheat flour and the effects of those proteins on retrogradation of wheat starch were investigated. The results showed that only glutenins retarded retrogradation of wheat starch and other 3 proteins promoted it. The results of IR spectra proved that no S–S linkage formed during retrogradation of wheat starch blended with wheat proteins. Combination of wheat starch and globulins or gliadins through glucosidic bonds hindered the hydrolysis of wheat starch by α‐amylase. The melting peak temperatures of retrograded wheat starch attached to different proteins were 128.46, 126.14, 132.03, 121.65, and 134.84 °C for the control with no protein, albumins, glutenins, globulins, gliadins groups, respectively, and there was no second melting temperature for albumins group. Interaction of wheat proteins and starch in retrograded wheat starch greatly decreased the endothermic enthalpy (△H) of retrograded wheat starch. Retrograded wheat starch bound to gliadins might be a new kind of resistant starch based on glycosidic bond between starch and protein.     

Changes in prolamin and high resistant starch composition during the production process of Boza, a traditional cereal-based beverage

The aim of this work was to analyze changes occurring in cereal protein and starch composition throughout the production process of Boza for its potential exploitation as functional beverage. A sharp decrease in the extractability of albumins, globulins, glutenins and prolamins was found in the processed samples after the cooking step. This phenomenon was confirmed analyzing the extracted cereal proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which also revealed an apparent decrease in the number of wheat albumin/globulin, glutenin and prolamin bands in the gruel samples in comparison with that shown by the related flours. The application of an improved extraction procedure and reverse-phase high-performance liquid chromatography analysis confirmed that the prolamin content in Boza decreased markedly in comparison with that of the flour samples. Under the experimental conditions applied, the resistant starch content of Boza resulted significantly higher than that of flours; thus, this beverage can be regarded as a “high fiber” food in accordance with the recent European regulations. This is the first report that throws light on changes occurring in protein and starch components throughout the production process of Boza and provides direct evidence on the low prolamin and high resistant starch contents of this traditional cereal-based beverage.     

Functional and electrophoretic characteristics of faba bean (Vicia faba) flour proteins as affected by germination

Faba beans (Vicia faba) were germinated at room temperature for 3 and 6 days respectively. The effect of germination on the protein fractions, protein solubility index, PAGE pattern and some functional properties i.e. emulsification capacity (EC), foaming capacity (FC), foam stability (FS), water and fat absorption capacities of the flour was studied. Germination decreased albumins, globulins and prolamins at different levels but non protein nitrogen and glutelins were increased. The protein solubility index was high at both extreme pH values with an isoelectric point (IP) at pH of 4.4-4.5. The solubility of the protein slightly increased due to germination at all the pH values. PAGE pattern revealed on obvious dissociation and utilization for both fast and slow moving protein fractions during germination. Emulsification and foaming properties vs pH profile were similar to the pattern of solubility vs pH. Both properties were high at acidic and alkaline pH's and the minimum values were at pH 4 to 5. Germination process improved EC, FC and FS of the flour in comparison with that of dry bean flour. Water absorption of faba bean flours was improved during germination but the fat absorption markedly decreased.     

A differential scanning calorimetry study of wheat proteins

Thermal properties of wheat proteins were studied by differential scanning calorimetry (DSC). In order to assess the endothermic peaks, protein samples were heated with different water contents. At very low water content it was possible to register the protein endotherms at 50 °C for albumins and globulins, and 58 °C for gliadins, whereas two endothermic peaks at 64 and 84 °C were assigned to glutenins. The enthalpies of the protein transitions were very small for albumins, globulins, and gliadins, but high enthalpies (11.47 and 14.43 J/g) were obtained in the case of glutenins, suggesting a more ordered structure of these proteins. Reversibility of the glutenin denaturation was demonstrated by DSC; the successive heating-cooling cycles showed a shift in the endotherm peaks to higher temperatures and also higher enthalpies were required after each cycle.     

