Chemical composition,functional properties,and bioactivities of rapeseed protein isolates

In order to utilize rapeseed protein from oil industry waste for food applications, rapeseeds were pretreated to remove the oil using hexane. Two protein isolates were prepared, one by precipitation at controlled pH and the other by ultrafiltration. The precipitated and ultrafiltered protein isolates, respectively, contained 70.8% and 98.7% protein. The ultrafiltered protein isolate had a better emulsification capacity than had whole egg. The ultrafiltered protein isolate had a protein solubility of 52.5–97.2% in the range pH 3–9, whilst the maximum protein solubility of the precipitated protein isolate was 26.4% in the pH range 7–9. There were no significant differences between the precipitated and ultrafiltered protein isolates regarding their angiotensin converting enzyme inhibition are their bile acid-binding capacity. Their bile acid-binding capacity and angiotensin converting enzyme inhibition capacities were lower than of those de-oiled soybean. They showed stronger DPPH radical-scavenging activity than did de-oiled soybean.     

New processing of lupin protein isolates and functional properties.

A growing demand for functional plant proteins could be identified, which properties are customized for specific applications and formulations as food ingredients. Native lupin proteins (alpha, beta, gamma) conglutin have a good solubility at appropriately chosen conditions. A novel procedure has been proposed to maintain the native protein properties. Lupin proteins are extracted from hexane deoiled lupin. The protein product type E comprises high molecular weight proteins (alpha, beta-conglutin), which are separated using alkaline extraction and acid precipitation procedures. The protein product type F is enriched in the gamma-conglutin fraction and is separated from the acid pre-extract applying cross flow filtration at pH 7-8. For the zirconium oxide membrane the filtration rate can be increased by appropriately chosen pH conditions up to 70 l/m2h. Lupin protein fraction (type E and F) are highly soluble protein isolates with outstanding emulsification, salt tolerance and foaming properties. These new lupin proteins (type E and F) offer extremely interesting properties for application in food systems and are available from pilot plant fractionation.     

Functional Properties of Lupin Seed (Lupinus mutabilis) Proteins and Protein Concentrates

Functional and electrophoretic properties of the seed flour and a protein concentrate prepared by alkaline extraction from lupin seeds (Lupinus mutabilis, cultivar H-6) were investigated. SDS-PAGE indicated presence of 13 and 12 subunits in the seed flour proteins and the protein concentrate, respectively. Lupin protein concentrate had good water and oil absorption and gelation properties. Solubility of lupin proteins was minimum at a pH of 4.0 but increased rapidly beyond pH 5.0. Foaming capacity of the protein concentrate could be improved by increasing concentration as well as by adding NaCl and was influenced by pH and incorporation of certain carbohydrates. Emulsion properties of lupin proteins were concentration and pH dependent. Moist heat improved the in vitro digestibility of the seed proteins. The seed flour as well as the protein concentrate did not have detectable trypsin, chymotrypsin, and α-amylase inhibitory activities.     

Functionality of Flours, Protein Fractions and Isolates from Field Peas and Faba Bean

Field pca and faba bean proteins are rich sources of lysine, and air classification of the pin milled flours essentially doubled the protein contents in the protein fractions. The proteins in these flours and protein fractions were highly soluble at acid pH and exhibited only a narrow range of insolubility at pH 4–5. Water holding and oil absorption capacities increased in proportion to protein contents of the flour, protein fraction, and isolate of each legume, including soybean flour and isolate, but oil emulsification properties were uniformly high among all products. The protein fractions exhibited excellent whipp-ability and foam stability compared to soybean controls, and their promising functional properties suggested potential applications in meat emulsions, beverages and bakery products.     

干燥方式对大豆分离蛋白功能性质的影响

本文以醇洗豆粕为原料制备大豆分离蛋白，着重探讨了冷冻和喷雾干燥两种干燥方式对大豆分离蛋白功能性质，如溶解度、凝胶性能、乳化性能、起泡性能与粘度等的影响。实验表明，冷冻干燥样品具有较低的粘度和溶解度，且凝胶性能和泡沫稳定性明显高于喷雾干燥样品；两种样品的乳化稳定性和起泡能力比较接近，但喷雾干燥样品的乳化活性略高于冷冻干燥样品。     

