Role of disulphide linkages between protein-coated lipid droplets and the protein matrix in the rheological properties of porcine myofibrillar protein-peanut oil emulsion composite gels

Mangang Wu, Youling L. Xiong, Jie Chen

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

The objective of the study was to establish disulphide interaction between protein-coated oil droplets and the surrounding protein matrix in myofibrillar protein (MP)-emulsion composite gels. An MP-stabilized peanut oil emulsion was treated with 0, 1, 3, 5 and 10. mM N-ethylmaleimide (NEM, a sulphydryl-blocking agent) and subsequently incorporated into a bulk MP sol to produce 5%-lipid, 2%-protein composites at pH 6.2. About 69% of sulphydryls in the emulsion (1% protein) were blocked by 1. mM NEM, and almost all were bound at ≥ 3. mM NEM. The loss of free sulphydryls resulted in a significant drop in the storage modulus (G') and rupture force of the composite gels. Microstructural examination revealed pores and oil leakage from emulsion droplets by NEM treatments, corresponding to declining rheological properties of the MP-emulsion composites. The results supported the hypothesis that disulphide cross-linking between MP-coated oil droplets and protein matrix contributed to the stabilization and reinforcement of protein-emulsion composite gels formed in comminuted muscle foods.

Original languageEnglish
Pages (from-to)384-390
Number of pages7
JournalMeat Science
Volume88
Issue number3
DOIs
StatePublished - Jul 2011

Bibliographical note

Funding Information:
The study was supported by the National Natural Science Foundation of China (grant no. 30972290 ), Program for Changjiang Scholars and Innovative Research Team, China (grant nos. IRT0627 and NCET-07-0377 ), the Ministry of Science and Technology, China (Grant no. 2010CB535014 ), and the State Key Laboratory of Food Science and Technology, Jiangnan University (grant no. SKLF-MB-200803 ).

Keywords

  • Disulphide
  • Emulsion
  • Gelation
  • Myofibrillar protein
  • N-ethylmaleimide

ASJC Scopus subject areas

  • Food Science

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