Effect of protein structure changes during different power ultrasound thawing on emulsification properties of common carp (Cyprinus carpio) myofibrillar protein

Effect of protein structure changes during different power ultrasound thawing on emulsification properties of common carp (Cyprinus carpio) myofibrillar protein

The impact of ultrasound thawing (UT) at different power (0 W, 100 W/0.132 W·cm , 300 W/1.077 W·cm , and 500 W/1.997 W·cm , namely WT, UT-100, UT-300, and UT-500) on protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein were investigated in...

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Veröffentlicht in:Ultrasonics sonochemistry 2023-12, Vol.101, p.106719-106719, Article 106719
Hauptverfasser: Sun, Qinxiu, Kong, Baohua, Zheng, Ouyang, Liu, Shucheng, Dong, Xiuping
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Carps
Emulsifying properties
Fish
Hydrophobic and Hydrophilic Interactions
Power
Protein Aggregates
Protein structure
Proteins
Solubility
Ultrasound thawing
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Zusammenfassung:The impact of ultrasound thawing (UT) at different power (0 W, 100 W/0.132 W·cm , 300 W/1.077 W·cm , and 500 W/1.997 W·cm , namely WT, UT-100, UT-300, and UT-500) on protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein were investigated in the present study. The result showed that the reactive sulfhydryl content, total sulfhydryl content, protein solubility, and absolute potential of UT-300 samples were obviously higher than those of other thawed samples, while the turbidity of UT-300 samples was lower (P 
ISSN:1350-4177
1873-2828
DOI:10.1016/j.ultsonch.2023.106719