2020
DOI: 10.1016/j.foodhyd.2020.105779
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Chemical interactions involved in microwave heat-induced surimi gel fortified with fish oil and its formation mechanism

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Cited by 78 publications
(56 citation statements)
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“…Sulfhydryl groups buried in protein are exposed during heating process and subsequently generate disulfide cross-linking [ 23 ]. The disulfide bonds display a type of rheological behavior known as rubber elasticity, and they are critical to maintaining network stability [ 34 ].…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Sulfhydryl groups buried in protein are exposed during heating process and subsequently generate disulfide cross-linking [ 23 ]. The disulfide bonds display a type of rheological behavior known as rubber elasticity, and they are critical to maintaining network stability [ 34 ].…”
Section: Resultsmentioning
confidence: 99%
“…The chemical interactions or bonds were determined according to the method of Yan et al [ 23 ] with slight modifications. Briefly, 1 g of surimi gels was added 10 mL 0.05 M NaCl (A), 0.6 M NaCl (B), 0.6 M NaCl + 1.5 M urea (C), and 0.6 M NaCl + 8 M urea (D) and homogenized for 2 min by homogenizer (Shanghai Fokker Equipment Co. Ltd., Shanghai, China).…”
Section: Methodsmentioning
confidence: 99%
“…Therefore, the nutritional enhancement of surimi products has become a significant research direction [3] , [4] . In response to this problem, the research thus far has been focused on add exogenous lipids, mainly vegetable oil [3] , [4] , [5] , [6] , [7] and animal fat [2] , [8] , [9] , which can not only enhance the nutrition but also improve the color and flavor of surimi products [3] , [10] .…”
Section: Introductionmentioning
confidence: 99%
“…However, when the addition of CO exceeded 40 mgÁmL −1 , the S 0 -ANS of MP gel showed a downward trend. This may be owing to the spatial hindrance caused by hydrophobic interaction between protein and oil, which hindered the rearrangement and further unfolding of protein molecular structures (Yan et al, 2020). Zhou et al, (2021) found that hydrophobic groups of MP molecules sufficiently contacted with the fat particles due to the emulsification effect, which formed the protein-coated fat droplets and made it difficult to be detected using ANS reagents.…”
Section: Hydrophobic Interactionmentioning
confidence: 99%
“…4), indicating that the structure of MP gels had changed. Amide I band (1600-1700 cm −1 ) is the most easily identified band to demonstrate protein secondary structure, which includes the α-helix, β-sheet, β-turn and random coil (Shao et al, 2011;Yan et al, 2020). After microwave heating treatment, α-helix composed around 40% of the secondary structure of MP with different CO addition.…”
Section: Secondary Structurementioning
confidence: 99%