Structural Changes of Myofibrillar Proteins in Marinated Duck Drumsticks during Ultra-high Pressure Processing Treatment
To investigate the improvement mechanism of ultra-high pressure treatment on the tenderness of marinated duck drumsticks,this study analyzed the pattern of structural changes of myofibrillar proteins during ultra-high pressure processing(400 MPa,15 min)by determining the surface hydrophobicity,sulfhydryl content,chemical force,secondary structure and microstructure.The results showed that the hydrophobicity of myofibrillar proteins initially increased and then decreased,reaching a maximum of 51.03 after 12 min of treatment.The total thiol content decreased by 40.6％ after 15 min of treatment,while the free thiol content increased by 42.7％ ,and disulfide bonds significantly(P＜0.05)increased by 189.2％ .Tryptophan and tyrosine residues were exposed,indicating changes in protein tertiary structure.After 15 min of ultra-high pressure treatment,the α-helix content of myofibrillar protein decreased from 20.63％ to 13.45％ ,and the content of irregular coils increased from 23.93％ to 28.67％ ,suggesting rearrangement of the protein secondary structure.SDS-PAGE electrophoresis and scanning electron microscopy results demonstrated protein depolymerization of ultra-high pressure processing treatment,significant reduction in particle size,and more uniform distribution.In conclusion,during ultra-high pressure processing,significant changes occur in the tertiary structure,secondary structure,and microstructure of duck drumsticks myofibrillar proteins,contributing to the improvement of duck meat tenderness.This study would provide a theoretical basis for the application of ultra-high pressure technology in improving meat tenderness.
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