Dose affected the role of gallic acid on mediating gelling properties of oxidatively stressed Japanese seerfish myofibrillar protein. (January 2020)

• Record Type: Journal Article
• Authors: Pan, Jinfeng; Lian, Hongliang; Jia, Hui; Hao, Ruoyi; Wang, Yujie; Ju, Huapeng; Li, Shengjie; Dong, Xiuping
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 118(2020)
• Publication Date: 2020-01
• Subjects: Gallic acid -- Myofibrillar protein -- Thiol-quinone adduct -- Phenoxyl radicals -- Rheological properties; Gallic acid (PubChem CID: 370) -- Trolox (PubChem CID: 40634) -- 2, 4-Dinitrophenylhydrazine (PubChem CID: 3772977) -- Bromophenol blue (PubChem CID: 8272) -- 2, 4, 6-Trinitrobenzenesulfonic acid (PubChem CID: 11045) -- 5, 5′-Dithiobis-(2-nitrobenzoic acid) (PubChem CID: 6254) -- β-mercaptoethanol (PubChem CID: 1567) -- Phenylmethylsulfonyl fluoride (PubChem CID: 4784) -- N-ethylmaleimide (PubChem CID: 4362); Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2019.108849
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: 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. Highlights: GA alleviated carbonyls formation, protected free amine, induced structure unfolding. Sulphydryl and α-helix structure content was stable in OX+5 but declined in OX+125. New polymers formed along with attenuation of MHC band in OX+125. G′ of OX+5 increased while G′ of OX+125 decreased compared with it of NOX. OX+125 radical peak showed narrower width, higher intensity than OX+0 radical peak.