豌豆粉丝厂废水中蛋白质的提取和性质研究

本论文以豌豆粉丝厂废水中的蛋白为原料提取豌豆分离蛋白,通过对提取工艺进行研究,确定了在pH12.0,固液比1∶20(g/mL),30℃下提取30min的提取条件,提取率达到62.25%。氨基酸分析结果表明,所提豌豆分离蛋白(PPI)氨基酸没有遭到破坏,营养价值较高。通过对PPI功能性质研究发现,除了吸水吸油性外,PPI的乳化性、乳化稳定性、起泡性都和大豆分离蛋白(SPI)接近。由此可见,PPI可以作为SPI的替代品应用于食品,具有很大的实用价值。采用DSC研究了PPI的热力学性质,在87.67℃(7S)和104.28℃(11S)有两个峰,这可能是在碱溶酸沉过程中,蛋白结构发生了一定变化造成的。     

影响豌豆蛋白乳化特性的分子机制

为了解豌豆蛋白的乳化特性及影响其乳化特性的分子机制,实现豌豆蛋白的高效应用,以豌豆蛋白粉为原料,与大豆油用高压均质法制备乳液,测定豌豆蛋白的乳化能力及稳定性,并考察其在乳液中的界面吸附特性及组分的竞争吸附。结果表明,在蛋白浓度1.0~30.0 mg/mL时,随着蛋白浓度的增加,界面吸附蛋白量显著上升,蛋白聚集体在竞争吸附中失去优势,7S和11S球蛋白的占比逐渐提高,乳液粒径降低,且乳化能力和稳定性增强;蛋白浓度≥20.0 mg/mL时,乳液平均粒径低至1.06μm,蛋白界面吸附趋于饱和状态,且7S球蛋白在竞争吸附中占明显优势,11S球蛋白次之,聚集体占比较低,且略低于原蛋白组成。     

热处理对大豆球蛋白乳化性的影响

分离纯化出7S、11S、SPI球蛋白,采用热处理三种球蛋白,考察热变性对蛋白乳化性及蛋白形成乳液的稳定性影响.结果表明,90℃热处理5min后SPI的乳化性达到最高,而在此变性条件下其组分7S的乳化性明显降低,11S的乳化性升高;热变性后SPI形成的乳液稳定性增强,7S乳液稳定性降低,11S乳液稳定性升高;热处理使蛋白发生不同程度变性,导致蛋白结构发生变化,蛋白乳化性改变,进而影响乳液性质.     

干燥方式对pH改性豌豆分离蛋白功能性和结构的影响

以豌豆为原料制备豌豆分离蛋白(PPI),比较了常用的两种干燥方式对pH改性PPI功能性的影响,并利用SDS-PAGE和红外光谱法研究了两种干燥方式对pH改性PPI结构的影响。研究结果表明:与冷冻干燥相比,喷雾干燥使改性处理后的PPI形成较多聚集体,同时使蛋白质的功能性质(溶解性、乳化性、胶凝性)略微降低;经过pH改性处理喷雾干燥PPI的乳化性和胶凝性显著高于未改性处理冷冻干燥PPI,喷雾干燥后PPI亚基发生更多的非二硫键共价聚集,使PPI发生部分变性,二级结构发生了变化。总之,喷雾干燥对PPI的功能性质有降低趋势,而pH改性处理可以大大改善PPI的功能性质从而弥补喷雾干燥带来的不足。     

Thanh法提取7S、11S球蛋白功能特性的研究

以中豆36为原料,分别提取大豆分离蛋白(SPI)、7S、11S球蛋白,系统地比较了它们的功能性质的差异。结果表明:SPI、7S及11S的功能特性之间存在较大差异,11S球蛋白具有较强的凝胶性、吸油性和溶解度;7S球蛋白具有较高的持水性和乳化性。     

