紫苏籽中不同蛋白组分的功能性质研究

以紫苏籽为原料,经粉碎过60目筛后石油醚脱脂得到紫苏籽脱脂粉,然后采用不同方法提取得到紫苏籽分离蛋白、清蛋白和球蛋白,研究了3种蛋白的氨基酸组成及持水性、溶解性、乳化性等功能特性。结果表明:紫苏籽脱脂粉中蛋白质含量丰富,不同紫苏籽蛋白的氨基酸组成相近,其中谷氨酸含量最高,且均含有8种必需氨基酸;分离蛋白的热变性温度稍高于其他两种蛋白;清蛋白的持水性、持油性较好;在pH 1～10范围内,3种蛋白的溶解性均呈现出U型变化趋势,其中球蛋白的溶解性最好;在不同pH下,球蛋白的乳化活性和乳化稳定性高于其他两种蛋白。     

萝卜籽粕蛋白质的组成及功能性质

以萝卜籽粕为原料,提取了其中的蛋白质;根据溶解性,萝卜籽粕蛋白中的清、球、谷、醇溶蛋白被分 离;用氨基酸自动分析仪测定了萝卜籽粕蛋白的氨基酸组成;物理化学方法测定萝卜籽粕蛋白的功能性质以及体外 清除1,1-二苯基-2-三硝基苯肼自由基、?OH、NO2 －、H2O2的能力。结果表明：萝卜籽粕蛋白中球、谷、清和醇溶蛋 白含量分别占总蛋白质的44%、33%、21%和2%;萝卜籽粕蛋白含18 种氨基酸,第一限制氨基酸为蛋氨酸,其氨基 酸评分为57。萝卜籽粕蛋白具有很好的功能性质及抗氧化能力,表明有很高的开发价值。     

Amino acid composition of storage proteins of a promising chickpea (Cicer arietinum L) cultivar

The amino acid compositions of flours made from the cotyledons and from the whole seeds of a disease-resistant, stable and high-yielding cultivar of chickpea (Cicer arietinum L) cv H75–35, known locally as Gaurav, have been analysed. These, together with similar analyses of the albumin, globulin, legumin and vicilin protein fractions, have been compared with those of other legumes. Seed protein content was 19·8 % with globulin constituting 62·4 % of the total seed protein. The ratios of albumin to globulin and legumin to vicilin were 1:4 and 6:1, respectively. The proportion of basic amino acids in the albumin was low whereas the reverse was true in the globulin. The legumin fraction seems to be superior in terms of total essential amino acids to those from other sources. Sulphur amino acids were the most limiting, followed by tryptophan or threonine depending on the fraction. However, the ratio of methionine to cystine was high (2·76:1). The extent of the sulphur amino acid deficiency was assessed, and possible approaches for its improvement are outlined.     

Amino acid profiles and quality from lotus seed proteins

BACKGROUND: Protein composition, amino acid profile and nutritional value of the lotus seed and its Osborne fractions were investigated. The seed was rich in protein with 19.85%, and showed well balanced amino acid composition compared with FAO/WHO pattern, Its nutritive properties were similar to those observed in the reference soybean protein. Phenylalanine, tyrosine, leucine and lysine were the limiting amino acids in the seed proteins. The albumin and globulin were the main protein fraction, the amino acid profile and nutritional value were close to the seed protein. RESULTS: Changes in transition temperature and thermal stability were observed through different solvent extractions. Albumin possessed the predominant thermal stability (81.4 °C) followed by globulin (74.49 °C), prolamin (69 °C) and glutelin (65.6 °C). So, solvent compositions influence the profile of AAs and their nutritive value, and aqueous solvent with 0.1 mol L^?1 NaCl was an efficient protein solubiliser. CONCLUSION: The results indicated that the extraction processes influenced the lotus seed protein quality and thermal stability. Overall, the study revealed that the lotus seed protein was nutritionally well‐balanced protein and might be of significant importance in the formulation of diets for humans. © 2012 Society of Chemical Industry     

