Comparison of biochemical characteristics and gel properties of chicken myofibrillar protein affected by heme-iron and nonheme-iron oxidizing systems

Muhan Zhang; Huan Bian; Jiaolong Li; Weili Yan; Daoying Wang; Weimin Xu; Lizhi Shu; Miaomiao Shi

doi:10.1016/j.foodres.2023.112538

Comparison of biochemical characteristics and gel properties of chicken myofibrillar protein affected by heme-iron and nonheme-iron oxidizing systems

Food Res Int. 2023 Mar:165:112538. doi: 10.1016/j.foodres.2023.112538. Epub 2023 Jan 26.

Authors

Muhan Zhang¹, Huan Bian¹, Jiaolong Li¹, Weili Yan¹, Daoying Wang², Weimin Xu¹, Lizhi Shu¹, Miaomiao Shi¹

Affiliations

¹ Jiangsu Key Laboratory for Food Quality and Safety State Key Laboratory Cultivation Base, Ministry of Science and Technology, Nanjing 210014, PR China; Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China; Key Laboratory of Cold Chain Logistics Technology for Agroproduct, Ministry of Agriculture and Rural Affairs, PR China.
² Jiangsu Key Laboratory for Food Quality and Safety State Key Laboratory Cultivation Base, Ministry of Science and Technology, Nanjing 210014, PR China; Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China; Key Laboratory of Cold Chain Logistics Technology for Agroproduct, Ministry of Agriculture and Rural Affairs, PR China. Electronic address: daoyingwang@yahoo.com.

PMID: 36869542
DOI: 10.1016/j.foodres.2023.112538

Abstract

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 α-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.

Keywords: Heat-induced gels; Hemin; Iron; Myofibrillar protein; Protein oxidation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Chickens*
Gels
Hemin
Iron*
Oxidants

Substances

Iron
ferric chloride
Hemin
Gels
Oxidants