Effect of hydroxyl radical-induced oxidation on the structure
and heat-induced gel properties of ovalbumin
Key Laboratory of Coarse Cereal
Processing, Ministry of Agriculture, College
of Pharmacy and Biological Engineering,
Chengdu University, Chengdu 610106,
People’s Republic of China
College of Food Science, Fujian Agriculture
and Forestry University, Fuzhou 350002,
People’s Republic of China
Key Laboratory of Fermentation
Engineering, Ministry of Education, Hubei
University of Technology, Wuhan, Hubei
National R&D Center for Egg Processing,
College of Food Science and Technology,
Huazhong Agricultural University, Wuhan
430070, People’s Republic of China
Qun Huang, College of Food Science,
Fujian Agriculture and Forestry University,
Fuzhou 350002, People’s Republic of
Meihu Ma, National R&D Center for Egg
Processing, College of Food Science and
Technology, Huazhong Agricultural
University, Wuhan 430070, People’s
Republic of China.
National Natural Science Foundation of
China, Grant/Award Number: No.
31601490; Earmarked Fund for Modern
Agro-industry Technology Research System,
Grant/Award Number: CARS-41-K23
The present study is aimed to investigate the effect of hydroxyl radical-induced oxidation on the
structure and gel properties of chicken ovalbumin. With the increase in oxidation time and H
dose, the carbonyl content in ovalbumin increased, while the free sulfhydryl content decreased.
The effect of oxidation on the structure of ovalbumin was examined, and the results indicated that
the disorder level increased. Oxidation of ovalbumin lowered the solubility, and the viscosity of the
solution decreased significantly. Oxidation weakened the water holding capacity and gel hardness,
as well as resulting in significant changes in the microstructure of ovalbumin gels. Hydroxyl radical-
induced oxidation caused destabilization of the ovalbumin structure, thereby affecting the heat-
induced gel properties.
The present study demonstrated the effect of hydroxyl radical-induced oxidation on chicken OVA,
concluding that the oxidation might be one of the primary reasons for the degradation of its gel
properties. Consequently, avoiding protein oxidation during storage and processing would help
maintain the functional properties of the chicken egg white. Therefore, this study provides impor-
tant information for the research and application of ovalbumin.
Ovalbumin (OVA) is widely applied in the food industry, and it is one of
the representative proteins that are used as a model in food research.
The well-known molecular structure and ease of acquisition make OVA
an ideal reference for studying the properties of other food proteins
(An et al., 2014; Liu et al., 2017). The effect of different treatments and
modifications of OVA is also a hotspot of study because the results
could provide important information on the understanding of the struc-
ture and property changes of food proteins during food processing and
The effects of several physical treatments and chemical modifica-
tions on the structure and functional properties of OVA have been
investigated. The emulsifying and foaming ability could be improved by
high intensity ultrasound treatment, while the stability of emulsions
and foams did not change significantly (Xiong et al., 2016a). Another
J Food Process Preserv. 2018;e13626.
2018 Wiley Periodicals, Inc.
Received: 8 November 2017
Revised: 26 December 2017
Accepted: 8 March 2018