Characterization and Analysis of Protein Structures in Oat Bran

Globulin, albumin, gluten, and gliadin in oat bran were prepared by the Osborn method using oat bran as starting material. We characterized the secondary and tertiary structures of 4 proteins using circular dichroism, Fourier‐transform infrared spectroscopy, and fluorescence spectroscopy in order to analyze the composition and functional mechanisms. The results showed that the amino acid composition in all the 4 proteins was relatively balanced, and the essential amino acid content in albumin and globulin was high. The molecular weights of albumin, globulin, gliadin, and gluten were 19 to 21, 15 to 53, 20 to 38, and 10 to 90 kDa, respectively. The composition of gluten was a little complex compared to those of the other oat bran proteins. The secondary structure distribution of the 4 proteins differed, and increase in the pH resulted in modification of the β‐sheet structure to α‐helical structure. Moreover, the α‐helix content and surface hydrophobicity were negatively correlated (r = –0.988, P < 0.05). The peak position (λ_max) and intensity of the fluorescence spectra of 4 proteins were in the order of gliadin > globulin > gluten > albumin, indicating that surface hydrophobicity of gliadin was the strongest and that of albumin was the weakest among the 4 proteins.     

Fractionation and biochemical characterization of moth bean (Vigna aconitifolia L.) proteins

Moth bean seeds contained 24 g/100 g protein (micro-Kjeldahl N×6.25) on a dry weight basis. Among the solvents tested, 0.1 mol/l NaOH and 0.1 mol/l sodium phosphate buffer (pH 7.5) were the most effective in solubilizing the seed flour proteins. Native isoelectric focusing of the total soluble proteins indicated moth seed proteins to be acidic (pI range 4.55-<6.55) with a few neutral to alkali proteins (pI range 7.35-9.3). Globulin fraction dominated the seed protein composition accounting for ∼64 g/100 g of the total soluble proteins in the seeds. The globulin fraction was composed of at least three major glycopeptides with an estimated molecular mass range of 45-55 kDa and several additional polypeptides in the 14-32 kDa range. Sulfur amino acids were the first limiting amino acids in the seed flour proteins. Native and heat denatured albumin and glutelin fractions were readily hydrolysed, in 30 min, by pepsin at 37 °C. Although resistant to proteolysis in the native state, heat denatured globulin (100 °C, 30 min, boiling water-bath) was completely digested to <14 kDa polypeptides by pepsin in 30 min at 37 °C. Moth bean was devoid of detectable phytohemagglutinating activity and had low trypsin inhibitory activity when compared with the corresponding activities in soybeans.     

Walnuts (Juglans regia L): proximate composition,protein solubility,protein amino acid composition and protein in vitro digestibility

Walnuts contained 16.66% protein and 66.90% lipids on a dry weight basis. Non‐protein nitrogen values ranged from 6.24 to 8.45% of the total nitrogen when the trichloroacetic acid concentration was varied within the range 0.25–1.0 M . Albumin, globulin, prolamin and glutelin respectively accounted for 6.81, 17.57, 5.33 and 70.11% of the total walnut proteins. Walnut proteins were minimally soluble at pH 4.0. The majority of total walnut protein polypeptides had estimated molecular weights in the range 12 000–67 000. The Stokes radius of the major protein in walnuts (glutelin fraction) was 66.44 ± 1.39 Å. Lysine was the first limiting essential amino acid in total walnut proteins as well as in the globulin and glutelin fractions. Leucine and methionine plus cysteine were the second limiting essential amino acids respectively for the prolamin and albumin fractions. Hydrophobic and acidic amino acids dominated the amino acid composition in all protein fractions. Native and heat‐denatured walnut glutelins were easily hydrolysed by trypsin, chymotrypsin and pepsin in vitro. © 2000 Society of Chemical Industry     

大叶紫薇果仁蛋白质和氨基酸的分析研究

对大叶紫薇果仁蛋白质与氨基酸进行了研究,测得果仁粗蛋白的含量为10.2 % ,其蛋白质组成为:清蛋白3.31%、球蛋白1.43%、醇溶蛋白2.09%、谷蛋白1.54%;含有18 种氨基酸,其中有营养必需的8 种氨基酸. 并根据模式蛋白质,应用化学分析法对果仁蛋白质营养价值进行了评价.     