New processing of lupin protein isolates and functional properties

A growing demand for functional plant proteins could be identified, which properties are customized for specific applications and formulations as food ingredients. Native lupin proteins (α, β, γ) conglutin have a good solubility at appropriately chosen conditions. A novel procedure has been proposed to maintain the native protein properties. Lupin proteins are extracted from hexane deoiled lupin. The protein product type E comprises high molecular weight proteins (α, β‐conglutin( which are separated using alkaline extraction and acid precipitation procedures. The protein product type F is enriched in the γ‐conglutin fraction and is separated from the acid pre‐extract applying cross flow filtration at pH 7–8. For the zirconium oxide membrane the filtration rate can be increased by appropriately chosen pH conditions up to 70 l/m²h. Lupin protein fraction (type E and F) are highly soluble protein isolates with outstanding emulsification, salt tolerance and foaming properties. These new lupin proteins (type E and F) offer extremely interesting properties for application in food systems and are available from pilot plant fractionation.     

Gelation and In Vitro Digestibility of Soybean Protein Isolate Treated by a Ternary System Containing Horseradish Peroxidase,Glucose Oxidase,and Glucose

The aim of the present study was to investigate the potential application of a ternary system containing horseradish peroxidase, glucose oxidase, and glucose for the oxidative cross-linking of soybean protein isolate. Protein content, reaction temperature, and original pH were fixed at 30 g/L, 37°C, and 7.0, while suitable glucose, glucose oxidase, horseradish peroxidase addition, and reaction time selected from single factor trials for the one-step treatment were 0.1 mmol, 4.0 U, 200 U/g protein, and 3 h, respectively. In the two-step treatment, glucose, glucose oxidase, and horseradish peroxidase addition were the same, but a reaction time of 1 or 2 h was used for the glucose oxidase or horseradish peroxidase treatment. Two modified soybean protein isolates obtained by the one- and two-step treatment contained some protein polymers, had relative dityrosine content of 414 and 381, respectively, and showed lower in vitro digestibility and less free sulfhydryl than the control soybean protein isolate. During acidification induced by glucono-δ-lactone, the modified soybean protein isolates showed shorter gelation time (57 and 61 versus 72 min), lower loss tangent and gelation point temperature (52.9 and 53.2 versus 62.7°C) but higher final storage modulus than the control soybean protein isolate. The acidified gels prepared from the modified soybean protein isolates also exhibited enhanced hardness, springiness, cohesiveness, and chewiness, and finer microstructural features. The ternary system was capable of treating protein ingredients to improve their gelation properties.     

Functional Properties of Guar Proteins

Water and fat absorption, emulsification capacity (E.C.), foaming capacity (F.C.), and foam stability (F.S.) of guar meal and protein isolate have been determined and compared with those of soybean meal and isolate. Guar meal had lower water absorption capacity, similar fat absorption capacity and greater F.S. and E.C. than soybean meal. Guar protein isolate (GPI) had lower water absorption capacity but higher fat absorption capacity than soy protein isolate (SPI). The foaming capacity and emulsification capacity were similar at all pH's except around pH 4. However the foam stability of GPI was greater than that of SPI.     

In vitro digestibility,physico-chemical and functional properties of apricot kernel proteins

The chemical composition of apricot kernel flour and protein isolates was determined. The flour contained about 48% protein, mainly albumins. The solubility at different pH values showed a single isoelectric point at pH 4 and the solubility increased in both acidic and alkaline pH. The digestibility of the protein was high in the pepsin-pancreatin system and quite low when pepsin or trypsin was used.The ultraviolet absorption spectrum of the proteins of both flour and protein isolates was typical of those of other vegetable proteins. The polyacrylamide gel electrophoresis pattern of apricot kernel proteins consisted of four major protein fractions. Water and fat absorption and emulsification capacity of flour and protein isolates were quite comparable with that of soybean. Detoxified apricot kernel flour and protein isolates appear to be good sources of protein for food products.     

