卵清蛋白
美拉德反应
化学
普鲁兰
糖基化
糖基化
色谱法
共价键
结合
蛋清
Zeta电位
多糖
生物化学
有机化学
化学工程
抗原
生物
免疫学
数学
受体
纳米颗粒
数学分析
工程类
作者
Long Sheng,Gong‐Jian Tang,Qi Wang,Jie Zou,Meihu Ma,Xi Huang
标识
DOI:10.1016/j.foodhyd.2019.105384
摘要
The aim of this research was to synthesize ovalbumin-pullulan conjugates through the Maillard reaction and compare the molecular characteristics of native ovalbumin (N-OVA), heated ovalbumin (H-OVA) and glycosylated ovalbumin (G-OVA). The glycosylation was monitored by the degree of graft and Amadori compound. Covalent binding between ovalbumin and pullulan was confirmed by SDS-PAGE and FTIR. CD spectra showed that glycosylation could inhibit the heat-induced formation of β-sheet. Due to the shielding effect of polysaccharide, H0 and fluorescence intensity of G-OVA were lower than those of heated group. Meanwhile, zeta potential values of G-OVA at three different pH were extreme small, close to zero. Compare with N-OVA, the free exposed sulfhydryl contents of conjugates increased and total free sulfhydryl contents decreased. For G-OVA, foaming stability was 50.5%, which was a factor of 7.1 higher than the value of N-OVA (7.1%). G-OVA foam displayed smaller and more homogeneous bubble size than N-OVA and H-OVA. In addition, G-OVA foam presented the slowest rate of the bubble size increase over time. Overall, Maillard reaction was proven to be successful in enhancing the foaming properties of ovalbumin.
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