极端pH处理对大豆分离蛋白、β-伴大豆球蛋白、大豆球蛋白结构和功能特性的影响

为丰富大豆蛋白柔性改性技术,采用极端pH条件(pH 1,2,3,4,10,11,12,13)处理大豆分离蛋白(SPI)、β-伴大豆球蛋白(7S)和大豆球蛋白(11S)。通过对SPI、7S和11S蛋白进行凝胶电泳分析、氨基分析、巯基分析和色氨酸荧光分析,并测定大豆蛋白表面疏水性、溶解性、乳化性和起泡性,探讨极端pH处理对SPI、7S和11S结构和性质的影响。结果表明:极端pH处理可导致SPI、7S和11S游离氨基和内源色氨酸荧光强度增加,蛋白表面疏水性提高,三级结构部分展开。此外,极端pH处理可诱导SPI与11S亚基部分解离,而对7S亚基影响较小。极端pH处理能够提高SPI、7S和11S蛋白溶解性、乳化性和起泡性。11S球蛋白可能是SPI结构变化和功能特性改善的主要贡献者。由此可见,极端酸碱处理通过诱导大豆蛋白高级结构的展开,改善其功能特性。     

大豆种子贮藏蛋白亚基特异种质的蛋白功能性评价

以4个蛋白亚基变异类型大豆品种(系)制备的分离蛋白和南农大黄豆粗7S蛋白为材料,以亚基正常品种南农大黄豆制备的分离蛋白为对照,对其溶解性、凝胶质构特性、乳化性、乳化稳定性以及DSC特性进行了测定.结果表明,11S组分单个亚基缺失对大豆蛋白的溶解性、乳化性、乳化稳定性和热稳定性影响不显著;11S组分含量显著降低或缺失能提高大豆蛋白的乳化性和乳化稳定性,但降低大豆蛋白变性温度和变性焓;在凝胶质构特性方面,7S组分含量与凝胶弹性呈显著正相关,11S组分含量与凝胶内聚性呈极显著正相关,与凝胶硬度、胶黏性和破裂强度呈显著正相关,与凝胶弹性呈极显著负相关.     

大豆7S球蛋白脱敏后功能特性研究

大豆蛋白拥有各种功能特性且广泛用于食品加工中,但大豆蛋白也是主要的致敏原。本文主要对脱敏后大豆7S球蛋白的乳化性、起泡性、表面疏水性和溶解性进行研究,并与脱敏前的大豆7S球蛋白、大豆11S球蛋白以及大豆分离蛋白的功能特性进行比较,结果显示。脱敏后的7S球蛋白溶解性增加。乳化性与大豆分离蛋白相当。起泡性和泡沫稳定性降低。     

葵花蛋白的分离及特性研究

通过盐提酸沉法提取葵花籽中的分离蛋白,通过盐溶盐析法分离其主要蛋白成分11S球蛋白,对葵花分离蛋白和其主要成分葵花11S球蛋白的溶解性、吸水性、吸油性、乳化性和起泡性进行研究并与大豆分离蛋白进行比较,发现葵花分离蛋白其功能特性都好于或接近大豆分离蛋白.葵花分离蛋白凝胶层析有5个峰,3个主峰的分子量分别380000、100000和27000,最大的主峰和葵花11S球蛋白吻合.对葵花分离蛋白和11S球蛋白进行电泳分析,发现11S球蛋白含有10条主带,是葵花分离蛋白主要成分.     

食用豆类球蛋白研究进展

该文比较分析大豆、绿豆、豌豆、蚕豆等蛋白含量及组成,就豆类蛋白主要成分―11S球蛋白、7S球蛋白和8S球蛋白亚基结构及性质,球蛋白提取方法及功能特性进行概述,并展望其研究发展趋势,以期为豆类球蛋白进一步研究及应用提供参考。     

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.     

