多元醇对大豆蛋白喷雾干燥的影响

研究了不同相对分子质量的多元醇对大豆蛋白喷雾干燥的影响.结果表明:添加多元醇后喷雾干燥所得大豆蛋白的性质发生了明显变化;随着多元醇相对分子质量的增加,大豆蛋白的氮溶指数提高,乳化活性提高,粒径减小,热稳定性提高,热变性程度降低.     

Effect of heat treatment on the properties of soy protein‐stabilised emulsions

The effect of heat treatment on the properties of soy protein‐stabilised emulsions was investigated. Emulsions were prepared with unheated and heat‐treated soy protein (NSP and HSP) dispersions. Heating on soy protein dispersions at 95 °C for 30 min resulted in smaller average oil droplet size, lower tendency for oil droplet flocculation, higher protein adsorption and lower viscosity. The properties of emulsions were significantly influenced by the protein concentration. The sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) profiles showed that the heat treatment on soy protein dispersions increased the protein adsorption at O/W interface. The viscosity of all samples at low shear rate was inversely proportional to the d₃₂, suggesting a positive relation to the total interfacial area per unit volume. Emulsions showed shear‐thinning behaviour. The relaxation time was found to increase with aqueous phase viscosity determined by the Cross viscosity model.     

Effect of soy milk powder addition on staling of soy bread

Effect of soy milk components (soluble fibre (SF), insoluble fibre (ISF), soy protein) on physicochemical properties (crust and crumb colour, water activity, total moisture content, “freezable” water (FW), “unfreezable” water (UFW), amylopectin recrystallisation (ARC), stiffness and firmness) of soy breads stored for 7 days was studied. By the end of storage ISF additions significantly increased ARC (from 0.01 to 0.57 W/g), whereas SF additions (0.30 W/g) retarded staling with respect to soy flour bread (0.39 W/g). Principal Component Analysis (PCA) of all the different treatments and formulations indicated that SMP addition resulted in the lowest firmness and least amylopectin retrogradation at the end of storage, likely due to the synergistic effect of soluble fibre, partly denatured soy proteins and lipid content of this ingredient.     

Thermal stability of soy protein isolate and hydrolysate ingredients

The objective of this study was to characterize the effects of pH, protein concentration and calcium supplementation on thermal stability, at 140 °C, of soy protein isolate (SPI) and soy protein hydrolysate (SPH) ingredients. Increasing pH between 6.4 and 7.5 led to significantly (p < 0.05) higher mean heat coagulation times (HCTs) at 140 °C, for all soy protein ingredients at 1.8, and 3.6% (w/v) protein. Increasing protein concentration from 1.8 to 7.2% (w/v) led to shorter HCTs for protein dispersions. Calcium supplementation up to 850 mg/L, except in the case of supplementation of SPI 1 with calcium citrate (CaCit), decreased HCT for soy protein ingredient dispersions, at pH 6.4 – 7.5. No significant differences (p < 0.05) were found in mean HCT for dispersions supplemented with calcium chloride (CaCl₂) and those supplemented with CaCit at 450, 650 and 850 mg/L Ca²⁺, in the pH range 6.4–7.5.     

Differential scanning calorimetry of lupin and soy proteins

Differential scanning calorimetry (DSC) was used to study the 7S and 11S globulin fractions extracted from lupin seed (Lupinus luteus) flour. In agreement with previous work on other lupin species, the isolate showed three denaturation peaks compared to the two observed with soy. By comparison with the isolated globulin fractions, the denaturation peaks at the two higher temperatures in the lupin isolate were assigned to the 11S and 7S globulins. The denaturation temperature of the lupin 7S globulin was about 10 K higher than that for the corresponding soy globulin, whereas the values for the 11S globulin were similar. All globulins displayed increasing thermal stability with decreasing moisture contents. Possible reasons for the differences in behaviour of soy and lupin protein isolates are discussed.     

