Effect of arabic gum and xanthan gum on the stability of pesticide in water emulsion

The effect of arabic gum (AG) and xanthan gum (XG) on the physicochemical properties of 2% pesticide avermyctin in water emulsions was systematically investigated by measuring creaming stability, droplet size, zeta potential, and rheology. Addition of AG and XG had significant influence on the physicochemical properties of emulsions. Emulsions showed high stability throughout the storage time in the AG concentration range of 0-0.14%. In contrast, addition of XG induced the apparent creaming of emulsion as the XG concentration increased from 0.011 to 0.15%, which might be well explained by the depletion flocculation of droplets. The droplet diameter increased progressively with increasing AG concentration; however, it sharply grew initially with XG concentration and reached a maximum, followed by a gradual decrease. Zeta potential increased gradually as AG concentration was lower than 0.081%, followed by a slight decrease, whereas it reduced dramatically as XG concentration increased from 0.011 to 0.040% and then remained almost unchanged. In the AG concentration range of 0-0.14%, the emulsion exhibited typical Newtonian flow behavior and the viscosity decreased a little. The XG emulsion exhibited Newtonian flow behavior at low XG concentrations (≤0.019%), whereas, non-Newtonian flow behavior was displayed at relatively high XG concentrations (>0.019%), wherein viscosity value and yield value increased gradually as XG concentration increased. In addition, the curves of shear stress versus shear rate for XG emulsion and solution were well fitted by a power law model and the Herschel-Bulkley model; the Herschel-Bulkley model fitted much better. The present study would provide useful information for the reasonable application of AG and XG in making stable pesticide emulsion.     

延长黄原胶缓释期的技术研究

【目的】研究了水杨酸(SA)在黄原胶(XG)及聚乙烯醇(PVA)为主要材料的基质型缓释系统中的释放速率。【方法】共设计了29个配方,分为4组:XG + PVA + SA、XG + PVA + 醋酸酯淀粉(AS) + SA、XG + PVA + 硬脂酸 + SA、XG + PVA + 壳聚糖(CS) + SA。根据设计的配方将材料研磨混匀后以聚乙烯醇溶液为粘合剂进行造粒。首先制作了6～10 mm五种造粒直径的缓释颗粒,并以4%、5%、6% (w/v)三种浓度的PVA溶液分别造粒,研究了造粒大小、PVA溶液浓度对颗粒释放行为的影响。确定造粒条件后研究了四种配方不同配比对颗粒释放行为的影响,采用静水溶出法和土柱淋溶法对释放行为进行表征,以水杨酸的释放率及累积释放量为指标绘制释放曲线。【结果】所制缓释颗粒的水杨酸释放曲线都遵循一个趋势:水杨酸释放率在前一段时间呈快速增长,转折点之后增长速度趋于平缓。根据试验结果分析,粗粒径的黄原胶溶胀更缓慢,对内容物的释放也会更慢。缓释颗粒直径较小时最终释放的百分比更高但由于比表面积大释放也更快,颗粒直径过大时最终释放的百分比会降低且持续时间也不会延长,最终选定造粒直径8 mm。对粘合剂PVA溶液的使用量的研究结果显示,在选取的三种PVA溶液浓度中,以浓度为4%的PVA溶液进行造粒、混合粉末与4%PVA溶液的比例(w/w)以1.1∶1为宜。四种不同组成的配方经优化后缓释效果最好的比例分别为:XG∶SA = 3∶1,在去离子水中释放持续约2.5天;XG∶AS∶SA = 3∶1∶1,在去离子水中释放持续时间2.5天;XG∶硬脂酸∶SA = 1∶1∶1,去离子水中持续时间约为3天;XG∶CS∶SA = 3∶1∶1,在去离子水中可持续4天,而在土柱中释放持续可达36天左右。【结论】使用0.178 mm粒径的黄原胶粉末,在XG∶CS∶SA = 3∶1∶1,造粒直径8 mm,以4% PVA溶液进行粘合造粒的条件下,所得缓释颗粒的土柱淋溶释放时间可长达36天,为本试验所得释放时间最长的缓释体系。该缓释系统成本较低廉,制作方法简单,对环境友好。     

Plasma-enhanced modification of xanthan gum and its effect on rheological properties

