Tea Polyphenols Affect Oxidative Modification and Solution Stability of Myofibrillar Protein from Grass Carp ( Ctenophar
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ORIGINAL ARTICLE
Tea Polyphenols Affect Oxidative Modification and Solution Stability of Myofibrillar Protein from Grass Carp (Ctenopharyngodon idellus) Xuepeng Li 1,2 & Cikun Liu 1 & Jinxiang Wang 1 Hongbo Mi 1 & Jianrong Li 1
&
Wenxie Li 1 & Boyan Lin 1 & Wenhui Zhu 1 & Yongxia Xu 1 & Shumin Yi 1 &
Received: 30 January 2020 / Accepted: 29 April 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract This study investigated the effects of different concentrations (0, 5, 10, 20, 50, and 100 μmol/g protein) of tea polyphenols (TP) on the oxidative modification and the physicochemical, structural, and gelling properties of myofibrillar protein (MP) from grass carp (Ctenopharyngodon idellus) oxidized by a hydroxyl radical-generating system. The results showed that low concentrations (5 and 10 μmol/g protein) of TP could effectively inhibit the formation of carbonyl groups and dityrosine, the loss of sulfhydryl groups and α-helix conformation, and the change of the tertiary structure of MP caused by hydroxyl radicals. Moreover, the presence of TP in all concentrations decreased the surface hydrophobicity of MP. TP at 10 μmol/g protein had better effects on preventing the oxidation-induced cross-linking and aggregation of myosin heavy chain (MHC) and actin of MP, keeping the stability of MP solutions with lower turbiscan stability index (TSI) values, and improving gelling properties characterized by higher hardness and gel strength of MP gels. By contrast, excessive presence of TP (20, 50, and 100 μmol/g protein) showed prooxidative effects on oxidatively stressed MP, which was detrimental to the MP and contributed to the denaturation and irregular aggregation of MP, the loss of MP solution stability, and lower gelling capacity with poor texture and gel strength. The concentration-dependent effects of TP on MP depended on the extent of MP oxidative modification and MP-TP interactions, indicating that a proper amount of TP has the potential to protect MP from oxidation and to enhance the gelling capacity of surimi during processing. Keywords Tea polyphenols . Grass carp . Myofibrillar protein . Oxidation . Solution stability . Protein gelation
Graphical Abstract
Introduction Fish proteins are sensitive to oxidation reaction, which can be initiated directly by reactive oxygen radicals (ROS), such as superoxide radicals, peroxide radicals, or hydroxyl radicals, or * Jinxiang Wang [email protected] * Jianrong Li [email protected] 1
National R & D Branch Centre for Surimi and Surimi Products Processing, College of Food Science and Technology, Bohai University, Jinzhou 121013, China
2
School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore
indirectly by the byproducts of lipid oxidation, such as malondialdehydes, hydroperoxide, etc. Protein oxidation occurs during handling, processing, and storage of fish and fish products because of their exposure to oxygen and oxidant additives [1–3]. Oxidation can lead to modifications of protein side chains and b
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