棉籽蛋白功能特性的研究

考察了棉籽浓缩蛋白、沉淀蛋白和溶解蛋白3种棉籽蛋白的氮溶指数、吸水性、吸油性、起泡性与泡沫稳定性、乳化性与乳化稳定性等功能特性。结果表明,棉籽溶解蛋白的乳化性和起泡性较佳;棉籽浓缩蛋白和沉淀蛋白,除吸油、吸水能力强之外,其他的功能特性均较差。在吸水性方面,棉籽蛋白的吸水性要低于菜籽沉淀蛋白,但高于大豆沉淀蛋白。在吸油性方面,棉籽蛋白均低于菜籽蛋白和大豆蛋白。     

Functional Properties of Chinese Rapeseed Protein Isolates

A membrane-based protein isolation process developed in our laboratory produced two protein isolates from CH₃OH/NH₃/H₂O-hexane-extracted Chinese rapeseed meal. Both contained ～99% protein (NX6.25), and they were essentially free of glucosinolates or their breakdown products (<2,2 μmol/g). Their functional properties were evaluated and compared with a commercial soybean protein isolate. The precipitated isolate gave high values for all properties except nitrogen solubility index (NSI) while the soluble isolate showed excellent NSI and fat absorption but poor emulsification characteristics. They both had good foaming properties. The two Chinese rapeseed protein isolates complemented each other and were comparable to soybean protein isolate in most functions.     

超声处理对黑豆蛋白与可溶性多糖复合物功能性质及结构的影响

将可溶性多糖与黑豆蛋白进行复合可以改变蛋白的许多功能性质。采用荧光分析、圆二光谱检测超声处理对黑豆蛋白与可溶性多糖复合物蛋白的功能性质及结构的影响。结果表明,将黑豆蛋白与可溶性多糖以1∶2的比例混合时,复合物的乳化性最好,此时复合物乳液比较稳定。用不同超声时间处理上述复合物溶液,处理16 min的复合物的乳化性最好,处理8 min的复合物的乳化稳定性最佳。同时随着超声时间的延长,蛋白质二级结构中α-螺旋含量上升,β-折叠下降,说明蛋白质的结构与功能性质有着密切关系。适当的超声处理可以改变黑豆蛋白与可溶性多糖复合物的结构,提高某些功能特性。     

A comparative study of the functional properties of amaranth and soybean globulin isolates

The functional properties of the amaranth globulin isolate were determined and compared to those of the well studied soybean globulin isolate. Functional properties investigated included protein solubility, heat coagulation, foaming and emulsifying activity and stabilities, as well as fat binding. Overall, the amaranth globulin isolate was found to have significantly higher solubility (p ⪇ 0.05) i.e., 9 times higher, and higher heat stability (p ⪇ 0.05) in the vicinity of its isoelectric point, pH 5–6, than the corresponding soybean globulin isolate. Between pH 3–9 the amaranth globulin isolate was found to have significantly higher (p ⪇ 0.05) foaming capacities and stabilities than the soybean isolate. Maximum foaming capacity for the amaranth globulin was determined to occur around its isoelectric point. The emulsifying activity of the amaranth globulin isolate was found to be significantly higher (p ⪇ 0.05) between pH 3–9 than the corresponding soybean globulin isolate. The most substantial difference between the two isolates was that the amaranth isolate showed maximal emulsifying activity and stability at pH 7.0. Little difference was observed in the fat absorption capacities between the two prepared isolates. Nutritionally, the amaranth globulin isolate was found to be of superior quality compared to the soybean globulin isolate due to its higher content of essential amino acids. Overall, the functional properties of the amaranth globulin isolate were much better than the soybean isolate especially in the vicinity of its isoelectric point, suggesting a potential advantage if used in various thermally processed food formulations that fall within this pH range; a range where more common isolates perform very poorly.     

Some functional properties of oilseed proteins

Oilseeds have potential food uses because of their high protein content. Besides, these proteins when added to a type of foods, supply desirable functional properties, such as whipping capacity and viscosity, emulsification and water and oil holding capacities. Rapeseed and soybean protein isolates were found to possess whipping capacity followed by those of sunflower, peanut, sesame, cottonseed and safflower. The addition of sugar improved the whipping properties of oilseed proteins. The whipping capacity of oilseed proteins decreased due to heating at 100 degrees C for time of 15 to 60 min. Soybean protein had the highest emulsifying capacity compared with the other oilseed proteins. The heated oilseed proteins had emulsification properties similar to or better than the control. Glandless cottonseed protein had high water and oil holding capacities. The water holding capacity of oilseed proteins decreased gradually as the duration of heating at 100 degrees C was increased. On the other hand the heated oilseed proteins had oil holding capacities similar to or better than unheated proteins.     