Analysis of protein fractions and some minerals present in chan (Hyptis suaveolens L.) seeds

Chan (Hyptis suaveolens L.) seeds have been used as food as well as in traditional medicine in several countries of America, Asia and Africa. Chan seed protein content was 13.9% on dry weight basis. Analysis of its protein composition showed 39% globulins, 36% glutelins, 24% albumins, and 1% prolamins. By defatting the flour with chloroform/methanol, it increased the extracted proteins and improved the protein band resolution after SDS-PAGE, showing 5 albumin bands, 8 globulin bands, and 2 prolamin and glutelin bands. The aromatic amino acid content in chan seeds is higher than those of other grains including maize, with good levels of branched chain amino acids. In general, except for lysine, it has a well-balanced amino acid composition, providing a good supply of almost all the essential amino acids for the different age groups. Magnesium content was high, whereas calcium, potassium, and phosphorous were in the average range when compared to barley, oat, rice, and wheat. The present results indicate that seeds from the chan plant could be relevant because of their nutritional properties and they have the potential to be widely used in the production of high-quality food. PRACTICAL APPLICATION: Chan seeds are presently used in a very limited manner as a food source; however, considering their high quality composition, they have the potential for a more extended use in the food industry.     

灰褐牛肝菌(Boletus griseus)子实体的营养评价及蛋白质组分分析

测定灰褐牛肝菌子实体的基本成分、单糖、脂肪酸和氨基酸组成,矿物质含量及其蛋白质连续累进组分的含量,并对其蛋白质的营养价值进行系统评价。结果表明:灰褐牛肝菌子实体中粗蛋白质量分数为28.22%;葡萄糖含量最高,为258.04 mg/g;17种脂肪酸被检出,亚油酸、油酸和棕榈酸分别占脂肪酸总量的35.91%、28.46%和24.50%;游离氨基酸共检出29种,其中Tyr和Ala含量较高,甜味氨基酸和鲜味氨基酸分别占游离氨基酸总量的23.37%和12.69%;水解氨基酸中必需氨基酸含量较高,占氨基酸总量的38%,其氨基酸评分、必需氨基酸指数、生物价、营养指数和氨基酸比值系数分别为71.88、69.93、64.52、19.73和50.05。灰褐牛肝菌富含Mg、Fe、Zn、Cu,同时有毒元素Cd含量相对较高。蛋白质连续累进组分中清蛋白含量最高,占总蛋白的65.62%,但其Cd含量较高,占总Cd量的38.79%。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析表明清蛋白和球蛋白的分子质量分布主要在40 k D,差异热量扫描分析表明其热变性温度分别为125.04℃和75.04℃。结果表明,灰褐牛肝菌子实体的营养价值较高,但是由于Cd元素含量较高,可能存在一定的健康风险。     

Functional and nutritional properties of isolated bovine blood proteins.

Various properties of freeze-dried fractions of bovine blood have been compared. Dried whole plasma, albumin, globulin and globin showed high solubility from pH 3 to 8, but this fell sharply with plasma on storage at 40°C and Aw 0.32 or higher. Albumin showed the best foaming properties followed by plasma, globulin and globin. These proteins in 1 % solution were able to emulsify 60, 115, 70 and 45% of their volume of oil, respectively. Net protein ratios were 3.57 for globulin, 1.96 for albumin and negative for globin. Chemical scores indicated that methionine was the most limiting amino acid for globulin and albumin. Isoleucine was limiting for globin.     

Extractability and Chromatographic Characterization of Wheat (Triticum aestivum L.) Bran Protein

About 70% of the protein for human consumption is derived from plants, with cereals as the most important source. Wheat bran protein has a more balanced amino acid profile than that of flour. We here for the first time report the amino acid, size exclusion, and SDS‐PAGE profiles of bran Osborne protein fractions (OPFs). Moreover, we also investigated how OPFs are affected when physical barriers which entrap proteins in bran tissues are removed. Albumin/globulin is the most abundant OPF. It is richer in lysine and asparagine/aspartic acid than other OPF. Most bran albumin/globulin proteins have a molecular weight (MW) lower than 30 k and their chromatographic profiles differ from those of flour. The prolamin has high levels of proline and glutamine/glutamic acid. It is rich in proteins with a MW of 30 to 45 k and about 66 k reflecting contamination with gliadin from endosperm. The glutelin has high levels of glycine, proline, and glutamine/glutamic acid. Its protein is of intermediate and high MW with little protein with MW lower than 30 k. The high (MWs from 80 to 120 k) and low (MW around 45 k) MW glutenin subunits of flour are also present in bran. The glutelin of wheat endosperm is named glutenin. Ball milling releases albumin/globulin and glutelin but not prolamin. Not all glutelin was endosperm glutenin as a substantial part was entrapped in the aleurone cells.     