植物球蛋白/姜黄素纳米复合物的制备及其对O/W型Pickering乳液氧化稳定性影响

本论文以两类植物球蛋白:豌豆分离蛋白(PPI)和大豆分离蛋白(SPI)为材料制备荷载姜黄素蛋白纳米复合物,并探究荷载前后蛋白所制备乳液的物理和氧化稳定性差异。结果表明:PPI和SPI在pH 3.0和pH 7.0下荷载前后蛋白纳米颗粒粒径没有明显变化。pH 7.0时两蛋白姜黄素荷载量均高于pH 3.0,各pH下SPI荷载量要高于PPI。表面疏水性的显著降低与荧光淬灭现象发生表明形成两种蛋白纳米复合物的主要作用力为疏水相互作用,同时在两pH下,PPI比SPI荧光蓝移趋势更明显且有效淬灭常数也更大,即更易形成复合物。与原蛋白相比,荷载后各蛋白颗粒所制备乳液乳化活性有少许降低,同时pH 3.0时各蛋白颗粒乳化活性要高于pH 7.0。各乳液生成初级氧化产物脂质氢过氧化物浓度的变化趋势与生成次级氧化产物TBARS相类似,均为荷载姜黄素后各乳液氧化水平加速,同时pH 3.0时各类型乳液油滴氧化程度均高于pH 7.0。     

Functional properties and structural characteristics of phosphorylated pea protein isolate

In order to expand the application of pea proteins in the food industry, pea protein isolate (PPI) was chemically phosphorylated to improve its functional properties. Based on the comprehensive membership value (CMV) degree, the optimal condition for PPI phosphorylation modification was as follows: pH 12, modification temperature at 70 °C and an addition of 7.0% (w/v) sodium tripolyphosphate (STP). Under this condition, the solubility, emulsifying property, emulsifying stability, foaming property and oil absorption capacity of the modified PPI were improved substantially. In addition, the structure of modified PPI was characterised by scanning electron microscope (SEM) and Fourier transform infrared (FTIR) spectroscopy. The results showed that the modified PPI had a smooth and uniform lamellar structure, where the content of α-helix and β-sheet structure increased, but the content of β-corner and random coil structure decreased. The thermodynamic properties were analysed by differential scanning calorimetry (DSC) and the results showed that ∆H of the modified PPI increased significantly. Finally, the optimum phosphorylated PPI was mixed with 0.4% (w/v) xanthan gum to form PPI fat mimics (PPI-FM). PPI-FM was added into mango mousse cake to reduce the amount of light cream, and the result showed up to 20% of light cream could be substituted.     

Effect of denaturation during extraction on the conformational and functional properties of peanut protein isolate

Peanut protein isolate (PPI) was extracted by alkali dissolution and acid precipitation from defatted peanut flour. The effects of extraction conditions on the denaturation and functional properties of PPI were investigated. In comparison with native peanut protein (NPP) which was extracted by ammonium sulfate, the PPI extracted by alkali dissolution and acid precipitation had a higher extent of denaturation. Arachin was affected more easily by the extraction process than conarachin and led to a noticeable decrease of thermal stability of PPI. PPI contained much lower sulfhydryl and disulfide bond contents than NPP. The analyses of intrinsic fluorescence spectra indicated a more compacted tertiary conformation of NPP than PPI. Extraction process influenced the functional properties of PPI, such as protein solubility, emulsifying activity index and foaming capacity. The relatively poor functional properties of PPI might be associated with protein denaturation/unfolding and subsequent protein aggregation.

Industrial relevance

Peanut is an important oilseed crop and a well-accepted food. After oil production through thermal treatment, the defatted peanut flour is the main byproduct, which possesses a large amount of proteins. However, due to the low extraction yield and poor functional properties of these proteins, they are not well utilised in industry till now. In this work, peanut proteins were extracted by two techniques. The results indicated that extraction technique could significantly modify the functional properties of peanut proteins. Therefore, this work is helpful for industrial utilisation of peanut proteins.     