Improved methodology for the characterisation of transgenic Bt-11 maize cultivars using RP-HPLC profiles of albumin,globulin, prolamin,and glutelin protein fractions and chemometric analysis

A clear differentiation between Bt-11 transgenic and isogenic non-transgenic maize cultivars has successfully achieved analysing the perfusion and monolithic RP-HPLC profiles of the albumin, globulin, prolamin, and glutelin maize fractions together with a discriminant analysis. Significant differences between transgenic and isogenic non-transgenic cultivars were observed in the chromatograms obtained from any of the four protein fractions. The application of linear discriminant analysis to the area percentages corresponding to every peak detected in every protein fraction was successfully employed for the classification of transgenic Bt maize lines obtaining a global percentage of correct classification of 100%. For perfusion RP-HPLC, the variables with more discriminant power and prediction capability were the following peaks: peaks 1 and 3 for albumins, peak 2 for globulins, peaks 3 and 6 for prolamins, and peaks 7 and 8 for glutelins. In the case of monolithic RP-HPLC, the variables were peaks 2 and 3 for albumins, peak 5 for globulins, peaks 5, 6, and 7 of prolamins, and peak 10 for glutelins.     

Protein Fraction in Edible Macedonian Mushrooms

 The protein distribution in each of fifty-two kinds of Macedonian edible mushrooms was established by the Landry and Moureaux fractionation scheme. The investigated Macedonian mushroom samples contained a relatively high total protein content (14.0–52.1%, dry basis). The abundance of protein fractions was as follows: albumins (24.78%), globulins (11.46%), glutelin-like material (7.43%), glutelins (11.46%), prolamins (5.67%), and prolamin-like material (5.31%). Received: 21 July 2000 / Revised version: 4 October 2000     

Extraction and fractionation of wheat flour proteins

With the aid of a 1.5% sodium dodecyl sulphate solution (SDS) the proteins of two Dutch wheat flours were separated into an SDS-soluble and an SDS-insoluble fraction. The SDS-soluble fraction was fractionated with the aid of ethanol precipitation and gel filtration chromatography into albumins, globulins, gliadins, glutenins II and III, and glutelins I, II, III and IV. The SDS-insoluble proteinaceous material was separated into glutenins I and glycoproteins. The protein fractions were identified with the aid of SDS-polyacrylamide gel electrophoresis and amino acid analysis. The glutenins I and II consist of A, B and C subunits. Their molecular weights ranged from about 600 000 to 10 million. The glutenins III consist only of B and C subunits and their molecular weights ranged from 300 000 to 600 000. A hypothesis explains how the glutenins III are the precursors for glutenins I and II and how they contribute to gluten's structure. The glutelins I consist of α β and γ subunits and their molecular weights ranged from about 600 000 to several millions. The glutelins II consist also of α β and γ subunits with a molecular weight of about 300 000 to 600 000, while the molecular weights of the glutelins III and IV ranged from 10 000 to 200 000. All glutelins are insoluble in 70 % aqueous ethanol and 5 M urea, but soluble in SDS and 0.1M NaOH. Only the glutelins III and IV are soluble in 0.1M HAc. The globulins consist of a heterogeneous fraction of components, their molecular weights arranged from 98 000 to 10 000. The gliadins form a heterogeneous but homologous group of polypeptides with an average molecular weight of 35 000. The albumins consist of components with molecular weights lower than 15 000.     

The influence of nitrogen fertilisation on quantities and proportions of different protein types in wheat flour

The flours of 13 wheat varieties grown at different levels of nitrogen fertilisation were characterised by the quantitative determination of flour protein groups and gluten protein types using a combined extraction/HPLC procedure. The results demonstrate that the quantities of albumins and globulins were scarcely influenced by different nitrogen fertilisation, whereas those of gluten proteins (gliadins, glutenins) were strongly influenced. The effect on gliadins was more pronounced than on glutenins, as well as the effect on major protein types (α-gliadins, γ-gliadins, LMW subunits of glutenin) in comparison with minor types (ω-gliadins, HMW subunits of glutenin). The proportions of hydrophilic proteins (ω-gliadins, HMW subunits of glutenin) were increased by high levels of nitrogen and those of hydrophobic proteins (γ-gliadin, LMW subunits of glutenin) were decreased. The degree of the effects on both quantities and proportions of flour protein groups and gluten protein types was strongly dependent on the variety. © 1998 SCI.