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

Anqi Guo, Jiang Jiang, Alma D. True, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

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.

Original languageEnglish
Pages (from-to)1308-1317
Number of pages10
JournalJournal of Agricultural and Food Chemistry
Volume69
Issue number4
DOIs
StatePublished - Feb 3 2021

Bibliographical note

Publisher Copyright:
© 2021 American Chemical Society.

Keywords

  • gelation
  • glucose oxidase
  • myofibrillar protein
  • phenolics
  • protein and lipid oxidation

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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