Influence of repeated freeze–thaw treatments on the functional and structural properties of myofibrillar protein from mirror carp (Cyprinus carpio L.)

The influence of repeated freeze–thaw (F-T) treatments (0, 1, 3 and 5) on the functional and structural properties of myofibrillar protein (MP) from mirror carp ( Cyprinus carpio L. ) was investigated according to the changes in rheological properties, particle distribution, Zeta (ζ)-potential, mole...

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Bibliographic Details
Published in:Food biophysics 2021-12, Vol.16 (4), p.492-501
Main Authors: Du, Xin, Li, Haijing, Nuerjiang, Maheshati, Rui, Litong, Kong, Baohua, Xia, Xiufang, Shao, Meili
Format: Article
Language:English
Subjects:
Analytical Chemistry
Biological and Medical Physics
Biophysics
Carp
Chemistry
Chemistry and Materials Science
Coils
Cyprinus carpio
Disulfide bonds
Food Science
Fourier transforms
Freeze-thawing
Hydrogen bonding
Hydrogen bonds
Hydrophobicity
Infrared spectra
Loss modulus
Original Article
Proteins
Random coil
Rheological properties
Storage modulus
Structure-function relationships
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Summary:The influence of repeated freeze–thaw (F-T) treatments (0, 1, 3 and 5) on the functional and structural properties of myofibrillar protein (MP) from mirror carp ( Cyprinus carpio L. ) was investigated according to the changes in rheological properties, particle distribution, Zeta (ζ)-potential, molecular force, Fourier transform infrared (FTIR) spectra and sulfhydryl content. After F-T treatment with five cycles, a significant decrease in the storage modulus values ( G' ), loss modulus values ( G" ), ζ- potential, total sulfhydryl content and reactive sulfhydryl content of MP was observed ( P  
ISSN:1557-1858
1557-1866
DOI:10.1007/s11483-021-09689-5