沙米麸皮和外胚乳分离蛋白的理化及功能性质

利用碱提-等电点沉淀技术分别从沙米麸皮和去皮沙米中提取出沙米麸皮分离蛋白(B-pro)和外胚乳分离蛋白(S-pro),研究这两种蛋白的理化及功能性质。结果表明,沙米麸皮中蛋白以球蛋白为主,而去皮沙米中以清蛋白为主。B-pro和S-pro纯度分别为94.33%、91.80%(m_d),S-pro颜色更白。两种蛋白均含有丰富的必需氨基酸,且S-pro中Lys含量较高。B-pro和S-pro的功能性质随pH值的变化均符合植物蛋白的一般规律,总体而言,不同pH值条件下S-pro的功能性均优于B-pro。与大豆分离蛋白和鸡蛋蛋白相比,B-pro和S-pro的持油能力及发泡性较好,而溶解性、持水力及乳化性较弱。     

Emulsifying and foaming properties of protein isolates prepared from heated milks

Surface activities at the air-water interface and the emulsifying and foaming properties of sodium caseinate, conventional casein-whey protein co-precipitate prepared from milk heated at 90°C × 15 min at pH 6.6 and milk protein isolates prepared from milks heated at 90°C × 15 min at pH 7.5 or at 60°C × 3 min at pH 10.0 were determined. The surface activities of the four proteins at the air-water interface were similar, while the emulsifying capacity and emulsion stabilizing ability of casein was less than that of the milk protein isolates or the conventional co-precipitate. Fat surface areas formed on emulsification with the four proteins were similar and increased with increasing power input. Total protein adsorbed at the interface and protein load (mg protein/m₂ fat) for the emulsions stabilized by sodium caseinate and the milk protein isolate prepared from the milk heated at 90°C × 15 min at pH 7.5 were similar and lower than those for emulsions stabilized by the other two proteins. Foam overruns followed the order: sodium caseinate > milk protein isolate prepared from milk heatedat90°C × 15min, pH 7.5 > milk protein isolate prepared from milk heated at 60°C × 3 min, pH 10.0 > conventional co-precipitate, while foam stabilities followed the reverse order.     

植物蛋白在肉制品中的应用研究

该文详细综述植物蛋白(大豆蛋白、花生蛋白与豌豆蛋白)的持水性、乳化性、凝胶性、吸油性等功能特性,重点综述它们在肉制品加工中所需要的功能特性及应用方法,并展望植物蛋白在肉制品加工中的应用前景.     

蒸谷米糠蛋白乳化性的研究

研究在不同质量浓度、不同温度、不同pH值、不同离子强度、不同蔗糖质量浓度等条件下,蒸谷米糠蛋白的乳化性和乳化稳定性的变化规律,并和大豆分离蛋白做比较。结果发现:蒸谷米糠蛋白乳化性和乳化稳定性均高于大豆分离蛋白,并变化幅度较大;温度、pH值对蒸谷米糠蛋白乳化性和乳化稳定性影响也较大,pH值接近中性可以平衡乳化性和乳化稳定性相互制约。     

Functional properties of raw and heat processed cashew nut (Anacardium occidentale, L.) kernel protein isolates

The functional properties viz. solubility, water and oil absorption, emulsifying and foaming capacities of the protein isolates prepared from raw and heat processed cashew nut kernels were evaluated. Protein solubility vs. pH profile showed the isoelectric point at pH 5 for both isolates. The isolate prepared from raw cashew nuts showed superior solubility at and above isoelectric point pH. The water and oil absorption capacities of the proteins were slightly improved by heat treatment of cashew nut kernels. The emulsifying capacity of the isolates showed solubility dependent behavior and was better for raw cashew nut protein isolate at pH 5 and above. However, heat treated cashew nut protein isolate presented better foaming capacity at pH 7 and 8 but both isolates showed extremely low foam stability as compared to that of egg albumin.     

大豆分离蛋白乳化性影响因素的研究

本文对影响大豆分离蛋白乳化性的外部因素进行了研究,实验证明大豆分离蛋白的乳化能力与蛋白质浓度、加热温度、pH值、NaCl浓度、卡拉胶浓度、搅拌时间密切相关。因此,在表征大豆蛋白的乳化特性及乳化稳定性(ESI)和乳化活性(EAI)时,应考虑这些因素。