High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution

Xing Chen, Youling L. Xiong, Xinglian Xu

Research output: Contribution to journalArticlepeer-review

84 Scopus citations

Abstract

This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H 2 O 2 , at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of H 2 O 2 blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H 2 O 2 by disrupting the intact myofibril structure and exposing buried –SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g H 2 O 2 , while untreated samples formed a gel upon heating. These results proved that HPH combined with H 2 O 2 is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.

Original languageEnglish
Pages (from-to)31-38
Number of pages8
JournalFood Chemistry
Volume285
DOIs
StatePublished - Jul 1 2019

Bibliographical note

Publisher Copyright:
© 2019 Elsevier Ltd

Keywords

  • Heat stability
  • High-pressure homogenization
  • Hydrogen peroxide
  • Myofibrillar protein
  • Protein beverage
  • Sulfhydryl blockage

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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