2017
DOI: 10.1007/s11947-017-2025-x
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Denaturation Kinetics and Aggregation Mechanism of the Sarcoplasmic and Myofibril Proteins from Grass Carp During Microwave Processing

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Cited by 31 publications
(13 citation statements)
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“…Previous studies have shown that the increase in turbidity is related to the formation of protein molecular aggregates [ 48 ]. In addition, higher aggregation rates and higher turbidity increases were also observed for longer microwave heating times for grass carp sarcoplasmic and myogenic fiber proteins [ 49 ]. Therefore, we speculate that the increase in turbidity may be due to the unfolding of QPI molecules, when treated at higher temperature and for a long time, the intramolecular and intermolecular interaction forces of proteins are enhanced, resulting in substantial aggregation of proteins [ 50 ].…”
Section: Resultsmentioning
confidence: 99%
“…Previous studies have shown that the increase in turbidity is related to the formation of protein molecular aggregates [ 48 ]. In addition, higher aggregation rates and higher turbidity increases were also observed for longer microwave heating times for grass carp sarcoplasmic and myogenic fiber proteins [ 49 ]. Therefore, we speculate that the increase in turbidity may be due to the unfolding of QPI molecules, when treated at higher temperature and for a long time, the intramolecular and intermolecular interaction forces of proteins are enhanced, resulting in substantial aggregation of proteins [ 50 ].…”
Section: Resultsmentioning
confidence: 99%
“…3 C), the two peaks were slightly left-shifted, indicating a size decline. This in turn indicated that the protein subunits might be rearranged by the limited protein molecules due to the hydrophobic interactions that resisted electrostatic repulsion [49] . Nevertheless, the 100–1,000 nm peak appeared to strengthen, and the > 1,000 nm peak appeared to attenuate after HIU treatment; this could be explained by the loss of MHC ( Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The differences in cooking losses found in this study could be due to the appearance of an external layer in samples treated by roasting, grilling and frying, while, in the microwave process, this protective rind is not generated [ 25 , 39 ]. Besides, the structure and function of protein may also be influenced as a result of the high electromagnetic field used by microwaved, because this generates aggregates that can favour the release of water [ 40 ]. Moreover, grilled samples presented the lowest cooking losses and they were similar to those obtained for roasted.…”
Section: Resultsmentioning
confidence: 99%