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.
|Number of pages||7|
|State||Published - Jul 2011|
Bibliographical noteFunding 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 ).
- Myofibrillar protein
ASJC Scopus subject areas
- Food Science