Improvement on gel properties of chicken myofibrillar protein with electron beam irradiation: Based on protein structure, gel quality, water state

被引:0
|
作者
Bai, Rong [1 ]
Han, Jincheng [1 ]
Ye, Xiang [1 ]
Yu, Jiangtao [2 ]
Jiang, Shengqi [1 ]
Li, Ziwei [1 ]
Zhang, Linlu [1 ]
Yang, Chunjie [1 ]
Chen, Ya [1 ]
Wang, Siying [1 ]
Ding, Wu [1 ]
机构
[1] Northwest A&F Univ, Coll Food Sci & Engn, Yangling 712100, Shaanxi, Peoples R China
[2] Yangling Hesheng Irradiat Technol Co Ltd, Yangling 712100, Shaanxi, Peoples R China
关键词
Electron beam irradiation; Myofibrillar protein; Secondary structure; Rheological property; Moisture distribution; GAMMA-IRRADIATION; PHYSICOCHEMICAL PROPERTIES; FUNCTIONAL-PROPERTIES; GELATION PROPERTIES; PORK MYOFIBRILLAR; CONFORMATION; OXIDATION; FIELD;
D O I
10.1016/j.ijbiomac.2024.135806
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This study aimed to investigate the effects of electron beam (E-beam) irradiation at different doses (0-15 kGy) on the solubility, rheological properties, emulsification characteristics, and moisture distribution of chicken myofibrillar proteins (MPs). Irradiation treatment notably increased the solubility, surface hydrophobicity, emulsification properties, and apparent viscosity of MPs, based on conformational changes caused by irradiation-induced oxidative denaturation of proteins. However, high doses of irradiation (15 kGy) induced in excessive cross-linking and aggregation of proteins, reducing the solubility, emulsification properties, and shear stress. Degradation of myosin heavy and light chains in irradiated MPs increased the content of beta-turns and random coils. Additionally, the initial relaxation times of T-21 and T-22 in irradiated protein gels were reduced, and the peak value of P-21 was increased, which improved the water-capturing ability of protein gels. Altogether, these results findings suggest that electron beam irradiation can be applied as a potential technique for modifying muscle proteins.
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页数:12
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