Curtailing Oxidation-Induced Loss of Myosin Gelling Potential by Pyrophosphate Through Shielding the S1 Subfragment

Zelong Liu, Alma D. True, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

In muscle food processing, where oxidation is inevitable, phosphates are usually added to improve water binding. This present study attempted to investigate the interactive roles of protein oxidation and pyrophosphate (PP) during thermal gelation of myosin. Myosin isolated from pork muscle was solubilized in 0.5 M NaCl at pH 6.2 then oxidatively stressed with an iron-redox cycling system that produces hydroxyl radicals with or without 1 mM PP and 2 mM MgCl2 at 4 °C for 12 or 24 h then heated to 50 °C at 1.3 °C/min. Protein conformational stability was measured by differential scanning calorimetry, and covalent cross-linking was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis following chymotrypsin digestion. The binding of PP to myosin suppressed disulfide bond formation in myosin subfragments 1 and 2 and partially inhibited oxidation-initiated cross-linking of heavy meromyosin during myosin gelation with a lesser effect on light meromyosin. In the presence of PP, myosin exhibited less loss of conformational integrity upon oxidation than myosin without PP. Rheological analysis from 20 to 75 °C indicated up to 32% decreases (P < 0.05) in elastic modulus (G′) of myosin gels due to oxidation. However, the presence of 1 mM PP, which also lowered the gelling capacity of myosin, inhibited the oxidation-induced G′ by nearly half (P < 0.05). These results suggest that the protection of myosin head from oxidative modification by PP can be a significant factor for the minimization of gelling property losses during cooking of comminuted meats. Practical Application: The association of myosin S1 subfragment possibly S2 as well with pyrophosphate prevents extensive myosin head-head cross-linking. This alleviates the negative impact of oxidation on the gel formation of myosin, an expected main form of myofibrillar protein due to pyrophosphate-induced actomyosin dissociation. Likewise, oxidative S1-S1 association inhibits the binding of pyrophosphate thereby reducing its gel-weakening effect. The mutual constraining roles of oxidation and pyrophosphate can be a significant factor for the minimization of gelling property losses during the manufacture of comminuted meat products.

Original languageEnglish
Pages (from-to)C1468-C1475
JournalJournal of Food Science
Volume80
Issue number7
DOIs
StatePublished - 2015

Bibliographical note

Publisher Copyright:
© 2015 Institute of Food Technologists®.

Keywords

  • Gelling properties
  • Myosin
  • Oxidation
  • Pyrophosphate

ASJC Scopus subject areas

  • Food Science

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