The structure and rheological properties of xanthan gum (XG) modified in a cold plasma environment were investigated. XG was functionalized in a capacitively coupled 13.56-MHz radio frequency dichlorosilane (DS)-plasma conditions and, consecutively, in situ aminated by ethylenediamine. The surface structure of modified XG was evaluated on the basis of survey and high-resolution ESCA, FTIR, and fluorescence labeling techniques. The types of species generated in DS-plasma were reported using residual gas analysis (RGA). The aqueous solutions of modified XG were cross-linked and cured at room temperature to form stable gels. The dynamic rheological characteristics of virgin XG and functionalized and cross-linked XG were compared. It was found that parameters such as plasma treatment time and concentration of solutions can be optimized to form stable gels of XG. Thus, cold plasma technology is a novel, efficient, and nonenzymatic route to modify XG.     

黄原胶溶液模拟消化污泥流动性能分析

为污泥消化反应器流场的可视化研究提供可行性方法,该文根据同流体流动相似准则分别从密度和流变学特性来分析黄原胶透明溶液作为常规消化污泥相似溶液的可行性。采用质量法和流变仪分别测量不同浓度污泥和添加KCl的黄原胶溶液的密度及流变特性。结果表明15 g/L添加KCl的黄原胶溶液与95%含水率污泥在密度不具有显著性差异的前提下具有相似的流变特性,流变曲线的决定系数分别为R2=0.995 3(动力黏度)、R2=0.893 5(剪切应力),均为典型的假塑性非牛顿流体。混合试验表明2种流体中示踪剂浓度的变化规律相似且均在40 min后趋于平衡浓度50 mg/L。等同性分析表明,在显著性水平α=0.05时,2种流体中以流变特性和密度为参数的双侧t检验不具有显著性差异,符合同流体流动相似准则。故添加KCl的黄原胶溶液可以作为污泥的透明相似溶液,为污泥等不透明生物质流体厌氧消化的模拟及可视化研究奠定基础。     

Emulsifying and foaming properties of ultraviolet-irradiated egg white protein and sodium caseinate

The physicochemical and functional properties of ultraviolet (UV)-treated egg white protein (EW) and sodium caseinate (SC) were investigated. UV irradiation of the proteins was carried out for 30, 60, 90, and 120 min. However, the SC samples were subjected to extended UV irradiation for 4 and 6 h as no difference was found on the initial UV exposure time. Formol titration, SDS-PAGE, and FTIR analyses indicated that UV irradiation could induce cross-linking on proteins and led to improved emulsifying and foaming properties (P < 0.05). These results indicated that the UV-irradiated EW and SC could be used as novel emulsifier and foaming agents in broad food systems for stabilizing and foaming purposes.     

Inhibiting effects of egg white dry-heated at 120 degrees C on heat aggregation and coagulation of egg white and characteristics of dry-heated egg white.

Dialyzed and freeze-dried egg white (FDEW) was dry-heated at 120 degrees C for up to 6 h. The inhibiting effects of the dry-heated egg white (DHEW) on the heat aggregation and coagulation of egg white (as 10% FDEW solution) and characteristics of the DHEW were examined. From the changes in turbidities and soluble protein contents of supernatant in various mixtures of 10% FDEW and DHEW solutions induced by heating (60 degrees C, 5 min), it was found that the inhibiting capacity increased with increases in the dry-heating time (DHT). The FDEW proteins were denatured with a mild conformational change (not secondary but tertiary structure) with the increase in DHT and aggregated partially. However, the more transparent solutions of DHEW containing soluble aggregates according to DHT were also obtained after heating. The transparency according to DHT came to be scarcely affected by the NaCl concentration and the dilution with diluents containing SDS, urea, and 2-mercaptoethanol. These findings suggest that the heat aggregations and coagulations of ovotransferrin and lysozyme in the FDEW were inhibited by their bindings with the soluble aggregates in DHEW.     