Val bean (Lablab purpureus L.) proteins: composition and biochemical properties

Val bean (Lablab purpureus L.) proteins were fractionated using the Osborne protein fractionation scheme and biochemically characterized. The seed flour contained 302 g kg^?1 protein (micro‐Kjeldahl N × 6.25) on a dry weight basis. Albumin, globulin, prolamin, and glutelin accounted for 22.8%, 45.1%, 1.8% and 30.3%, respectively, of the total soluble seed proteins. Among the solvents tested, 0.1 mol L^?1 aqueous NaOH was the most effective protein solubilizer. Isoelectric focusing indicated the seed proteins to be predominantly acidic (pI range was ～4–7). Val globulin is a glycoprotein composed of at least three polypeptides in the molecular mass range 51–64 kDa. Albumin fraction had the highest trypsin inhibitory activity, while the globulin fraction registered the highest hemagglutinating activity. Sulfur amino acids were the first limiting amino acids in the total seed proteins. The proportion of essential to total [E/T(%)] amino acids for the bean flour was 36.97%. Among the protein fractions, glutelin fraction had the highest E/T (42.86%) followed by albumin (41.57%), globulin (39.87%), and prolamin (39.15%). Native globulin, although resistant to pepsin, was effectively digested in vitro upon moist heat (100 °C, 30 min) denaturation. Copyright © 2007 Society of Chemical Industry     

Composition,physicochemical properties of pea protein and its application in functional foods

Abstract

Field pea is one of the most important leguminous crops over the world. Pea protein is a relatively new type of plant proteins and has been used as a functional ingredient in global food industry. Pea protein includes four major classes (globulin, albumin, prolamin, and glutelin), in which globulin and albumin are major storage proteins in pea seeds. Globulin is soluble in salt solutions and can be further classified into legumin and vicilin. Albumin is soluble in water and regarded as metabolic and enzymatic proteins with cytosolic functions. Pea protein has a well-balanced amino acid profile with high level of lysine. The composition and structure of pea protein, as well as the processing conditions, significantly affect its physical and chemical properties, such as hydration, rheological characteristics, and surface characteristics. With its availability, low cost, nutritional values and health benefits, pea protein can be used as a novel and effective alternative to substitute for soybean or animal proteins in functional food applications.     

Characterisation and functional properties of watermelon (Citrullus lanatus) seed proteins

BACKGROUND: People in developing countries depend largely on non‐conventional protein sources to augment the availability of proteins in their diets. Watermelon seed meal is reported to contain an adequate amount of nutritional proteins that could be extracted for use as nutritional ingredients in food products. RESULTS: Osborne classification showed that globulin was the major protein (≥500 g kg ^?1) present in watermelon seed meal, followed by albumin and glutelin. Sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that the polypeptides had low molecular weights ranging from 35 to 47 kDa. Isoelectric focusing revealed that the isoelectric point of most proteins was in the acidic range 4–6. These proteins are rich in aspartic acid, glutamic acid and serine. An increase in pH (5–9) significantly (P < 0.05) decreased the denaturation enthalpy of these proteins. Among functional properties, albumin exhibited a much higher dispersibility index (810.3–869.6 g kg^?1) than globulin (227.8–245.4 g kg^?1), glutelin (182.1–187.7 g kg^?1) and prolamin (162.3–177.7 g kg^?1). Digestibility was in the ranges 760.6–910.0 and 765.5–888.5 g kg^?1 for Mateera and Sugar Baby watermelon protein fractions respectively, while surface hydrophobicity ranged from 126.4 to 173.2 and from 125.8 to 169.3 respectively. The foaming and emulsifying properties of albumin were better than those of the other proteins studied. CONCLUSION: The good nutritional and functional properties of watermelon seed meal proteins suggest their potential use in food formulations. Copyright © 2010 Society of Chemical Industry     

