Aggregation of hen egg white proteins with additives during agitation
Aggregation of hen egg white proteins with additives during agitation
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DOI：
10.1016/j.lwt.2021.111378
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发表时间：
2021-04-22
影响因子：
6
通讯作者：
Shiraki, Kentaro
中科院分区：
文献类型：
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作者：
Hong, Taehun;Iwashita, Kazuki;Shiraki, Kentaro
蛋清蛋白（HEWPs）的聚集是食品工业蛋制品生产中的一个重要问题。搅拌过程中heps的聚集是由蛋白质的气液界面变性引起的，这与它们的热聚集不同。在本研究中，我们研究了在添加剂存在的情况下，搅拌引起的高分子量聚合物的聚集和共聚集机制。两亲性表面活性剂和两亲性添加剂抑制了搅拌引起的heps聚集，而不是众所周知的聚集抑制剂精氨酸。溶菌酶（LYZ）和卵清蛋白（OVA）在搅拌过程中显著形成共聚集体，并通过与变性溶菌酶的二硫键结合而稳定。相比之下，溶菌酶和卵转铁蛋白（OVT）形成共聚集体的程度低于OVA，这是由于这两种蛋白之间的相互作用较弱。这些数据表明，在搅拌过程中，LYZ和OVA之间的静电吸引和二硫交换在heps的共聚集中起着关键作用。本文提出的理论和技术，不仅可能成为一个适当的处理方法，更安全的巴氏灭菌和运输的基础，而且提供了信息的混合蛋白聚集在各个领域的应用。
Aggregation of hen egg white proteins (HEWPs) is an important issue in the production of egg products in the food industry. The aggregation of HEWPs during agitation is caused by the gas-liquid interface denaturation of proteins, which is different from their thermal aggregation. In this study, we investigated the mechanism of aggregation and the co-aggregation of HEWPs induced by agitation in the presence of additives. The aggregation of HEWPs caused by agitation was suppressed by amphiphilic surfactant and amphiphilic additives, rather than by the well-known aggregation suppressor, arginine. Lysozyme (LYZ) and ovalbumin (OVA) dramatically formed co-aggregates that were stabilized by disulfide bonding with denatured lysozyme during agitation. In contrast, lysozyme and ovotransferrin (OVT) formed co-aggregates to a lower extent than that observed for OVA, due to the weak interaction between these two proteins. These data indicate that the electrostatic attraction and disulfide exchange between LYZ and OVA play critical roles in the co-aggregation of HEWPs during agitation. This article proposes not only the theory and techniques that may become the basis of an appropriate processing method for safer pasteurization and transportation of HEWPs but also provides information about the aggregation of mixed proteins used in various fields.