Stabilization of O/W emulsions via interfacial protein concentrating induced by thermodynamic incompatibility between sarcoplasmic proteins and xanthan gum
Stabilization of O/W emulsions via interfacial protein concentrating induced by thermodynamic incompatibility between sarcoplasmic proteins and xanthan gum
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DOI：
10.1016/j.foodhyd.2021.107242
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发表时间：
2021-10-01
影响因子：
10.7
通讯作者：
Yang, Zongyun
中科院分区：
文献类型：
--
作者：
Du, Feifei;Qi, Yue;Yang, Zongyun
本研究发现肌浆蛋白(SPS)与黄原胶(XG)在水溶液中的热力学不相容以及界面浓缩增强了乳状液的稳定性。在pH=7.2时，研究了SP和XG浓度对相图的影响。当XG固定在0.5%时，随着溶液体系中SP浓度的增加，水相体系的平均粒径逐渐减小。这可能归因于XG聚集性的降低。TurBiscan稳定性指数和Delta背散射曲线表明，1%是SP的临界浓度，热力学不相容大大增强，一旦超过1%，就会导致相分离。粒度分布结果和激光共聚焦扫描显微镜图像显示，在乳液体系中，当SP浓度达到2%(w/v)时，液滴的粒度分布和絮凝作用减小。界面性质的研究结果表明，由于XG的界面浓缩作用，更多的SPS被吸附到油水界面，导致界面压力升高。XG的存在使Zeta电位从-23.42 mV下降到-21.80 mV，说明电荷稳定作用不是SP/XG乳液稳定的主要因素。添加0.5%XG的乳状液具有较好的物理稳定性。我们的研究可能对SPS的循环利用和界面浓缩效应对肉类蛋白乳状液的调节具有潜在的意义。
Thermodynamic incompatibility between sarcoplasmic proteins (SPs) and xanthan gum (XG) in aqueous solutions and enhanced emulsion stabilization induced by interfacial concentrating were discovered in this research. The phase diagram was investigated in the dependence of the concentrations of SP and XG at pH 7.2. With XG fixed at 0.5%, as the SP concentration in the solution system was increased, the mean particle size of the aqueous system decreased gradually. This might be attributed to the reduction in the aggregation of XG. The Turbiscan Stability Index and delta backscattering profiles indicted that 1% was the critical SP concentration, thermodynamic incompatibility then enhanced greatly and led to phase separation once exceeding 1%. Particle size distribution results and confocal laser scanning microscopy images revealed that in the emulsion system, the particle size distribution of the droplets and flocculation decreased as the SP concentration reached 2% (w/v). The results of interfacial properties suggested that due to the interfacial concentrating effect by XG, more SPs are adsorbed onto the oil-water interface, resulting in an increase in interfacial pressure. The decrement in zeta-potential in the presence of XG (from -23.42 mV to -21.80 mV at 2% SPs) implied that the charge stabilization effect did not dominate in the stabilization of SP/XG-based emulsions. The emulsion with 0.5% XG showed better physical stability. Our research may have potential implications for the recycle of SPs and the regulation of meatprotein-based emulsions by the interfacial concentrating effect.