Journal
MEAT SCIENCE
Volume 201, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2023.109187
Keywords
Eugenol; Myofibrillar protein; Gelation; Rheology; Texture
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The effects of different concentrations of eugenol (EG) on the structural properties and gelling behavior of myofibrillar proteins (MPs) were investigated. EG decreased protein content and stability, but increased hydrophobicity and aggregation of MPs. The gelling properties of MPs were improved at lower EG concentrations, but hindered at higher concentrations.
The effects of different concentrations of eugenol (EG = 0, 5, 10, 20, 50, and 100 mg/g protein) on the structural properties and gelling behavior of myofibrillar proteins (MPs) were investigated. The interaction of EG and MPs decreased free thiol and amine content, and reduced tryptophan fluorescence intensity and thermal stability, but enhanced surface hydrophobicity and aggregation of MPs. Compared with the control (EG free), the MPs' gels treated with 5 and 10 mg/g of EG had a higher storage modulus, compressive strength, and less cooking loss. A high microscopic density was observed in these EG-treated gels. However, EG at 100 mg/g was detrimental to the gelling properties of the MPs. The results indicate that an EG concentration of 20 mg/g is a turning point, i.e., below 20 mg/g, EG promoted MPs gelation, but above 20 mg/g, it impeded gelation by interfering with protein network formation. The EG modification of MPs could provide a novel ingredient strategy to improve the texture of comminuted meat products.
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