关键词: acidic pH electrostatic interaction emulsifying properties soy protein isolate γ-polyglutamic acid

Mesh : Emulsions / chemistry Soybean Proteins / chemistry Polyglutamic Acid Static Electricity Emulsifying Agents / chemistry

来  源:   DOI:10.1111/1750-3841.16873

Abstract:
In order to improve the emulsifying properties of soy protein around isoelectric point, soy protein isolate (SPI) and γ-polyglutamic acid (γ-PGA) complexes were prepared by electrostatic interaction. The formation of SPI-γ-PGA electrostatic complex and emulsifying properties were investigated by monitoring turbidity, zeta potential, intrinsic fluorophores, emulsion characterization, and microstructure observation. The results showed that the formation of SPI-γ-PGA electrostatic complex was identified through turbidimetric analysis and zeta-potential measurement. Intrinsic fluorescence spectrum indicated internal structure changes of electrostatic complexes. Furthermore, SPI-γ-PGA complex-stabilized emulsions showed better stability with small droplet sizes and slow growth as well as the uniform microstructure around the isoelectric point (pH 4.0-5.0) than SPI-formed emulsions. Under the different thermal treatments and ionic strengths, emulsions stabilized by SPI-γ-PGA-soluble complex resulted in improved emulsion stability to environmental stresses. This may be attributed to the increased steric repulsion and electrostatic repulsion by SPI-γ-PGA complexes at oil-water interfaces. The findings derived from this research would provide theoretical reference about SPI-γ-PGA electrostatic complex that can be applied in acid beverages and developed a novel plant-based sustainable stabilizer for emulsions. PRACTICAL APPLICATION: The electrostatic interaction between SPI and γ-PGA improved the emulsifying characteristics of soy protein around isoelectric point. The results derived from this research would expand applications of SPI-γ-PGA-soluble electrostatic complex that can be applied in acid beverages, as well as a novel plant-based sustainable stabilizer for emulsions.
摘要:
为了提高大豆蛋白在等电点附近的乳化性能,通过静电相互作用制备了大豆分离蛋白(SPI)和γ-聚谷氨酸(γ-PGA)复合物。通过监测浊度,研究了SPI-γ-PGA静电复合物的形成和乳化性能,zeta电位,固有荧光团,乳液表征,和微观结构观察。结果表明,通过比浊法分析和ζ电位测量,确定了SPI-γ-PGA静电复合物的形成。本征荧光光谱显示了静电配合物内部结构的变化。此外,与SPI形成的乳液相比,SPI-γ-PGA复合物稳定的乳液显示出更好的稳定性,液滴尺寸小,生长缓慢,等电点(pH4.0-5.0)附近的微观结构均匀。在不同的热处理和离子强度下,通过SPI-γ-PGA可溶性复合物稳定的乳液可改善乳液对环境压力的稳定性。这可能归因于SPI-γ-PGA复合物在油-水界面处的空间排斥和静电排斥增加。这项研究的发现将为SPI-γ-PGA静电复合物在酸性饮料中的应用提供理论参考,并开发了一种新型的基于植物的可持续乳液稳定剂。实际应用:SPI与γ-PGA之间的静电相互作用改善了大豆蛋白在等电点附近的乳化特性。这项研究的结果将扩大SPI-γ-PGA可溶性静电复合物的应用,可应用于酸性饮料,以及一种新型的基于植物的可持续乳液稳定剂。
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