The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.
|Number of pages||9|
|State||Published - Aug 1 2015|
Bibliographical noteFunding Information:
The authors would like to acknowledge the financial support from the China Scholarship Council ( CSC ) to grant author Cao the opportunity to perform the study at the University of Kentucky. The study was supported by National Natural Science Foundation , China (Grant 31301497 ) and the USDA National Institute of Food and Agriculture , USA. (Hatch project 1005724 ). Approved for publication as journal article number 14-07-092 by the Director of the Kentucky Agricultural Experiment Station.
© 2015 Elsevier Ltd.
Copyright 2015 Elsevier B.V., All rights reserved.
- Chlorogenic acid
- Myofibrillar protein
- Protein gelation
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science