Abstract Ovotransferrin (OVT) is the main protein component of egg white responsible for initial gelation due to its high thermal susceptibility. Co-aggregation of lysozyme (LYZ) is involved in OVT aggregate formation at low temperatures during pasteurization. Undesirable formation of aggregates limits the degree of thermal processing that can be applied to egg white products. However, the characteristics of co-aggregates of OVT and LYZ have not been elucidated. Here, we determined the thermal co-aggregation process of OVT and LYZ in terms of protein composition, structure, intermolecular forces, and morphology. The amount of LYZ involved in co-aggregates was dependent on the amount of aggregated OVT regardless of the mixing ratio. Native LYZ had the capability of precipitating soluble OVT aggregates by non-covalent association. The co-aggregates of OVT and LYZ formed colloidal particles with a large network, which was not observed in systems consisting of either protein alone. The hierarchical co-aggregation of OVT and LYZ started from the aggregation of OVT involving LYZ non-covalently, which suppresses electrostatic repulsion between soluble OVT aggregates, followed by the growth of insoluble aggregates by disulfide bond crosslinkage between the soluble aggregates. These results provide information regarding efficient pasteurization and thermal processing of hen egg white.

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卵转铁蛋白和溶菌酶的共聚集

摘要 卵转铁蛋白（OVT）是蛋清的主要蛋白质成分，由于其高热敏感性而负责初始凝胶化。在巴氏杀菌过程中，溶菌酶的共聚集 (LYZ) 参与了低温下 OVT 聚集的形成。不希望的聚集体形成限制了可应用于蛋清产品的热处理程度。然而，尚未阐明 OVT 和 LYZ 共聚集体的特征。在这里，我们在蛋白质组成、结构、分子间力和形态方面确定了 OVT 和 LYZ 的热共聚集过程。无论混合比例如何，共聚集体中 LYZ 的数量取决于聚集的 OVT 的数量。天然 LYZ 具有通过非共价结合沉淀可溶性 OVT 聚集体的能力。OVT 和 LYZ 的共聚集体形成具有大网络的胶体颗粒，这在单独由任一蛋白质组成的系统中均未观察到。OVT 和 LYZ 的分层共聚集开始于 LYZ 非共价参与的 OVT 聚集，这抑制了可溶性 OVT 聚集体之间的静电排斥，然后通过可溶性聚集体之间的二硫键交联使不溶性聚集体生长。这些结果提供了关于鸡蛋清的有效巴氏杀菌和热处理的信息。这抑制了可溶性 OVT 聚集体之间的静电排斥，然后通过可溶性聚集体之间的二硫键交联来抑制不溶性聚集体的生长。这些结果提供了关于鸡蛋清的有效巴氏杀菌和热处理的信息。这抑制了可溶性 OVT 聚集体之间的静电排斥，然后通过可溶性聚集体之间的二硫键交联来抑制不溶性聚集体的生长。这些结果提供了关于鸡蛋清的有效巴氏杀菌和热处理的信息。