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2021
DOI: 10.1007/s11483-021-09689-5
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Influence of repeated freeze–thaw treatments on the functional and structural properties of myofibrillar protein from mirror carp (Cyprinus carpio L.)

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Cited by 12 publications
(6 citation statements)
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“…Endogenous fluorescence spectroscopy is widely used to measure tryptophan residues with the aim of evaluating the changes in protein tertiary structures ( Du et al, 2021 ). Aromatic amino acid residues are the main contributors to the intrinsic fluorescence of proteins, such as tryptophan, tyrosine, and phenylalanine.…”
Section: Resultsmentioning
confidence: 99%
“…Endogenous fluorescence spectroscopy is widely used to measure tryptophan residues with the aim of evaluating the changes in protein tertiary structures ( Du et al, 2021 ). Aromatic amino acid residues are the main contributors to the intrinsic fluorescence of proteins, such as tryptophan, tyrosine, and phenylalanine.…”
Section: Resultsmentioning
confidence: 99%
“…Subsequent trials found that the freeze-thawing caused MP denaturation and aggregation, as evidenced by the reduced protein solubility and Ca 2+ -ATPase activity, the increased particle size, and the high molecular weight of MP, as well as the increased average roughness of the MP film (Rg, atomic force microscopy), leading to the reduced gel-forming ability. A previous study on the MP gelling properties of mirror carp treated with freeze-thawing (frozen at −25 °C and thawed at 4 °C for 12 h) found that freeze-thawing decreased the storage modulus G’ of MP gels, and the ζ-potential of MP declined from 26.87 mV to 23.9 mV, while the median diameter ( d V,0.5 ) of protein increased from 24.41 μm to 32.3 μm, implying protein aggregation of MP occurred during freeze-thawing [ 29 ]. Consequently, changes in the functional and structural properties of MP are responsible for the decreased gelling properties.…”
Section: Resultsmentioning
confidence: 99%
“…Additionally, it was also found that the SF led to a significant rise in the β-sheet content of crayfish gels ( p < 0.05) at the expense of α-helix, presumably due to the disruption of hydrogen bonding in α-helix by large ice crystals during slow freezing. It has been reported that freeze-thaw treatments could promote the conversion of α-helix (ordered rigid structure) to a relatively loose β sheet (disordered flexible structure) in the MP of mirror carp ( Cyprinus carpio L.), owing to the broken hydrogen bonds by physical effects as well as the protein oxidation accelerated by freeze-thawing [ 29 ]. Therefore, freeze-thawing not only affects the tertiary structure of crayfish meat gels, but also the secondary structure.…”
Section: Resultsmentioning
confidence: 99%
“…Referring to the method of Du et al . (2021), the krill mince was lyophilized and mixed thoroughly with potassium bromide in a mass ratio of 1:100 in an agate mortar. The sample was put in Fourier Transform Infrared Spectroscopy (Spectrum II PerkinElmer, Japan) for measurements from 4000 to 400 cm −1 .…”
Section: Methodsmentioning
confidence: 99%