Changes in gel characteristics of egg white under strong alkali treatment

Changes in gel characteristics of egg white under strong alkali treatment
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强碱处理下蛋清凝胶特性的变化

DOI:
10.1016/j.foodhyd.2014.10.026
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发表时间:
2015-03-01
期刊:
影响因子:
10.7
通讯作者:
Wang, Menglin
Wang, Menglin
中科院分区:
农林科学1区
文献类型:
--
作者:
Chen, Zhangyi;Li, Jianke;Wang, Menglin

文献摘要

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研究了鸡蛋白色(EW)经强碱溶液处理后的凝胶特性,如流变学特性、质构特性、微观结构和分子间作用力的变化。EW的粘度在凝胶前阶段逐渐增加。凝胶形成后,其质构性质和微观结构发生动态变化。随着强碱的持续处理,所形成的凝胶被破坏并逐渐崩解。巯基(SH)和二硫键(SS)含量的变化表明,在强碱条件下,氧化和SH-SS键交换反应迅速发生。然而,SS键很容易被打破,在非常高的pH值。EW凝胶的选择性蛋白质溶解度表明,超过一半的总债券是离子。此外,三分之一的键是SS。这些键中约10%是疏水相互作用,并且存在很少的氢键。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳图谱显示,碱处理使凝胶中的蛋白质发生降解和聚集。因此,卵清蛋白参与SS键的交联迅速促进碱处理,也牵连在凝胶形成支持的各种分子间的力量,如离子键和疏水相互作用。(C)2014爱思唯尔有限公司版权所有。
Changes in gel characteristics, such as rheological and textural properties, microstructures, and intermolecular forces, of egg white (EW) treated with strong alkaline solution were investigated. The viscosity of EW increased gradually in the pre-gel phase. After the gel was formed, the textural properties and microstructures became dynamically changeful. With continuous strong alkali treatment, the formed gel was destroyed and gradually collapsed. Changes in sulfhydryl (SH) group and disulfide (SS) bond contents suggested that oxidation and SH-SS bond exchange reactions rapidly occurred under strong alkali conditions. However, SS bonds were easily broken at very high pH. Selective protein solubility of EW gels indicated that more than half of the total bonds were ionic. Furthermore, one third bonds were SS. Approximately 10% of these bonds was hydrophobic interactions, and few hydrogen bonds were present. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles revealed that the proteins in the gel were degraded and aggregated by alkali treatment. Hence, ovalbumin was involved in the cross-linking of SS bonds rapidly promoted by alkali treatment, and also implicated in gel formation supported by various intermolecular forces, such as ionic bond and hydrophobic interactions. (C) 2014 Elsevier Ltd. All rights reserved.