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

Autor: Zhang M; 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., Bian H; 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., Li J; 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., Yan W; 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., Wang D; 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., Xu W; 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., Shu L; 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., Shi M; 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.
Jazyk: angličtina
Zdroj: Food research international (Ottawa, Ont.) [Food Res Int] 2023 Mar; Vol. 165, pp. 112538. Date of Electronic Publication: 2023 Jan 26.
DOI: 10.1016/j.foodres.2023.112538
Abstrakt: 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 FeCl 3 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 FeCl 3 . 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.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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