Tetrasodium pyrophosphate ameliorates oxidative damage to the TGase-catalyzed gelation of actomyosins

Abstract

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.

Keywords: 2,4,6-Trinitrobenzenesulfonic acid (PubChem CID: 11045); Acrylamide (PubChem CID6579); Actomyosin; Coomassie brilliant blue R250 (PubChem CID: 23693030); Gelation; N-Ethylmaleimide (PubChem CID: 4362); Phenylmethylsulfonyl fluoride (PubChem CID: 4784); Piperazine-N,N'-bis(2-ethanesulfonic acid) (PubChem CID: 79723); Propyl gallate (PubChem CID: 4947); Protein oxidation; Tetrasodium pyrophosphate; Tetrasodium pyrophosphate (PubChem CID: 24403); Transglutaminase; Trolox C (PubChem CID: 40634); β-Mercaptoethanol (PubChem CID: 1567).