Journal
MEAT SCIENCE
Volume 88, Issue 3, Pages 384-390Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2011.01.014
Keywords
Myofibrillar protein; Emulsion; Disulphide; Gelation; N-ethylmaleimide
Categories
Funding
- National Natural Science Foundation of China [30972290]
- Innovative Research Team, China [IRT0627, NCET-07-0377]
- Ministry of Science and Technology, China [2010CB535014]
- State Key Laboratory of Food Science and Technology, Jiangnan University [SKLF-MB-200803]
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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. (c) 2011 Elsevier Ltd. All rights reserved.
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