Phosphorylation modification of myofibrillar proteins by sodium pyrophosphate affects emulsion gel formation and oxidative stability under different pH conditions
Author:
Affiliation:
1. College of Biotechnology and Food Science
2. Tianjin University of Commerce
3. Tianjin 300134
4. China
5. Tianjin Key Laboratory of Food Biotechnology
Abstract
The work explored the mechanisms responsible for the enhanced emulsion gel properties of myofibrillar proteins by phosphorylation modification.
Funder
National Natural Science Foundation of China
National Basic Research Program of China
Publisher
Royal Society of Chemistry (RSC)
Subject
General Medicine,Food Science
Link
http://pubs.rsc.org/en/content/articlepdf/2019/FO/C9FO01397K
Reference47 articles.
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3. 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
4. Cold gelation of β-lactoglobulin oil-in-water emulsions
5. Transglutaminase-set soy globulin-stabilized emulsion gels: Influence of soy β-conglycinin/glycinin ratio on properties, microstructure and gelling mechanism
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