Journal
ULTRASONICS SONOCHEMISTRY
Volume 54, Issue -, Pages 311-320Publisher
ELSEVIER
DOI: 10.1016/j.ultsonch.2019.01.026
Keywords
Common carp (Cyprinus carpio); Ultrasound; Protein structure; Muscle microstructure; Protein thermal stability
Categories
Funding
- National Key Research and Development Plan during the 13th five-year plan period [2016YFD0401504-03]
- National Natural Science Foundation of China [31771990]
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This study investigated the effect of ultrasound-assisted immersion freezing (UIF) at different ultrasonic power levels on the myofibrillar protein primary, secondary and tertiary structures of common carp (Cyprinus catpio). Furthermore, protein thermal stability, electrophoresis pattern, and microstructure of the muscle tissue were also studied. Compared with a control, an ultrasonic power of less than 175 W had no significant negative effect on protein primary structure (P > 0.05), including total sulfhydryl, reactive sulfhydryl, carbonyl groups, free amino groups, dityrosine content, and surface hydrophobicity. UIF at 175 W (UIF-175) minimized the changes in protein secondary and tertiary structures. There were no obvious changes in the SDS-PAGE patterns of the control and frozen sample proteins. Microstructure analysis showed that an appropriate ultrasonic power (UIF175) promoted the formation of smaller and more uniform ice crystals, reduced the damage of muscle tissue by ice crystals, and maintained the sarcomere integrity. In addition, UIF-175 samples had higher protein thermal stability. Overall, ultrasound treatment at a proper power (UIF-175) effectively minimized the changes in protein structure and protected the protein thermal stability during freezing process.
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