不同制备方法桑叶蛋白功能性质的比较

以广东桑大10为原料,采用水提法制备叶蛋白浓缩液,用加热法、酸沉法、酸热法、盐析法沉淀叶蛋白,分别得到蛋白样品RC、SC、SR、LC。对所得样品进行功能性质测定,与大豆分离蛋白对比,得出不同样品的功能特点。结果表明,异亮氨酸、赖氨酸分别为桑叶粉的第一、第二限制性氨基酸。不同沉淀方法对叶蛋白的功能性质有显著影响:LC的溶解性、起泡性、乳化性、吸油性最好,均优于SC、SR及RC;SR的持水性优于SC及RC,但乳化性、起泡性较差;RC、LC的胶凝性最好。与SPI相比,4个样品的吸油性均优于SPI,持水性、胶凝性则显著低于SPI(p0.05);LC的乳化稳定性(68.57%)及SC的起泡性(40%)最好,显著优于SPI(54.86%、37.67%),RC与SPI相当,SR最差,显著低于SPI(p0.05)。LC电镜扫描结果显示其具有典型的蜂巢结构。     

超声处理辅助大豆分离蛋白改善蛋黄乳化性

蛋黄(Egg yolk,EY)的乳化特性易受加工因素影响,为了改善其乳化性能,采用大豆分离蛋白(Soy protein isolate,SPI)辅以超声处理,探究不同超声功率对大豆分离蛋白改善蛋黄乳液乳化性及蛋黄蛋白性能的影响.结果 表明:在EY中添加SPI,可以显著提高EY的乳化活性(Emulsifying acti...     

糖基化大豆分离蛋白对肌原纤维蛋白功能特性的影响

选择70℃条件下反应4 h所得到的糖基化大豆分离蛋白样品(蛋白与葡萄糖质量比1∶1)与肌原纤维蛋白以不同比例(9∶1、8∶2、7∶3、6∶4、5∶5)进行复配,测定不同复合蛋白的乳化性能、浊度、表面疏水性、凝胶特性(质构特性、白度值、微观结构分析),探讨糖基化大豆分离蛋白对肌原纤维蛋白功能性质的影响及其机理。结果表明:复合蛋白的乳化性和表面疏水性均较肌原纤维蛋白显著提升(P0.05);复合蛋白的浊度随着加热温度的升高(30~80℃)而不断增加,随着糖基化大豆分离蛋白比例的加大,浊度不断变小;肌原纤维蛋白与糖基化大豆分离蛋白混合凝胶的硬度和弹性均显著优于其与天然大豆分离蛋白混合凝胶(P0.05),微观结构比其与天然大豆分离蛋白混合凝胶更加致密均匀;与纯肌原纤维蛋白凝胶相比,混合凝胶的白度值下降,但混合比例为9∶1时白度值下降不显著(P0.05)。     

琥珀酰化和棕榈酰化对大豆蛋白界面特性的影响

以琥珀酸酐和棕榈酸N-羟琥珀酰亚胺酯为酰化剂,使琥珀酰基和棕榈酰基与大豆分离蛋白(SPI)共价结合,主要检测了改性程度对SPI溶解性、表面疏水性、乳化性、在油-水界面上的吸附动力学及其界面膨胀流变特性的影响,分析了溶解性和表面疏水性与其界面特性的关系,比较了亲水和疏水改性对大豆蛋白界面特性的影响。研究显示,随着琥珀酰化程度的增加,SPI的水溶性增加,表面疏水性下降,蛋白分子在油-水界面上的吸附速率增加,吸附膜的界面膨胀模量增大,体系的乳化性能得到有效改善;适度的棕榈酰化(酰化程度为30.21%)使SPI的表面疏水性增加,溶解性没有明显降低,蛋白分子在油-水界面上的吸附加快,吸附膜的膨胀模量增大,乳化性能得到一定的改善;而当棕榈酰化程度达50%左右时,溶解性下降到近40%,吸附速率明显降低,乳化体系无法形成;比较而言,亲水的琥珀酰化比疏水的棕榈酰化对SPI界面特性的影响更为明显。因此,共价结合疏水基团使大豆蛋白表面疏水性增加对其界面特性的改善是有限的。     

