Related Experiment Video
Updated: Aug 2, 2025
Author Spotlight: Purifying High-Quality Tubulin to Study Protein Dynamics and Therapeutic Applications
Published on: October 11, 2024
Concentration-dependent effect of eugenol on porcine myofibrillar protein gel formation
Hongsheng Chen1, Jinming Ma2, Deyin Pan2
1College of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, United States; China-Canada Cooperation Agri-Food Research Center of Heilongjiang Province, Daqing, Heilongjiang 163319, China.
Abstract:
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.
