Journal
FOOD CHEMISTRY
Volume 428, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2023.136687
Keywords
Curcumin; Myofibrillar protein; Emulsification; Gelation
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The regulation mechanism of curcumin on the emulsification and gelation properties of myofibrillar protein was studied. Curcumin increased the emulsifying activity index of myofibrillar protein but decreased its turbiscan stability index and surface hydrophobicity, leading to oil droplet aggregation. Medium amounts of curcumin changed the 3D network architectures of emulsion gels, improving their water-holding capacity, storage modulus, springiness, and cohesiveness. The presence of curcumin also affected the secondary structure of myofibrillar protein in the gels. Overall, curcumin has the potential to be used as a structural modifier in emulsified meat products due to its dose-response.
The regulation mechanism of curcumin (CUR) in the oil phase on the emulsification and gelation properties of myofibrillar protein (MP) was investigated. CUR enhanced the emulsifying activity index (EAI) of MP but decreased its turbiscan stability index (TSI) and surface hydrophobicity, which exacerbated oil droplet aggre-gation. Medium amounts (200 mg/L) of CUR changed the 3D network architectures of emulsion gels from lamellar to reticular, improving the gels' water-holding capacity (WHC), storage modulus, springiness, and cohesiveness. Besides, the LF-NMR revealed that CUR had limited effects on the mobility of immobilized and free water. The & alpha;-helix of MP in gels with medium amounts of CUR decreased from 51% to 45%, but the & beta;-sheet increased from 23% to 27% compared to those without CUR. Overall, CUR has the potential to become a novel structural modifier in emulsified meat products due to its dose-response.
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