2022
DOI: 10.1016/j.lwt.2021.112279
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Effect of κ-carrageenan on quality improvement of 3D printed Hypophthalmichthys molitrix-sea cucumber compound surimi product

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Cited by 40 publications
(18 citation statements)
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“…The gel matrix can be analyzed by using FT-IR spectroscopy to detect functional groups associated with intramolecular and intermolecular structures [ 38 ]. The amide bands of proteins have several distinct vibrational modes, including amide I, II, and III.…”
Section: Resultsmentioning
confidence: 99%
“…The gel matrix can be analyzed by using FT-IR spectroscopy to detect functional groups associated with intramolecular and intermolecular structures [ 38 ]. The amide bands of proteins have several distinct vibrational modes, including amide I, II, and III.…”
Section: Resultsmentioning
confidence: 99%
“…When heated MfP in fish mince crosslinked to form regular three‐dimensional gel network structures, water and other soluble ingredients could be trapped inside which offers the hydrogel good WHC. The WHC reflects the water retention ability of the gel under external forces, which is dependent on the variations in protein‐water interactions and gel structures (Yu et al, 2021). As shown in Figure 1a, the changes in WHC of GC‐FBs under the influence of EWP addition followed the same trend as that of the gel strength of the samples, with a correlation coefficient of .98.…”
Section: Resultsmentioning
confidence: 99%
“…The FT-IR spectra for crayfish meat gels as influenced by freeze-thawing treatments are displayed in Figure 5 C. The gels exhibited absorption bands at 3270 cm −1 (amide A, N–H or O–H stretching), 2920 cm −1 (amide B, C–H stretching), 1622 cm −1 (amide I, C=O and C=N stretching), 1521 cm −1 (amide II, C–N stretching and N–H bending), 1238 cm −1 (amide III, C–H bending), and 1071 cm −1 (C–O and C–C stretching) [ 14 ]. The migration of the amide A band could be used to estimate the interaction between protein and water molecules [ 37 ]. Commonly, the amide I band located at 1600–1700 cm −1 is often applied to estimate the information of protein secondary structures, including α-helix, β-turn, β-sheet, and random coil [ 14 ].…”
Section: Resultsmentioning
confidence: 99%