Toward better understanding of salt-induced hen egg white protein aggregation using field-flow fractionation

Field-flow fractionation techniques including sedimentation field-flow fractionation (SdFFF) and flow field-flow fractionation (FlFFF) were applied to investigate hen egg white protein aggregation. The thermally induced aggregation of hen egg white protein was observed at temperatures of 60 degrees C and higher. Particle size and size distribution of hen egg white protein aggregates were characterized by SdFFF to investigate parameters affecting ZnCl 2-induced aggregation of hen egg white protein. At a fixed concentration of 1.0 M ZnCl 2 and an incubation time of 15 min, the mean particle diameters of the aggregates were determined to be 0.43, 0.67, and 0.80 mum for hen egg white protein contents of 5, 6.25, and 7.5% (w/v), respectively. With the incubation time of 15 min, increasing the concentration of ZnCl 2 from 0.5 to 1.0 and to 1.5 M caused the mean particle diameter of the aggregates to grow from 0.37 to 0.42 and to 0.68 mum, respectively at 5% (w/v) hen egg white protein. Upon prolonged contact time, larger aggregates were formed. Furthermore, FlFFF was employed as a novel approach to determine the efficiency of protein utilization for aggregation. The pH values as well as ZnCl 2 and protein concentrations influenced the efficiency of protein utilization for aggregation. With the optimum condition, that is, a protein concentration higher than 2% (w/v) and a pH greater than 5, the efficiency of protein utilization was approximately 65%.     

Correlation of the protein structure and gelling properties in dried egg white products

The relationship between protein structure and aggregation, as well as heat-induced gelling properties, of seven dried egg white (DEW) products was investigated. Strong correlations were found between average molecular weight and hydrophobicity plus surface SH groups of DEW-soluble protein aggregate (SPA). This suggests that hydrophobic interactions and disulfide bond formation between protein molecules were involved in the aggregation. The average molecular weight of DEW products with alkaline pHs was relatively higher than those with neutral pHs and the same degree of protein unfolding, probably because of more disulfide bond formation between protein molecules. In addition, strong correlations were found between hydrophobicity, surface SH groups plus average molecular weight of DEW-SPA, and physical properties of the gels from DEW products. These data indicated that controlling the aggregation of DEW proteins in the dry state is crucial to controlling the gelling properties of DEW.     

Proteomics analysis of egg white proteins from different egg varieties

The market of specialty eggs, such as omega-3-enriched eggs, organic eggs, and free-range eggs, is continuously growing. The nutritional composition of egg yolk can be manipulated by feed diet; however, it is not known if there is any difference in the composition of egg white proteins among different egg varieties. The purpose of the study was to compare the egg white proteins among six different egg varieties using proteomics analysis. Egg white proteins were analyzed using two-dimensional gel electrophoresis (2-DE), and 89 protein spots were subjected to LC-MS/MS. A total of 23 proteins, belonging to Gallus gallus , were identified from 72 detected protein spots. A quiescence-specific protein precursor in egg white was identified for the first time in this study. Significant differences in the abundant levels of 19 proteins (from 65 protein spots) were observed among six egg varieties. Four proteins, ovalbumin-related protein Y, cystatin, avidin, and albumin precursor, were not different among these six egg varieties. These findings suggest that the abundance, but not the composition, of egg white proteins varied among the egg varieties.     

Proteomic analysis of hen egg white

Hen egg white is an original biological fluid in which major proteins have been widely studied, unlike the minor components. In this study, two-dimensional electrophoresis associated with mass spectrometry enabled the separation of 69 protein spots and their matching with major proteins, which were already known, and with minor proteins. Sixteen proteins were identified, and among them, two had never been previously detected in hen egg white, i.e., Tenp, a protein with strong homology with a bacterial permeability-increasing protein family (BPI), and VMO-1, an outer layer vitelline membrane protein. Thirteen proteins present a very wide polymorphism (ovotransferrin, ovomucoid, clusterin, etc.), some of them up to nine isoforms (ovoinhibitor). Eleven functional protein families were identified (serpin, transferrin, protease inhibitors Kazal, glycosyl hydrolases, lipocalin, bactericidal permeability-increasing protein, clusterin, UPAR/CD59/Ly6/ snake neurotoxin, cysteine protease inhibitor, VMO-1, and folate receptor families). These various biological functions could be interesting for further valorizations. In addition, three spots remain unidentified, probably because these proteins are not yet indexed in the international protein databanks.     

