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Emulsifying properties of ovalbumin: Improvement and mechanism by phosphorylation in the presence of sodium tripolyphosphate

卵清蛋白 化学 傅里叶变换红外光谱 Zeta电位 X射线光电子能谱 核化学 纳米颗粒 材料科学 生物 核磁共振 有机化学 化学工程 纳米技术 免疫学 物理 工程类 免疫系统
作者
Zhouyi Xiong,Maojie Zhang,Meihu Ma
出处
期刊:Food Hydrocolloids [Elsevier]
卷期号:60: 29-37 被引量:107
标识
DOI:10.1016/j.foodhyd.2016.03.007
摘要

In this work, ovalbumin (OVA) was phosphorylated by dry-heating at three different pH values (5.0, 7.0 and 9.0) and 45 °C for 12 h in the presence of sodium tripolyphosphate (STP). The results indicated that, when compared with native OVA (N-OVA), the zeta potential absolute value of phosphorylated OVA (PP-OVA) increased from 2.13 mv (N-OVA) to 13.57(PP-OVA-pH5.0), 16.00(PP-OVA-pH 7.0) and 11.20 mv (PP-OVA-pH 9.0); the volume-weighted mean diameter (D [4,3])of emulsions stabilized by the N- and PP-OVA decreased from 70.22 μm (N-OVA) to 37.16(PP-OVA-pH 5.0), 16.21(PP-OVA-pH 7.0) and 43.52 μm (PP-OVA-pH 9.0); and PP-OVA emulsions exhibited a more narrow monomodal size distribution and a smaller particle size than those of N-OVA, with the corresponding emulsifying activities index (EAI) increased from 92.71(N-OVA) to 142.51(PP-OVA-pH5.0), 224.88(PP-OVA-pH 7.0), and 150.97(PP-OVA-pH 9.0), respectively. The microscopic observation showed that the emulsion droplets of PP-OVA were more densely and uniformly distributed than those of N-OVA. Furthermore, characterization of PP-OVA by Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and 31P nuclear magnetic resonance (31P NMR) revealed that phosphate groups were bound to the -OH on serine and threonine and the -NH2 on lysine and arginine, with covalent interactions (C–O–P and C-N-P bounds) formed between OVA and STP. This study demonstrated that the introduction of phosphate groups could increase the amount of negative charge and intermolecular repulsion, decrease the particle size of droplets and improve the emulsifying ability of PP-OVA.
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