Glucose oxidase promotes gallic acid-myofibrillar protein interaction and thermal gelation

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51 Scopus citations


The effect of glucose oxidase (GOx)catalytic oxidation on the efficacy of gallic acid (GA)to modify the chemical structure and gelling behavior of myofibrillar protein (MP)was investigated. In contrast to non-oxidized MP samples where GA induced very little changes, GA (0, 6, 30, and 60 µmol/g MP)under GOx treatment promoted sulfhydryl and amine loss (up to 58% and 49%, respectively). The attenuation of intrinsic tryptophan fluorescence in the GA/GOx-treated MP corroborated the finding. The gelling capacity of MP, corresponding to disulfide and non-disulfide bond formation in protein aggregates, was markedly enhanced by 60 µmol GA under GOx, up to 86% in gel storage modulus G' and 53% in gel strength. The GOx-aided GA modification of MP could be a potential ingredient strategy in meat processing to promote textural attributes of cooked products.

Original languageEnglish
Pages (from-to)529-536
Number of pages8
JournalFood Chemistry
StatePublished - Sep 30 2019

Bibliographical note

Publisher Copyright:
© 2019 Elsevier Ltd


  • 2,4,6-Trinitrobenzenesulfonic acid (PubChem CID: 11045)
  • 2,4-Dinitrophenylhydrazine (PubChem CID: 3772977)
  • 5,5′-Dithio-bis(2-nitrobenzoic acid)(PubChem CID: 6254)
  • Gallic acid
  • Gallic acid (PubChem CID: 370)
  • Gelation
  • Glucose oxidase
  • Glucose oxidase (PubChem CID: 11973707)
  • Meat
  • Myofibrillar protein
  • β-Mercaptoethanol (PubChem CID: 1567)

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science


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