2017
DOI: 10.1002/jsfa.8242
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Gelation of barramundi (Lates calcarifer) minced muscle as affected by pressure and thermal treatments at low salt concentration

Abstract: P-C treatment can reduce salt concentration added to barramundi gels to 10 g kg . P-S and P-C treatment can result in higher mechanical and functional properties of barramundi gels at conventional salt concentration (20 g kg ) as compared to HI gels. © 2017 Society of Chemical Industry.

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Cited by 9 publications
(7 citation statements)
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References 33 publications
(80 reference statements)
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“…Most of the water loss during cooking was from the juice expelled by protein denaturation. Changes in muscle protein solubility represent an increase in protein denaturation, as the solubility decreases due to the formation of insoluble protein aggregates that cannot be extracted (Truong, Buckow, Nguyen, & Furst, 2017). It has been reported that significant differences were detected in the effects of cooking methods on the solubility of total proteins of treated samples (Dai et al ., 2014).…”
Section: Discussionmentioning
confidence: 99%
“…Most of the water loss during cooking was from the juice expelled by protein denaturation. Changes in muscle protein solubility represent an increase in protein denaturation, as the solubility decreases due to the formation of insoluble protein aggregates that cannot be extracted (Truong, Buckow, Nguyen, & Furst, 2017). It has been reported that significant differences were detected in the effects of cooking methods on the solubility of total proteins of treated samples (Dai et al ., 2014).…”
Section: Discussionmentioning
confidence: 99%
“…Salt‐soluble protein content indicates the degree of myofibrillar protein denaturation and aggregation 23 . In general terms, HPP pretreatment decreased salt‐soluble protein content in comparison with non‐treated samples (Fig.…”
Section: Resultsmentioning
confidence: 92%
“…The freeze‐driven weight loss reductions observed after HPP pretreatment have been related to the protein structural changes induced by pressure 13 . In this regard, several authors observed muscle compaction and protein gelation in micrographs of HPP‐treated fish samples, 4,6,23 which could lead to the muscle displaying better water retention ability 6 …”
Section: Resultsmentioning
confidence: 99%
“…High pressure causes protein denaturation with increased pressure and temperature. [11,30] The reason for this is that the combination of pressure and heat improve the efficiency of protein aggregation and gelation and lead to heat-induced helix-coil transition. [31] Thus, here, excessive temperature resulted in the weakening of molecular interactions and the destruction of the network structure in gels.…”
Section: Instrumental Texturementioning
confidence: 99%