加工工艺对荞麦蛋白功能特性的影响

探讨了加工工艺对荞麦蛋白(BWP)功能特性的影响。pH＜5．0和 pH＞6．0时,喷雾干燥制备的荞麦蛋白(SBWP)的溶解度高于商品大豆分离蛋白(SPI)(P＜0．05)。pH＜7．0时,超声协助提取荞麦蛋白(U- BWP)的溶解度较搅拌提取荞麦蛋白(M-BWP)和脱脂、超声协助提取荞麦蛋白(DU-BWP)好；pH＞7．0时,结果相反。总体来说,BWP 持油能力较 SPI 强,且冷冻干燥制备的荞麦蛋白(F-BWP)的持水、持油能力强于 S-BWP (P＜0．05)。BWP 的乳化活性与其溶解度呈正相关。pH 4．0～5．0时,BWP 的乳化活性指数(EAI)最小而乳化稳定性(ES)最高。脱脂处理明显提高了 BWP 的 EAI 和 ES。     

高压均质对大豆分离蛋白功能性质的影响

为了了解高压均质技术对大豆分离蛋白（SPI）功能性质的影响,采用不同的均质压力、均质次数和料液比对大豆分离蛋白溶液进行了高压均质处理,并分析处理前后SPI功能性质的变化.结果表明：高压均质可在一定程度上提高SPI的溶解性、乳化活性及其稳定性和起泡性及泡沫稳定性.均质压力在0～70 MPa的范围内升高时,SPI的溶解性、乳化稳定性、起泡性和泡沫稳定性得到了相应的改善,而乳化活性在压力为40 MPa时达到最高;均质次数由1次向3次增加时,SPI的乳化稳定性、起泡性及泡沫稳定性得到了提高,而溶解性和乳化活性则降低;均质物料料液比在1∶16～1∶8 （g∶mL）的范围内逐步增大时,SPI的各项功能性质均有不同程度的提高,并在料液比为1∶8时达到了最高值.     

Improving Functional Properties of Soy Protein Hydrolysate by Conjugation with Curdlan

ABSTRACT:  Soy protein hydrolysate was conjugated with curdlan through the naturally occurring Maillard reaction to extend its application in food processing. The gel-forming and emulsifying properties of soy protein hydrolysates were significantly improved ( P < 0.05) by conjugation with curdlan. The soy protein hydrolysate–curdlan conjugate (SPHCC)–soy protein isolate (SPI) mixed gel had a much thicker network than the soy protein hydrolysate and SPI mixed gel judged from scanning electron microscopic images. The improvement of gelling properties of soy protein hydrolysate by curdlan-conjugate was attributed to both the decrease in the repulsive forces among soy protein hydrolysates and the increase in the solubility. The covalent binding of soy protein hydrolysates and curdlan also showed a profound effect on the antioxidative activity of the soy protein hydrolysates. The higher antioxidative activity of SPHCC was related to the peptide reductants produced from the Maillard reaction and the higher emulsifying property of SPHCC. The conjugates of soy protein hydrolysate and curdlan can be used as a functional food additive having excellent gel-forming, emulsifying properties and antioxidative activity.     

不同方法制备的大豆分离蛋白功能性质的比较研究

采用普通的碱溶酸沉方法、Samoto法、钙离子沉淀法制备出几种大豆分离蛋白,并对其产率、总脂含量及溶解性、乳化性等物化性质和功能性质进行系统比较。结果表明：钙离子沉淀法制备的大豆分离蛋白(Less-LP SPI)的产率是碱溶酸沉大豆分离蛋白(APP)产率的65%,但高于由Samoto法提取的7S与11S两种大豆分离蛋白产率之和;Less-LP SPI的总脂含量比APP降低了45%,由Samoto法提取的亲脂性蛋白(LP)中总脂含量达到7.48%,而7S与11S蛋白中脂含量分别为1.45%、2.36%。在功能性质上,LP的溶解性、乳化活性均比较差,7S、11S质量比1:2混合蛋白的溶解性最好,而Less-LP SPI在pH≤10时溶解性低于APP;乳化性方面,Less-LP SPI的乳化活性稍低于7S、11S质量比1:2的混合蛋白及APP,但乳化稳定性远高于后者。总体上,Less-LP SPI脂含量少、乳化稳定性好,方法简单,且可提高其货架期。     

大豆分离蛋白溶解性和乳化性影响因素研究

研究了pH、大豆分离蛋白(SPI)质量浓度、NaCl浓度、搅拌时间和温度等因素对SPI溶解性和乳化性的影响.结果表明,0.8%的SPI在pH 6.0的条件下,实验浓度范围内的NaCI均使SPI溶解性和乳化性降低,适当的延长搅拌时间和升高温度可以显著提高SPI溶解性和乳化性.在室温条件下,搅拌50 min时SPI溶解度最...     

Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions

The effects of low-frequency (20 kHz) ultrasonication at varying power (200, 400 or 600 W) and time (15 or 30 min) on functional and structural properties of reconstituted soy protein isolate (SPI) dispersions were examined. Ultrasonic treatments reduced both the storage modulus and loss modulus of SPI dispersions and formed more viscous SPI dispersions (fluid character). Moreover, ultrasound treatment significantly decreased the consistency coefficients and increased the flow behaviour index of SPI dispersions. Scanning electron microscopy of lyophilized ultrasonicated SPI showed different microstructure with larger aggregates compared to non-treated SPI. No significant change was observed in the protein electrophoretic patterns by SDS-PAGE. However, free sulfhydryl content, surface hydrophobicity and protein solubility of SPI dispersions were all increased with ultrasonic treatment. Differences in solubility profiles in the presence versus absence of denaturing (0.5% sodium dodecyl sulphate and 6 M urea) and reducing (mercaptoethanol) agents suggested a decrease in non-covalent interactions of SPI in dispersion after ultrasonic treatment. Secondary structure analysis by circular dichroism indicated lower α-helix and random coil in SPI treated at lower power, in contrast to higher α-helix and lower β-sheet in SPI treated with higher power (600 W). In conclusion, under the conditions investigated in this study, ultrasonic treatment resulted in partial unfolding and reduction of intermolecular interactions as demonstrated by increases in free sulfhydryl groups and surface hydrophobicity, leading to improved solubility and fluid character of SPI dispersions, while larger aggregates of ultrasonic-treated SPI in the dry state were formed after lyophilization.     

Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties

Effects of combined extrusion pre-treatment and controlled enzymatic hydrolysis on the physico-chemical properties and emulsifying properties of soy protein isolates (SPI) have been investigated. Results showed that extrusion pre-treatment caused a marked improvement in the accessibility of SPI to enzymatic hydrolysis, resulting in changes in degree of hydrolysis (DH), protein solubility (PS), surface hydrophobicity (H₀) and molecular weight distributions (MWD) for ESPIH (extrusion pre-treated SPI hydrolysates). It was observed that emulsion systems formed by control SPI or SPIH (SPI hydrolysates) (20% v/v oil, 1.6% w/v emulsifier, and pH 7.0) were unstable over a quiescent storage period of 21 days, due to bridging flocculation and creaming. However, ESPIH (9.1% DH) was capable of producing a very fine emulsion (d₃₂ = 0.42 μm, d₄₃ = 2.01 μm) which remained stable over a long term quiescent storage. Various surface properties of ESPIH products have also been studied in relation to DH and emulsifying functionalities. It was suggested that significantly increased protein solubility and decreased molecular weight could be the main reasons for the greatly improved emulsifying capability of ESPIH. This study demonstrated that modified soy protein could be an excellent emulsifying agent for food and other applications. It also demonstrated that combined extrusion pre-treatment and enzymatic hydrolysis could be a highly effective method for functionality modification of globular proteins.     

大豆分离蛋白-黄原胶-茶多酚复合物的制备及其乳液性质表征

以大豆分离蛋白（SPI）、黄原胶（XG）、茶多酚(TP)为原料,改变原料的添加顺序制备三元复合物SPI-XG-TP和SPI-TP-XG,研究了不同复合物的结构与乳化特性的差异。结果表明：蛋白质与多糖、多酚复合之后其结构发生一定程度的改变,且复合物的乳化特性都得到了改善,两种三元复合物中SPI-XG-TP稳定的乳液粒径更小,电位绝对值更大,乳化活性更高,但乳化稳定性略低于SPI-TP-XG稳定的乳液。大分子间能够相互交联形成三元复合物并改变蛋白质的结构,不同原料添加顺序的复合物的结合过程不同     

