Tetrasodium pyrophosphate ameliorates oxidative damage to the TGase-catalyzed gelation of actomyosins
- Food Chem. 2022 Jun 1:378:132128. doi: 10.1016/j.foodchem.2022.132128.
- 1. College of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, China.
- 2. College of Food Science, Shenyang Agricultural University, Shenyang, Liaoning 110866, China.
- 3. College of Food Science, Shenyang Agricultural University, Shenyang, Liaoning 110866, China. Electronic address: [email protected].
The present study attempted to investigate the interactive roles of protein oxidation (0-20 mM H2O2) and tetrasodium pyrophosphate (TSPP) on the crosslinking efficiency of actomyosin mediated by Transglutaminase (TGase). Oxidation at 0-20 mM H2O2 was not conducive to TGase-mediated crosslinking as indicated by the relative reduction of free amine consumption from 35.3% to 11.7%, and caused the principle crosslinking sites to progressively convert from Myosin subfragment-1 (S1) to subfragment-1 (S2) as evidenced by electrophoresis. However, the binding of TSPP to Myosin alleviated oxidation suppression to TGase-catalyzed crosslinking in varying degrees and retarded the migration of crosslinking site from S1 to S2. Moreover, oxidation (especially 20 mM H2O2) decreased the final (90 °C) elasticity index (EI) and water holding capacity of TGase-treated actomyosin gel, while TSPP intensified those of TGase-catalyzed actomyosin gel, indicating that TSPP had a positive effect on ameliorating the oxidative stress to TGase-catalyzed gelation of actomyosin.
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Cat. No.Product NameDescriptionTargetResearch Area
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Research Areas: Infection