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Myofibrillar Protein Cross-Linking and Gelling Behavior Modified by Structurally Relevant Phenolic Compounds

Guo, Anqi, Jiang, Jiang, True, Alma D., Xiong, Youling L.·2021·Journal of Agricultural and Food Chemistry

Abstract

Protein gelation is an important phenomenon in processed meats. The present study investigated the structure-activity relationship of six phenolic compounds, that is, gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) in a myofibrillar protein (MP) gelling system under controlled oxidative conditions. All phenolics induced unfolding and promoted cross-linking of MP via sulfhydryl or amine groups. At an equal molar concentration, EGCG boosted the elastic MP gel network more than other phenolics except PG. However, all three monophenols (GA, CA, and PG) and the diphenol QT increased the MP gel strength more than CC (diphenol) and EGCG (triphenol). The flavanol structure appeared to interfere with the protein gel structure development. All phenolics retarded lipid oxidation in MP-emulsion composite gels during refrigerated storage with the least polar phenolic compounds, PG and QT, showing the greatest efficacy.

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Cited by

Metadata

Authors
Guo, A., Jiang, J., True, A. D., & Xiong, Y. L.
Affiliations
  • Department of Animal and Food Sciences, University of Kentucky, Lexington, Kentucky 40546, United States
  • College of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China
Venue
Journal of Agricultural and Food Chemistry
Published
2021-01-25
Volume
69
Issue
4
Pages
1308-1317
ISSN
  • 0021-8561
  • 1520-5118
Cited by
120
References
1
Language
en
Funders
National Institute of Food and Agriculture (1020736)

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.