Effects of AOT reverse micelle on properties of soy globulins

This study was focused on the influence of AOT reverse micelle on physical–chemical properties of 7S and 11S globulins from soy proteins, and compared with aqueous buffer extraction. The results showed that the contents of the surface hydrophobicity and SH groups of 7S and 11S globulins and SS bonds of 11S globulin, using AOT reverse micelle extraction, were augmented, and SS bonds of 7S globulin decreased. The thermal and rheological properties of 7S and 11S globulins extracted using the two methods were studied by differential scanning calorimetry (DSC) and rheometery. It was found that the peak denaturation temperature and heat of transition of 7S and 11S globulins with aqueous buffer extraction were different from that with AOT reverse micellar extraction. The AOT reverse micelle did not affect the gel properties of 11S globulin, while it influenced 7S globulin’s. Hardness, springiness, gumminess, adhesiveness and chewiness of 7S globulin from AOT reverse micelle were lower than that from aqueous buffer extraction, but gumminess was higher.     

Effect of succinylation on the functional and physicochemical properties of α‐globulin,the major protein fraction from Sesamum indicum L.

α‐Globulin the major protein fraction fromSesamum indicum was succinylated to different levels and the effect of the chemical modification was evaluated both on the functional and physicochemical properties. The results suggest that the pH of minimum solubility shifted to the more acidic side (pH ˜ 4.5–5.5) for the succinylated α‐globulin whereas for control α‐globulin the pH of minimum solubility was 6.5. Succinylation also increased emulsion activity and emulsion stability of the protein. The emulsion stability increased from a control value of 53 ± 3 s to a value of 122 ± 5 s. Bulk density, water absorption capacity, oil absorption capacity, foam capacity and foam stability were evaluated in phosphate buffer (pH 7.0) containing 0.5 M sodium chloride and all these properties showed increased values as a result of succinylation. Ultracentrifugation studies showed that the % composition of 7S component increases with concomitant decrease in that of 11S fraction with the increase in percentage of succinylation. Further increase in succinylation resulted in only 2S component which is a dissociated form of 11S and/or 7S protein fractions. The fluorescence emission studies showed a decrease in the fluorescence emission intensity of α‐globulin as a result of succinylation. The thermal stability of the protein molecule decreased due to progressive succinylation as indicated by decrease in the apparent thermal denaturation temperature from a control value of 84 to 62°C at a succinylation level of 40%. These results suggest that succinylation improves the functional characteristics of α‐globulin. Such changes in the functional properties have been attributed partly to the dissociation of the protein molecule at higher levels of succinylation and the increase in the net negative charge on the protein.     

Dynamic oscillatory rheological measurement and thermal properties of pea protein extracted by salt method: Effect of pH and NaCl

The effects of two important factors, pH (3.0-10.0) and NaCl (0-2.0 M), on pea protein gelation properties were studied using dynamic oscillatory rheometer and differential scanning calorimeter (DSC). The strongest gel stiffness was achieved at 0.3 M NaCl; higher or lower salt concentrations lead to weakening of the gel. The gelation temperature was also influenced by ionic strength; salt had a stabilization effect which inhibited pea protein denaturation at higher salt concentrations resulting in higher gelling points (p < 0.05). At a NaCl concentration 2.0 M, pea protein gelation was completely suppressed at temperatures ?100 °C. The pH also played an important role in gel formation by pea protein isolates since acid and base cause partial or even total protein denaturation. In this paper the maximum gel stiffness occurred at pH 4.0 in 0.3 M NaCl; higher or lower pH values resulted in reduced gel stiffness (p < 0.05). pH also altered the denaturation temperature of the pea protein; higher pH values resulted in higher denaturation temperatures and higher enthalpies of denaturation (p < 0.05). At pH 3 pea proteins seem like completely denatured by acid as the DSC curve showed a straight line. The gelation temperature (gelling point) peaked at pH ∼6.0 (89.1 °C). Careful adjustment of pH and NaCl concentration would enable the food industry to effectively utilize the salt-extracted pea protein isolate as a gelling agent.     

