2019
DOI: 10.1039/c9ra03517f
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Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)

Abstract: This work studied the effects of KGM with different degrees of deacetylation (DDs) on the physicochemical properties of silver carp (Hypophthalmichthys molitrix) surimi gels.

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Cited by 48 publications
(36 citation statements)
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“…The results are likely because the negative charge of gelatin or κ ‐carrageenan neutralized the positive charges exposed on the surimi protein surface and ruptured the ionic linkages . However, the differences in pH values might change the charge distribution sites of amino acids when excessive hydrocolloids were added into the surimi gels, resulting in a slight increase of ionic bonds and the observed decrease in gel strength (Figs and ) . Ding et al .…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The results are likely because the negative charge of gelatin or κ ‐carrageenan neutralized the positive charges exposed on the surimi protein surface and ruptured the ionic linkages . However, the differences in pH values might change the charge distribution sites of amino acids when excessive hydrocolloids were added into the surimi gels, resulting in a slight increase of ionic bonds and the observed decrease in gel strength (Figs and ) . Ding et al .…”
Section: Resultsmentioning
confidence: 99%
“…29 However, the differences in pH values might change the charge distribution sites of amino acids when excessive hydrocolloids were added into the surimi gels, resulting in a slight increase of ionic bonds and the observed decrease in gel strength (Figs 1 and 4). 30 Ding et al 31 also reported that the breaking force of surimi gels from yellowcheek carp and grass carp had a significant negative correlation with the ionic bonds content. In short, the hydrocolloids-protein interactions take place via ionic interaction, leading to changes in the gel strength and protein network structure of silver carp surimi.…”
Section: Soluble Protein Contentmentioning
confidence: 97%
“…The functional groups of WPC/PUL gels were evaluated by IR spectroscopy. A resolution of 4 cm −1 and wavenumber range of 4000–400 cm −1 were used 15 …”
Section: Methodsmentioning
confidence: 99%
“…A resolution of 4 cm −1 and wavenumber range of 4000-400 cm −1 were used. 15 Low amplitude dynamic oscillatory measurements Changes in storage modulus (G") and loss modulus (G") of WPC/PUL gels during the forming process were determined by a controlled stress rheometer (MARS 60; Thermo Fisher Scientific Ltd., Waltham, MA, USA) using dynamic oscillation measurements. The parameters were 1 Hz, strain amplitude of 2% and gap of 1 mm.…”
Section: Infrared (Ir) Spectroscopymentioning
confidence: 99%
“…This corresponded to the lowest TCA-soluble peptide content (Table 1), owing to the effectiveness of adequate washing, which can remove endogenous protease enzymes. To avoid gel weakening caused by leftover proteases, the surimi preparation was set at 40 • C, and cooked at 90 • C. Myosin denatures and aggregates more at 48 • C, eventually producing a stable gel [40]. The G' was then increased once again, peaking around 65-69 • C, suggesting the establishment of a strong gel network due to higher attractive forces (e.g., disulfide bond, and hydrophobic interaction).…”
Section: Oscillatory Dynamic Rheologymentioning
confidence: 99%