丙酮酸基对黄原胶/魔芋葡甘聚糖复配体系凝胶特性的影响

为了实现对复配凝胶体系状态的调控,扩展凝胶在食品中的应用,该研究通过酸性热处理调控黄原胶中丙酮酸基含量变化,研究其对黄原胶结构、流变特性及黄原胶(Xanthan Gum)与魔芋葡甘聚糖(Konjac Glucomannan)复配凝胶特性(如溶胶-凝胶转换温度、流变特性等)的影响.研究结果表明;XG螺旋结构随丙酮酸基减少...     

与黄原胶生物合成相关的"1.9" kb EcoRI DNA片段的序列测定分析

对Ｘａｎｔｈｏｍｏｎａｓｃａｍｐｅｓｔｒｉｓｐｖ．ｃａｍｐｅｓｔｒｉｓ（下称Ｘｃｃ）８００４菌株染色体基因组中９．４ｋｂＨｉｎｄⅢＤＮＡ的“１．９”ｋｂＥｃｏＲＩ酶切片段的测序分析结果表明,该ＥｃｏＲＩＤＮＡ片段的实际长度为１．８８ｋｂ。在核苷酸水平上与Ｘｃｃ的ｇｕｍ基因有９８％的一致性;这一ＥｃｏＲＩ片段上有两个有意义的ＯＲＦ：ＯＲＦ１和ＯＲＦ２。ＯＲＦ１是一个不完整的ＯＲＦ;在氨基酸水平上,ＯＲＦ１和ＯＲＦ２的推断性编码产物蛋白分别与ｇｕｍＡ基因编码的ＧｕｍＡ及ｇｕｍＢ基因编码的ＧｕｍＢ蛋白有１００％的一致性。因此在１．８８ｋｂＥｃｏＲＩ片段上存在一完整的ｇｕｍＢ基因。     

Stability of monoterpenes encapsulated in gum Arabic by spray-drying

Microencapsulation using spray-drying was tested with gum arabic and monoterpenes as wall and core materials, respectively. Citral, linalool, beta-myrcene, limonene, and beta-pinene were used at concentrations of 10, 20, and 30% with respect to the wall material. The greatest percentages of retention occurred at a concentration of 10%. Linalool and citral presented the greatest losses with increase in concentration. The hydrocarbons used were the most retained. Of the hydrocarbons, beta-pinene was better retained in the capsules than limonene, and beta-myrcene was the least retained of all. The capsules presented similar external morphologies, with no apparent cracks or porosity and an average size varying between 15.7 and 23.2 microm. The stability of the capsules to temperature was monitored for 33 days. The degradation products of the monoterpenes were evaluated. The results indicated a greater stability of the capsules containing beta-pinene and citral than of those containing linalool and beta-myrcene presenting the lowest retentions.     

Improvement of functional properties of egg white protein through phosphorylation by dry-heating in the presence of pyrophosphate

Egg white protein (EWP) was phosphorylated by dry-heating in the presence of pyrophosphate at pH 3.0-7.0 and 85 degrees C for 1 and 5 days, and the functional properties of the phosphorylated EWP (PP-EWP) were investigated. The phosphorylation was accelerated with a decrease of pH from 7.0 to 3.0 and for heating times from 1 to 5 days. The phosphorus content of EWP increased approximately 1.05% by dry-heating at pH 4.0 and 85 degrees C for 5 days in the presence of pyrophosphate, which was higher than that of casein. The electrophoretic mobility of EWP increased with an increase in the phosphorylation level. The surface hydrophobicity of EWP increased by phosphorylation. The heat stability, emulsifying properties, and digestibility of EWP were improved by phosphorylation. The calcium phosphate-solubilizing ability of EWP was enhanced by phosphorylation. A firmer and transparent heat-induced gel of PP-EWP was obtained, and the water-holding capacity of heat-induced PP-EWP gel was higher that that of the control. These results suggest that phosphorylation by dry-heating in the presence of pyrophosphate is a useful method for improving the functional properties of EWP.     