Differential scanning calorimetric study of meals and constituents of some food grain Legumes

Two thermal transitions were observed in soya bean meal by differential scanning calorimetry (DSC) and on the basis of previous data were ascribed to the denaturation of the 11S globulin, glycinin, and the 7S globulin, β-conglycinin. Three DSC transitions were apparent in Vicia faba meal; one was associated with starch gelatinisation, and was absent from thermograms of soya bean because the latter stores oil rather than starch. The remaining two transitions were identified with the 11S globulin, legumin, and a 7S globulin, vicilin. The denaturation parameters of legumin and glycinin were very similar, in contrast to those of vicilin and β-conglycinin. From this it was concluded that legumin and glycinin probably represent homologous proteins, whereas the two 7S proteins possess intrinsically different structures to one another. Cowpeas (Vigna unguiculata) and dry beans (Phaseolus vulgaris) afforded two major transitions which were assigned to 7S globulins and starch. From its DSC profile, the 7S globulins of cowpea appeared heterogeneous, but nevertheless possessed denaturation characteristics similar to those of vicilin of V. faba. In contrast, the thermal behaviour of the 7S globulin of dry beans (glyco-protein II) was distinct from that of any of the other 7S globulins investigated. Three protein transitions were observed in the three lupin species examined. As in the case of soya bean, no starch transition was present. On the basis of the correspondence in transition temperature, one of the protein transitions was assigned to the 11S globulin component. Overall, this study indicates the potential of DSC as a means for obtaining data on seed protein homology from whole meals rather than the extracted proteins.     

酰化对大豆蛋白分子结构影响的研究

目的:研究化学改性对大豆分离蛋白(SPI)分子结构的影响;方法:采用SDS-PAGE电泳、DSC热分析手段探讨酰化对蛋白分子结构特征的影响;结果:DSC图谱显示,SPI经过琥珀酰化处理后热稳定性得到显著改善,乙酰化处理对大豆蛋白的热稳定性影响不大。SDS-PAGE电泳结果显示,改性后蛋白的11S酸性亚基和7S含量大大减少,说明SPI经酰化处理后亚基发生了降解。随着酸酐添加量的增大,11S球蛋白分子逐步分解为亚基。琥珀酰化的电泳图谱预示着可能存在一个琥珀酰化的临界点,在这一点上,解离的蛋白亚基突然展开。结论:实验结果有助于阐明SPI酰化后功能性质发生变化的内在结构因素。     

Physicochemical, functional and angiotensin converting enzyme inhibitory properties of amaranth (Amaranthus hypochondriacus) 7S globulin

BACKGROUND: Amaranth 7S globulin is a minor globulin component and its impact on the properties of an amaranth protein ingredient depends on its proportion in the variety of amaranth being considered. Some physicochemical, functional and angiotesin I‐converting enzyme (ACE) inhibitory properties of amaranth vicilin were studied in this work and compared with the 11S globulin. RESULTS: Fluorescence spectroscopy results indicated that 7S globulin tryptophans were more exposed to the solvent and, by calorimetry, the 7S globulin denaturation temperature (T_d) was found lower than the 11S globulin T_d, suggesting a more flexible structure. The 7S globulin surface hydrophobicity was higher than that of the 11S globulin, which is in agreement with the better emulsifying properties of the 7S globulin. The solubility in neutral buffer of the 7S globulin (851 ± 25 g kg^?1) was also higher than that of the 11S globulin (195 ± 6 g kg^?1). Bioinformatic analyses showed the presence of ACE inhibitory peptides encrypted in 7S tryptic sequences and peptides released after in vitro gastrointestinal digestion showed a high ACE‐inhibitory capacity (IC₅₀ = 0.17 g L^?1), similar to that of 11S globulin peptides. CONCLUSION: Compared with the 11S globulin, the 7S globulin presents similar ACE inhibitory activity and some functional advantages, better solubility and emulsifying activity, which suits some food requirements. The functional behavior has been related with the structural properties. Copyright © 2011 Society of Chemical Industry