Effects of drying conditions on some physical properties of soy protein films

The influence of drying conditions (air temperature and relative humidity) on mechanical properties, solubility in water, and color of two kinds of soy protein isolate film: a commercial one (CSPI) and other obtained under laboratory conditions (LSPI) were evaluated using the response surface methodology (RSM). Soy protein films were prepared by casting using glycerol as plasticizer. The films were dried in a chamber with air circulation under controlled conditions of relative humidity (24%, 30%, 45%, 60%, 66%) and air temperature (34, 40, 55, 70, 76 °C). It was verified that mechanical properties of films made from LSPI and CSPI are influenced in a very different way by the drying conditions due to a diverse initial protein conformation in both materials, as was revealed by DSC and SDS–Page studies. The solubility of the LSPI film was affected by temperature and relative humidity, being lowest (～50%) for films obtained at high RH and temperatures ranging from 45 to 76 °C. For CSPI films, in contrast, solubility did not depend on the drying process and it remained relatively constant (～40%). The optimal drying conditions determined by RSM were: 70 °C and 30% RH for CSPI films and 60 °C and 60% RH for LSPI films. Dried under these conditions, CSPI films presented a higher tensile strength, lower elongation at break, lower solubility and better water and oxygen permeability than LSPI ones.     

大豆分离蛋白薄膜对草莓保鲜效果评价

以大豆分离蛋白复合成膜溶液对草莓进行涂膜保鲜实验,在常温下测定膜液的透光率,并通过草莓的失重率、呼吸强度及感官品质评价了不同涂膜液对草莓的保鲜效果。结果表明,配方为5%的大豆分离蛋白、0.3%的亚硫酸钠、0.2%的Tween-80、3%的甘油和1%的油酸的复合膜保鲜效果良好,大豆分离蛋白薄膜能够明显减弱草莓的蒸腾作用,降低烂果率并抑制其呼吸强度。     

预热变性程度对大豆蛋白凝胶性质的影响

以非还原SDS-PAGE表征大豆蛋白的预热变性程度,并采用质构分析、流变分析研究预热变性程度对大豆蛋白凝胶性质的影响。SDS-PAGE结果表明,随着加热温度的升高蛋白质变性速率逐渐增大,相同加热时间条件下,蛋白质变性程度随加热温度升高呈S型曲线上升。质构、流变分析结果表明:随着预热变性程度的增大,大豆蛋白凝胶硬度先增大后减小,变性程度为86.11%时凝胶硬度最大,是未经预热变性的大豆蛋白凝胶硬度的2.15倍;凝胶弹性则随预热变性程度的增大持续增大;变性程度在22.28%以上时大豆蛋白形成凝胶更快,但完全变性大豆蛋白在形成凝胶时的降温阶段不能形成很好的凝胶结构。粒径分析结果表明,预热变性程度对大豆蛋白凝胶性质的影响与蛋白质预热变性时形成的聚集体尺寸及形态有关。     

Protein and glycerol contents affect physico-chemical properties of soy protein isolate-based edible films

This study was conducted to determine the effect of both soy protein and glycerol contents on physico-chemical properties of soy protein isolate-based edible (SPI) films. The aim of this study was to better understand the influence of SPI and GLY contents on the behavior of the physico-chemical properties of soy protein isolate-based films. Films were casted from heated (70 °C for 20 min) alkaline (pH 10) aqueous solutions of SPI at 6, 7, 8, and 9 (w/w %), glycerol (50%, w/w, of SPI) and SPI at 7 (w/w %), glycerol (40, 60, 70 %, w/w of SPI). Water vapor permeability (WVP), was measured at 25 °C and for four different relative humidities (30–100%, 30–84%, 30–75%, 30–53%). Surface properties and differential scanning calorimetry were also measured. Varying the proportion of SPI and GLY had an effect on water vapor permeability, wetting and thermal properties of SPI films. A synergistic effect of glycerol and protein was observed on the water vapor permeability. Glycerol and RH gradient strongly enhance the moisture absorption rates and permeability of SPI based films. SPI content weakly increases the WVP and does not modify the surface properties. The temperature of denaturation of soy protein decreases glycerol content except for the higher concentration whereas it increases with protein ratio.Industrial relevanceThis topic of research aims to control mass transfers within composite foods or betweenfoods and surrounding media (for instance the headspace in packagings). The targeted applications from this work deals with the food product coating or the coating of paper-based packaging for limiting both the loss of water and flavors by cheese based products. This will allow to maintain the weight of the cheese during “ripening” and commercialization, and also to prevent (off-) flavour dissemination from very odorant cheese as produced in France and Poland.     

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.     

