Comparison of biochemical characteristics and gel properties of chicken myofibrillar protein affected by heme-iron and nonheme-iron oxidizing systems
文献类型： 外文期刊
作者： Zhang, Muhan 1 ; Bian, Huan 1 ; Li, Jiaolong 1 ; Yan, Weili 1 ; Wang, Daoying 1 ; Xu, Weimin 1 ; Shu, Lizhi 1 ; Shi, Miaomiao 1 ;
作者机构： 1.Minist Sci & Technol, Jiangsu Key Lab Food Qual, Safety State Key Lab Cultivat Base, Nanjing 210014, Peoples R China; Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Peoples R China; Minist Agr & Rural Affairs, Key Lab Cold Chain Logist Technol Agroprod, Nanjing, Peoples R China
关键词： Myofibrillar protein; Protein oxidation; Hemin; Iron; Heat-induced gels
期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：8.1； 五年影响因子：7.7 ）
ISSN： 0963-9969
年卷期： 2023 年 165 卷
页码：
收录情况： SCI
摘要： In this study, the effect of hemin and non-heme iron on the biochemical and gelling properties of chicken myofibrillar protein (MP) was compared. Results revealed that free radicals from hemin incubated MP were significantly higher than that in FeCl3 incubated samples (P < 0.05), and had higher ability to initiate protein oxidation. The carbonyl content, surface hydrophobicity, random coil increased with oxidant concentration, whereas the total sulfhydryl and alpha-helix content decreased in both oxidizing systems. The turbidity and particle size were increased after oxidant treatment, indicating oxidation promoted the cross-linking and aggregation of protein, and the degree of aggregation was higher in hemin treated MP compared with that incubated with FeCl3. The biochemical changes of MP resulted in an uneven and loose gel network structure, which significantly reduced the gel strength and water holding capacity (WHC) of the gel.
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