Amino acid profiles of chemical and anatomical fractions of oat grains

Anatomical fractions of oat grains obtained by manual dissection and chemical fractions corresponding to the four major classes of protein present in seeds have been analysed for amino acids by automated column chromatography. Estimates of lysine indicate that this amino acid is concentrated in the embryo and in the albumin and globulin fractions. The salt-soluble proteins can be identified on gels of polyacrylamide following electrophoresis. It is suggested that selection of varieties with high levels of salt-soluble protein offers a means of improving the amino acid balance of oat proteins in relation to the feeding of non-ruminant animals.     

Effects of gamma irradiation on edible seed protein,amino acids and genomic DNA during sterilization

This work describes radiation-induced effects on edible seed protein profiles, carbohydrates, amino acids and genomic DNA during gamma sterilization. The total protein and carbohydrate was decreased with increasing dose compared to control samples. Oryzasativa L. Cv-2233 exhibited a minimum effect in terms of its loss in total soluble protein content, compared to other seeds at 6 kGy, and the soluble protein fraction, containing 14–16 kDa albumins and 22 kDa globulin, was unchanged up to 6 kGy. In Cicer arietinum, the effect of gamma rays was more pronounced on albumin and prolamin with respect to glutelin and globulin. The easy-to-digest and difficult-to-digest proteins were not significantly affected up to 4 kGy. However, the soluble free amino acids of all the seeds increased with increasing dose. The total DNA content and band intensities both decreased with increasing absorbed dose; however, the band positions were unchanged for all seed types.     

Japanese barnyard millet (Echinochloa frumentacea): Protein content,quality and SDS–PAGE of protein fractions

Total protein from five varieties of Japanese barnyard millet (Echinochloa frumentacea,) was separated into albumin/globulin, prolamin and glutelin fractions. The protein fractions were examined by sodium dodecylsulphate polyacrylamide gel electrophoresis. Total protein of the varieties ranged from 110·5 to 139·3 mg g^?1 of which 11·3–17·2% was albumin/globulins, 6·8–9·3% prolamins, 7·5–11·6% prolamin–like, 5·9–9·1% glutelin-like and 39·3–54·4% true glutelins. Amino acid analyses of the total protein showed that the varieties had essentially the same ammo acid composition. With the exception of lysine the amino acid levels adequately matched the provisional FAO scoring pattern. The amino acid composition of the protein fractions was also very similar. Electrophoretic analysis showed that the albumin/globulin fraction contained three or four components; the prolamin and glutelin fractions each had five components. The glutelin fraction had higher molecular weight components than the other two fractions.     

热变性大米蛋白的结构和性质研究Ⅰ米蛋白加热前后的溶解特性和氨基酸变化

为探讨热变性米蛋白的性质与结构关系,分析了大米蛋白加热前后的溶解性能和氨基酸组成变化。结果表明,米渣中各种蛋白质的含量大大低于未受高温处理的原料大米;米渣蛋白中胱氨酸含量比大米谷蛋白提高83%,说明大米醇溶蛋白、球蛋白和清蛋白等受热后也存在于米渣中;米渣谷蛋白胱氨酸含量比米渣蛋白降低23%,说明胱氨酸是影响米渣蛋白溶解的重要因素。     

Quantitative studies on the cotyledonary proteins in the genus Pisum

Forty-five lines of peas including primitive or wild forms, field peas, and round and wrinkled garden peas, were grown under uniform conditions and the seeds examined for variation in protein characteristics likely to influence nutritional value. The characters measured were crude protein, extractable protein, globulins and albumins, the percentages of legumin, total sulphur and protein sulphur, carbon: nitrogen and nitrogen: sulphur ratios. The extractable protein was separated quantitatively into an albumin fraction (20–35%) and a globulin fraction (legumin and vicilin). Without exception lines high in albumin content were low in legumin content (correlation coefficient r= ?0.757). As both the albumin fraction and legumin are rich in sulphur amino acids, this negative correlation has important implications for attempts through plant breeding to improve the nutritional quality of legume seed proteins, by increasing the sulphur amino acid content. Total sulphur was not correlated with any other protein character.