Enhanced bactericidal action and masking of allergen structure of soy protein by attachment of chitosan through Maillard‐type protein‐polysaccharide conjugation

The soy protein‐chitosan conjugate was formed by the Maillard reaction in dry state (relative humidity 65%) at 60°C for 2 weeks to improve the functional properties. The antimicrobial activity of the Maillard‐type soy protein‐chitosan conjugates enhanced 2–3 times that of soy protein‐chitosan mixture. The soy protein‐chitosan conjugate showed excellent emulsifying property with the progress of Maillard‐type conjugation. The allergenicity of soy protein was greatly decreased by the attachment of chitosan through Maillard reaction. The immonoblotting analysis with patient's sera revealed that soy protein‐chitosan conjugate was more effective to mask the allergen structure of soy protein causing from 34 kDa‐protein (Gly m Bd 30K) than soy protein‐galactomannan conjugate. The Western blotting showed that allergen (34 kDa‐protein) was completely masked by soy protein‐chitosan conjugation, while it was not completely masked by soy protein‐galactomannan conjugation.     

Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures

Microbial transglutaminase (MTGase)-catalyzed interaction and gelation of mixed myofibrillar (MPI)/soy (SPI) protein isolates were investigated at varying ionic strengths and MPI:SPI ratios, with or without SPI being preheated (80?°C). MTGase treatments in deionized water converted myosin heavy chain and actin into lower molecular-weight polypeptides, which gradually diminished as the ionic strength increased up to 0.6 M NaCl. A reduced intensity in the electrophoretic bands of soy proteins (7S and 11S except the basic subunits) was observed in all treatments, suggesting cross-linking with MPI. The enzyme treatment slightly increased the thermal transition (denaturation) temperatures of MPI/SPI but greatly enhanced (P<0.05) the elasticity of the mixed protein gels when compared with untreated samples, independent of incubation time.     

大豆肽的超滤分离及其清除自由基活性研究

采用不同截留相对分子质量的超滤膜进行超滤分离大豆分离蛋白酶解液,研究超滤过程中操作压力、料液质量浓度、超滤时间对超滤膜通量的影响,确定最佳超滤条件,并测定各超滤级分清除·OH与DPPH·的能力。结果表明:在操作压力0.2 MPa、料液质量浓度50 g/L、通过相对分子质量为10、3、1 k D超滤膜的操作时间80 min、通过相对分子质量为5 k D的超滤膜的操作时间100min的超滤条件下分离大豆肽,超滤效果较好;相对分子质量小于3 k D的小分子大豆肽具有较高的自由基清除率,且对于·OH与DPPH·的清除率具有较高的一致性。     

Tracking isoflavones: From soybean to soy flour,soy protein isolates to functional soy bread

Soybean seeds with three different levels (low, intermediate and high) of isoflavones were processed to soy flour and soy protein isolates (SPIs) and developed into functional soy breads. The effect of factors involved in all steps of the process was investigated by tracking the composition and concentration of native forms of isoflavones. The total isoflavone contents were 8033.3, 10570.1 and 15169.0 nmol/g DM (dry matter) in the three soybeans; 13201.5, 20034.4 and 26014.3 nmol/g DM in defatted soy flours; 9113.2, 13274.6 and 17918.3 nmol/g DM in the SPI; 2782.7, 4081.4 and 5590.3 nmol/g DM in soy breads, respectively. The bread making processes did not affect the total isoflavone content, but changed glucosides/acetylglucosides to aglycones. Malonylglucosides were stable prior to baking but degraded to acetylglucosides and further to glucosides during baking. Our results provide critical information for the production of functional soy breads that contain varying amounts of soy isoflavones.     

Effects of oxidative modification on thermal aggregation and gel properties of soy protein by peroxyl radicals

Effects of protein oxidation on thermal aggregation and gel properties of soy protein by 2,2′‐azobis (2‐amidinopropane) dihydrochloride (AAPH)‐derived peroxyl radicals were investigated in this article. Incubation of soy protein to increase concentration of AAPH resulted in a decrease in particle size and content of thermal aggregates during thermal‐induced denaturation. Protein oxidation resulted in a decrease in water‐holding capacity (WHC), gel hardness and gel strength of soy protein gel. An increase in coarseness and interstice of the gel network was accompanied by uneven distribution of interstice as extent of oxidation of soy protein increased. A decrease in disulphide content and formation of oxidation aggregates in the process of oxidative modification were contributed to the decline of particle size and content of thermal aggregates during thermal‐induced denaturation, leading to a decrease in WHC, gel hardness and gel strength of soy protein gel.     

Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction

The functional acid-precipitated soy protein (SAPP)–dextran conjugate was prepared by dry-heated storage at 60 °C under 79% relative humidity (RH) for 5 days through Maillard reaction between the ε-amino of lysine in soy proteins and the reducing-end carbonyl residue in the dextran. The covalent attachment of dextran to SAPP was confirmed by SDS-polyacrylamide gel electrophoresis and gel filtration chromatography. Functional properties of soy protein depend on the structural and aggregation characteristics of their major components (storage globulins 7S and 11S). The conjugate seemed to be predominantly formed by 7S, and the acidic subunits of 11S in soy protein. The emulsifying properties of the SAPP–dextran conjugate were about four times higher than those of SAPP. The solubility of the protein was not enhanced as a result of preheating, but rather it was not decreased when the conjugated protein was heated at 90 °C for 20 min due to the presence of the polysaccharide. The excellent emulsifying properties of SAPP–dextran conjugate were maintained even at pH 3.0 and were further improved at pH 10.0. The object of Maillard reaction is to guarantee the suitable reaction degree, and the resulting soluble conjugate can have excellent emulsifying properties.     

亚油酸氢过氧化物氧化修饰对大豆蛋白热变性和聚集的影响

以亚油酸氢过氧化物代表脂质氢过氧化物氧化修饰大豆分离蛋白,采用圆二色光谱、内源荧光光谱、粒径分析以及相对分子质量分布研究氢过氧化物氧化修饰对大豆蛋白热变性和聚集的影响.结果发现亚油酸氢过氧化物氧化修饰使得大豆蛋白热稳定性下降,热变性过程中形成聚集体粒径随着蛋白质氧化程度的升高呈现先增加后减小的趋势,热变性大豆蛋白冷却后的粒径和聚集体含量则随着蛋白质氧化程度的增加而下降.     

Assessment of the effects of soy protein isolates with different protein compositions on gluten thermosetting gelation

Although soy proteins are known to have a deleterious effect on gluten thermosetting gelation, the causes are still poorly understood. Different sources of soy protein isolates (SPI) were used to investigate the interactions between gluten and soy proteins during hydro-thermal treatments. Commercial SPI and isolates prepared from soybean lines with different subunit composition were used to study the influence of protein denaturation and subunit composition on thermoset gel formation. Rapid Visco Analyser analysis showed that replacement of gluten with more than 1% SPI decreased the peak viscosity and interfered with formation of thermoset gels. However, peak viscosity was higher for 11% gluten + 2% SPI than for 11% gluten alone, suggesting a cooperative effect. After heating and cooling, 11% gluten + 2% SPI rich in A1 and A2 subunits formed a coherent thermoset gel suggesting that the cysteine residue content of soy proteins can affect gel formation.     

Pectin stabilization of soy protein isolates at low pH

The stabilizing behaviour of pectins in acidified dispersions of soy protein was studied. Objective of this work was to understand if different soy isolates and different pectins show differences in stability. The behaviour of a commercially available isolated soy protein (ISP) was compared to that of a soy protein in the laboratory. At pH 3.8 while suspensions of commercial ISP showed significant precipitation, the native SPI (prepared in the laboratory) was much more stable against precipitation. High methoxyl pectin (HMP) had better stabilization behaviour than low methoxyl pectin (LMP). A higher amount of HMP was needed to avoid protein precipitation of native SPI, compared to that used for commercial ISP. It was demonstrated that at low pH pectin forms soluble complexes with SPI through electrostatic interactions.     

High-pressure treatment effects on proteins in soy milk

Effects of high-pressure treatment on the modifications of soy protein in soy milk were studied using various analytical techniques. Blue shifts of λ_max could be observed in the fluorescence spectra. Spectrofluorimetry revealed that the soy protein exhibited more hydrophobic regions after high-pressure treatment. Electrophoretic analysis showed the change of soy protein clearly and indicated that soy proteins were dissociated by high pressure into subunits, some of which associated to aggregate and became insoluble. High-pressure denaturation occurred at 300 MPa for β-conglycinin (7S) and at 400 MPa for glycinin (11S) in soy milk. High pressure-induced tofu gels could be formed that had gel strength and a cross-linked network microstructure. This provided a new way to process soy milk for making tofu gels.