Dose affected the role of gallic acid on mediating gelling properties of oxidatively stressed Japanese seerfish myofibrillar protein
Autor: | Ruoyi Hao, Hui Jia, Shengjie Li, Xiuping Dong, Jinfeng Pan, Yujie Wang, Hongliang Lian, Huapeng Ju |
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Rok vydání: | 2020 |
Předmět: |
0106 biological sciences
Chemistry Radical 04 agricultural and veterinary sciences Protein oxidation 040401 food science 01 natural sciences Adduct chemistry.chemical_compound 0404 agricultural biotechnology Polymerization 010608 biotechnology Biophysics Amine gas treating Gallic acid Myofibril Protein secondary structure Food Science |
Zdroj: | LWT. 118:108849 |
ISSN: | 0023-6438 |
DOI: | 10.1016/j.lwt.2019.108849 |
Popis: | The study investigated effects of gallic acid (GA, 0, 1, 5, 25 and 125 μmol/g) on properties of oxidatively stressed Japanese seerfish myofibrillar protein (MFP). Results showed that GA alleviated carbonyls formation and protected free amine. 5 μmol/g GA stabilized sulphydryls and secondary structure while 125 μmol/g GA enabled great loss of sulphydryls and reduced α-helix structure. Analysis of tryptophan fluorescence and surface hydrophobicity indicated that GA induced the unfolding of MFP structure but not in a dose-response fashion. Polymers were formed along with marked attenuation of myosin heavy chain in MFP with 125 μmol/g GA, and its particle size was the largest. Compared with purely oxidized MFP, MFP with 125 μmol/g GA showed a radical peak with narrower peak width but higher intensity. Results imply that high dose GA formed thiol-quinone adducts, enhancing polymerization. It also formed stable protein-bound phenoxyl radicals, inhibiting protein oxidation. Compared with non-oxidized group, storage modulus of MFP with 5 μmol/g GA increased sharply but that of MFP with 125 μmol/g GA decreased distinctly. The study suggests the role of GA on MFP depends much on its dose. Low dose GA could be used for improving fish MFP gelling property. |
Databáze: | OpenAIRE |
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