Relationship of co-gelation and co-aggregation on egg white ovalbumin-lysozyme heteroprotein complex: Formation and thermodynamics

Jingbo Liu; Hongyu Jiang; Min Zhang; Meng Yang; Ting Zhang; Zhiyang Du; Menglei Xu; Xuanting Liu

doi:10.1016/j.foodchem.2022.133030

Relationship of co-gelation and co-aggregation on egg white ovalbumin-lysozyme heteroprotein complex: Formation and thermodynamics

Food Chem. 2022 Sep 15:388:133030. doi: 10.1016/j.foodchem.2022.133030. Epub 2022 Apr 22.

Authors

Jingbo Liu¹, Hongyu Jiang², Min Zhang², Meng Yang², Ting Zhang³, Zhiyang Du², Menglei Xu⁴, Xuanting Liu⁵

Affiliations

¹ Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China. Electronic address: ljb168@sohu.com.
² Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China.
³ Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China. Electronic address: tingzhang@jlu.edu.cn.
⁴ Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China; China State Key Laboratory of Supramolecular Structure and Materials, Jilin University, Changchun 130012, China. Electronic address: xumenglei@jlu.edu.cn.
⁵ Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China. Electronic address: lxt920523@163.com.

PMID: 35483286
DOI: 10.1016/j.foodchem.2022.133030

Abstract

This study aimed to establish binary protein system on egg white ovalbumin (OVA) -lysozyme (LYS), and investigated the relationship between co-aggregation and co-gelation. We focused on the formation of OVA-LYS complex, the typical thermo-dynamically favored coacervation process, in terms of gelling properties, microstructure and thermodynamics. Benefited from synergistic effects during co-gelation, the thermally induced gels of OVA-LYS complex formed at extremely low protein concentration (18 mg/mL) and showed higher storage modulus with increasing LYS concentration. Moreover, the rising particle size, reduced zeta potential, unordered secondary structure and strengthened protein chain were observed with the addition of LYS. Remarkably, the divalent ions enhanced thermodynamic stability of OVA-LYS complex, although the growth of aggregates units were prevented by ions at room temperature. ITC and molecular docking analyses revealed the binding affinity stoichiometry and combination phase, which were closely related to the decrease of minimum energy resulted from the formation of hydrogen bond.

Keywords: Co-aggregation; Co-gelation; Isothermal titration calorimetry; Lysozyme; Molecular docking; Ovalbumin.

MeSH terms

Antiviral Agents
Egg White*
Gels / chemistry
Molecular Docking Simulation
Muramidase* / chemistry
Ovalbumin / chemistry
Thermodynamics

Substances

Antiviral Agents
Gels
Ovalbumin
Muramidase