紫苏分离蛋白功能性研究

为了开发紫苏蛋白在食品工业中的应用,以大豆分离蛋白为对照,研究紫苏分离蛋白的功能特性。结果表明：紫苏分离蛋白的溶解性与大豆分离蛋白的溶解性随pH值变化的趋势基本一致,但在等电点时紫苏分离蛋白的溶解性高于大豆分离蛋白。在pH7.0时,紫苏分离蛋白的持水性、起泡性及泡沫稳定性、乳化性和凝胶性均不及大豆分离蛋白。但紫苏分离蛋白的吸油性仅稍小于大豆分离蛋白,此外,在紫苏分离蛋白的蛋白质质量浓度为3g/100mL以后,其乳化稳定性与大豆分离蛋白的乳化稳定性基本相当。紫苏分离蛋白在食品加工中作为一种蛋白质强化剂具有一定潜力。     

超高压条件下大豆分离蛋白美拉德反应及乳化性质

本文研究超高压（High Hydrostatic Pressure,HHP）条件下,不同压力（0.1、100、200、300 MPa）在60 ℃时,对大豆分离蛋白（Soybean Protein Islates,SPI）与果糖（Fructose,Fru）美拉德反应产物的影响。以接枝度及乳化活性为指标,并分析最佳条件下所得产物以及产物乳状液的结构性质。结果表明在压力200 MPa、质量比0.8:1、反应时间24 h、溶液pH 8.0条件下,产物的乳化活性及乳化稳定性均有提升,乳化活性为(85.36±0.04) m2/g,是SPI与Fru混合物的1.71倍,是SPI的2.17倍,乳化稳定性为(27.66±0.03) min,是SPI与Fru混合物的1.15倍,是SPI的1.40倍。凝胶电泳图分析表明糖分子以共价键的形式接入到SPI分子中。圆二色谱图分析得知在200 MPa的条件下改性SPI二级结构发生改变,内源荧光光谱分析表明在200 MPa的压力可以使SPI的空间结构发生改变。粒径、电位和激光共聚焦显微镜微观图均可表明200 MPa的压力对蛋白乳状液稳定性的提升。     

添加儿茶素对喷雾干燥后的大豆分离蛋白结构、功能性和消化特性的影响

商用大豆分离蛋白（Soybean Protein Isolate,SPI）经高温喷雾干燥处理后,蛋白会发生一定程度的变性聚集,使溶解性等功能性质降低。本研究通过添加不同含量的儿茶素（Catechin,C）,探究儿茶素-大豆蛋白相互作用对喷雾干燥大豆分离蛋白结构和功能特性的影响。结果表明:随着儿茶素添加量的增加,儿茶素的荷载率和装载含量逐渐增加,SPI与儿茶素结合后其表面疏水性和巯基含量逐渐下降;添加儿茶素可有效改善喷雾干燥SPI导致的功能下降问题,在儿茶素添加量为1%时,与对照组SPI相比,溶解性提高了36.4%,乳化性、乳化稳定性分别提高了13.7%和14.3%;在儿茶素添加量为0.25%时,凝胶硬度与对照组相比提高了43.6%,进一步研究发现凝胶网络结构主要依赖于二硫键,其次是氢键、离子键,且此时凝胶流变特性中的储能模量显著高于其他各处理组（P<0.05）;通过原子力显微镜发现,添加儿茶素后凝胶的微观结构向规则均匀致密转化,当儿茶素添加量为0.25%时,复合物凝胶的聚集程度较小,但儿茶素的加入降低了喷雾干燥SPI的消化率。综上所述,在喷雾干燥过程中儿茶素能够与SPI中的基团结合,导致巯基含量和表面疏水性降低,进而干预了蛋白质分子间的热聚集,从而改善SPI的功能特性。     

Functional properties of gelation-like protein hydrolysates from scallop (<Emphasis Type="Italic">Patinopecten yessoensis</Emphasis>) male gonad

Gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad (SMG) were obtained by enzymatic hydrolysis using neutrase. Functional properties of SMG hydrolysates (SMGHs) with different degree of hydrolysis (DH: 4.94, 6.84, 7.53 and 11.86%, respectively) were evaluated with the objective to investigate the relations between hydrolysis characteristics and functionalities. The results showed that hydrolysis with neutrase improved the gelation property, solubility, water-holding capacity (WHC), oil-holding capacity (OHC), and surface hydrophobicity (SH), but not foaming capacity (FC) of SMG. The SMGHs at high DH (11.86%) showed better gelation property and solubility than that at low DH (4.94–7.53%). However, the maximum values of WHC, OHC, and SH of SMGHs were found at DH of 4.94%, significantly higher than (p < 0.05) or equivalent to (p > 0.05) that of soy protein isolate (SPI) for WHC and OHC. Emulsifying capacity of SMGHs is independent of DH, but restricted by pH environment. The emulsifying activity index of all SMGHs was significantly higher than that of SPI in pH 5 (p < 0.05) and slightly higher than or equivalent to that of SPI in pH 7. Meanwhile, SMG and SMGHs were abundant in glycine, lysine, alanine, glutamic acid, and aspartic acid, containing all the essential amino acids (41.63–42.90% of the total amino acids). These results imply that SMGHs might be utilized as multifunctional and nutritive ingredients in food industry.     

减压等离子体处理对大豆分离蛋白功能性质的影响

运用减压等离子体处理大豆分离蛋白(soybean protein isolate,SPI),研究处理时间对SPI溶解性、乳化活性、触变性、热稳定性及表面粗糙度等功能性质的影响。结果表明:经100 W的减压等离子体处理150 s后,SPI的溶解度、乳化活性指数和吸水性均达到最大,分别为572.83μg/mL、0.584 m2/g和12.675 g/g,比对照分别增加约35%、15%和48%;吸油性随着处理时间的延长呈现先降低后上升的趋势,当处理时间为300 s时达到最大值2.071 mL/g,比对照增加了12%;流变学研究表明减压等离子体处理使SPI的黏度有所降低,但未影响其触变性及剪切变稀行为;差示扫描量热分析表明减压等离子体处理略微降低了SPI的热稳定性,扫描电子显微镜观察结果则表明减压等离子体处理增加了SPI颗粒的表面粗糙度。上述研究表明,减压等离子体处理可以改善SPI的溶解性、乳化性、吸水性、吸油性,因此在SPI的改性中具有潜在的应用价值。     

Water‐soluble myofibrillar proteins prepared by high‐pressure homogenisation: a comparison study on the composition and functionality

To expand utilisation of meat in various products, the characterisation and functionalities of water‐soluble myofibrillar proteins (WSMP) induced by high‐pressure homogenisation (HPH) were determined by comparison with those of soy protein isolate (SPI) and whey protein isolate (WPI). WSMP had high contents of protein (87.40%), which was mainly composed of myosin, actin and tropomyosin. The essential amino acids of WSMP achieved the FAO/WHO/UNO (2007) standards for preschool children, and the contents of lysine and sulphur‐containing amino acids of WSMP were higher than those of SPI, making it desirable for children formulations. WSMP showed higher surface hydrophobicity while its water solubility was similar to that of SPI, but lower than that of WPI. WSMP demonstrated superior water/oil absorption capacities and emulsifying properties. The fibrous structure and high hydrophobic activity characteristics of WSMP were able to stabilise oil droplets with submicron droplet size, consequently responsible for its excellent emulsifying properties.     

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.     

Physical properties of emulsion gels formulated with sonicated soy protein isolate

This study aimed to determine the effect of high-intensity ultrasound (HIU) on physical properties of soy protein isolate dispersions (SPI) and their addition to emulsion gels (EG) containing soybean oil (SBO), inulin (IN) and carrageenan (CAR). Sonicated and non-sonicated SPI dispersions were mixed with CAR, IN and SBO and heated at 90 °C for 30 min to gel the emulsion. An increase in solubility and oil binding capacity was observed in sonicated SPI dispersions (S-SPI) compared to the non-sonicated ones. HIU changed the molecular weight of SPI and decreased apparent viscosity in the dispersions. The use of S-SPI in the EG reduced the droplet size and increased the hardness and G′ values. The use of S-SPI allowed a reduction of 75% of carrageenan in the EG without affecting the hardness of the gel. The results suggest that HIU can be used to improve rheological properties of functional EG.