2020
DOI: 10.1039/d0ra04487c
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Gel properties of Amur sturgeon (Acipenser schrenckii) surimi improved by lecithin at reduced and regular-salt concentrations

Abstract: This study examined the gel properties of Acipenser schrenckii (A. schrenckii) surimi with 10 and 30 g kg−1 of added lecithin at reduced-salt (3 g kg−1 NaCl) and regular-salt (30 g kg−1 NaCl) concentrations.

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Cited by 14 publications
(10 citation statements)
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“…The protein structure changed with the crosslinking between Ca 2+ and NS‐L‐surimi, which was caused by the formation of a denser structure due to molecular linking. The hydration of Ca 2+ and NS‐L could compete with protein molecules to bind water molecules, which weakened the hydrogen bonds between protein−water and enhanced the hydrophobic environment of the protein surface 28 . Thus, the denser structure and the change of water distribution strengthened WHC, elasticity, resilience, as well as the gel strength.…”
Section: Resultsmentioning
confidence: 99%
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“…The protein structure changed with the crosslinking between Ca 2+ and NS‐L‐surimi, which was caused by the formation of a denser structure due to molecular linking. The hydration of Ca 2+ and NS‐L could compete with protein molecules to bind water molecules, which weakened the hydrogen bonds between protein−water and enhanced the hydrophobic environment of the protein surface 28 . Thus, the denser structure and the change of water distribution strengthened WHC, elasticity, resilience, as well as the gel strength.…”
Section: Resultsmentioning
confidence: 99%
“…The hydration of Ca 2+ and NS-L could compete with protein molecules to bind water molecules, which weakened the hydrogen bonds between protein−water and enhanced the hydrophobic environment of the protein surface. 28 Thus, the denser structure and the change of water distribution strengthened WHC, elasticity, resilience, as well as the gel strength. Moreover, the increased hydrophobicity with Ca 2+ was attributed to the salt dissolution of Ca 2+ stretched more protein molecules to expose more hydrophobic groups, making the hydrophobic force rise and the protein aggregate.…”
Section: Relationships Between Chemical Bonds and Mechanical Propertiesmentioning
confidence: 99%
“…The effects of lecithin addition at different levels on the breaking force and deformation of surimi gels are presented in Figure 2a and 2b, respectively. When heated, the myofibrillar proteins in salted surimi pastes reveal reactive surfaces, which collaborate to create intermolecular interactions [20]. A three-dimensional network arises when there are enough intermolecular bonds, producing a surimi gel.…”
Section: Breaking Force and Deformationmentioning
confidence: 99%
“…Hydrogen bonds strengthen the hydrogel during the cooling phase and help to stabilize the bound water inside of it. Temperature-induced strengthening of intermolecular hydrophobic contacts is thought to be the main mechanism underlying the creation of surimi gel [20].…”
Section: Breaking Force and Deformationmentioning
confidence: 99%
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