alpha-Casein improves the gel properties of dried egg white

The effects of addition of alpha-casein (alpha-CN) to dried egg white (DEW) were investigated by measuring transparency, hardness, and water-holding capacity (WHC) of the heat-induced gels. A DEW concentration of 8% (w/w) was required for formation of a self-supporting gel following heating at 80 degrees C for 20 min at pH 7. Solutions of alpha-CN, even up to a protein concentration of 12% (w/w), did not gel under the same conditions. The addition of alpha-CN (0.5-4%) to 8% DEW caused the increase in gel hardness gels, as compared with DEW gels alone at a total amount of protein concentrations, and the mixed gels became transparent with the increase of added alpha-CN concentrations. The 10% mixed protein solutions of alpha-CN (3-6%) and DEW (4-7%) formed transparent gels, although each protein did not gel individually at their protein concentrations. Mixture with 2:8 mixing ratio of alpha-CN to DEW at a total protein concentration of 10% showed synergistic effects in improving DEW gel properties above pH 7 and below 25 mM NaCl. The improvements (hardness, transparency, and WHC) of DEW gel by alpha-CN seem to be caused mainly by the inhibition of alpha-CN against heat coagulation of DEW protein.     

Immunochemical and structural analysis of pepsin-digested egg white ovomucoid

Ovomucoid, an egg protein comprising approximately 10% egg white, was digested using the enzyme pepsin, and fragments were isolated by anion-exchange and reverse phase HPLC. Four distinct fragments were identified by analysis with SDS-PAGE, including three large fragments with molecular weights of around 24, 18, and 14 kDa. N- and C-terminal and amino acid sequencing analyses identified the fragments as V134-C186 (domain 3), V21-A133, and A1-A133 (domain 1+2). Further separation and sequencing of the fraction composed of small peptides, to determine their exact makeup and location in the protein, remained to be carried out and identified a peptide G51-Y73. All four fragments showed IgE-binding activity, as measured by ELISA, using human sera from egg-allergic individuals. Little change in the digestibility of ovomucoid by trypsin and chymotrypsin was observed following digestion with pepsin, indicating that pepsin-digested ovomucoid retains its trypsin (protease) inhibitor activities. Reduced carboxymethylated ovomucoid was prepared, and digestion with pepsin produced significantly more peptides than did the digestion of the native ovomucoid, indicating that the disulfide bonds play a significant role in the digestive resistance of ovomucoid. The reduction of ovomucoid enhanced its digestibility and lower allergenicity of the protein.     

Stability of citral in emulsions coated with cationic biopolymer layers

Multilayer emulsions containing citral were prepared by the layer-by-layer deposition technique based on the electrostatic interaction between negatively charged emulsion droplets and two positively charged biopolymer coatings, chitosan (CS) and ε-polylysine (EPL). The optimum concentrations of both CS and EPL were determined through the ζ-potential and particle size measurements and were found to be 1.5 mg/mL for CS and 6 mg/mL for EPL. Quartz crystal microbalance with dissipation monitoring (QCM-D) was conducted to monitor the binding between emulsion droplets and cationic polymers, and our results proved the existence of strong interactions between emulsions and the cationic polymer coatings. The stability of citral and the production of the off-flavor compounds were analyzed by solid-phase microextraction gas chromatography (SPME-GC). The results suggested that the addition of the cationic CS interfacial layer was effective in improving the stability of citral during storage.     

Comparison of different electrophoretic separations of hen egg white proteins

The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS-PAGE, native-PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white.     

Stabilization of oil-in-water emulsions by cod protein extracts

The ability of two protein fractions extracted from cod to form and stabilize oil-in-water emulsions was examined: a high salt extracted fraction (HSE protein) and a pH 3 acid extracted fraction (AE protein). Both fractions consisted of a complex mixture of different proteins, with the predominant one being myosin (200 kDa). The two protein fractions were used to prepare 5 wt % corn oil-in-water emulsions at ambient temperature (pH 3.0, 10 mM citrate-imidazole buffer). Emulsions with relatively small mean droplet diameters (d(3,2) < 1 microm) and good creaming stability (> 9 days) could be produced at protein concentrations > or =0.2 wt % for both fractions. The isoelectric point of droplets stabilized by both protein fractions was pH approximately 5. The emulsions were stable to droplet flocculation and creaming at relatively low pH (< or =4) and NaCl concentrations (< or =150 mM) when stored at room temperature. In the absence of salt, the emulsions were also stable to thermal treatment (30-90 degrees C for 30 min), but in the presence of 100 mM NaCl droplet flocculation and creaming were observed in some of the emulsions, particularly those stabilized by the AE fraction. The results suggest that protein fractions extracted from cod can be used as emulsifiers to form and stabilize food emulsions.