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1.
Environ Pollut ; 343: 123161, 2024 Feb 15.
Article in English | MEDLINE | ID: mdl-38104760

ABSTRACT

In this study, ceria nanoparticle (CNP) was used as a capping agent to investigate the efficiency and mechanism of simultaneously controlling the release of sediment internal Arsenic (As) and tungsten (W). The results of incubation experiment demonstrated that CNP capping reduced soluble As and W by 81.80% and 97.97% in overlying water, respectively; soluble As and W by 65.64% and 60.13% in pore water, respectively; and labile As and W in sediment by 45.20% and 53.20%, respectively. The main mechanism of CNP controlling sediment internal As and W was through adsorption via ligand exchange and inner-sphere complexation, as determined through adsorption experiments, XPS and FIRT spectra analysis. Besides, CNP also acted as an oxidant, facilitating the oxidation of AsⅢ to AsV and thereby enhancing the adsorption of soluble As. Additionally, sediment As and W fractions experiments demonstrated that the immobilization of As and W with CNP treatment via transforming mobile to stable fractions was another mechanism inhibiting sediment As and W release. The obtained significant positive correlation between soluble As/W and Fe/Mn, labile As/W and Fe/Mn indicated that iron (Fe) and manganese (Mn) oxidation, influenced by CNP, serve as additional mechanisms. Moreover, Fe redox plays a crucial role in controlling internal As and W, while Mn redox plays a more significant role in controlling As compared to W. Meanwhile, CNP capping effectively prevented the release of As and W by reducing the activity of microorganisms that degrade Fe-bound As and W and reduced the release risk of V, Cr, Co, Ni, and Zn from sediments. Overall, this study proved that CNP was a suitable capping agent for simultaneously controlling the release of As and W from sediment.


Subject(s)
Arsenic , Metals, Heavy , Water Pollutants, Chemical , Arsenic/analysis , Tungsten , Geologic Sediments , Metals, Heavy/analysis , Manganese/analysis , Water , Water Pollutants, Chemical/analysis , Phosphorus
2.
Int J Biol Macromol ; 253(Pt 3): 126815, 2023 Dec 31.
Article in English | MEDLINE | ID: mdl-37690646

ABSTRACT

The relationship between myosin denaturation, aggregation and water migration in Nemipterus virgatus myosin gels with different treatment processes under optimal low pressure coupled with heat treatment was investigated to clarify the molecular mechanism of water migration. With the different treatment processes, the proportion of bound water of the myosin gels increased significantly (P < 0.05). Denaturation of myosin S1 sub-fragments and α-helical unfolding during different treatment processes led to an increase in ß-sheets content. These promote increased exposure of Try residues and hydrophobic groups of myosin, formation of clathrate hydrates, and reduced mobility of bound water. Furthermore, hydrophobic interactions and disulfide bonds caused the head-head and head-hinge to coalesce into a 3D honeycomb network with greater fractal dimension, less lacunarity, smaller water hole diameter and more water holes. This increased the capillary pressure experienced by the bound water, causing immobile water to migrate towards the bound water. The present study may be necessary to improve the mechanism of water migration in protein gel systems and to promote the industrial application of high pressure processing technology in surimi-based foods.


Subject(s)
Hot Temperature , Water , Animals , Fishes/metabolism , Myosins/metabolism , Gels/chemistry , Fish Products/analysis
3.
Food Res Int ; 157: 111230, 2022 07.
Article in English | MEDLINE | ID: mdl-35761546

ABSTRACT

The effect of optimal low-level pressure coupled with heat treatment (OPH treatment) on the gel properties and water migration of Nemipterus virgatus surimi was studied and compared with optimal high-pressure processing treatment (OP treatment) and traditional two-stage heat treatment (H treatment). Furthermore, the mechanism of OPH treatment in improving the gel properties were explored based on myosin. OPH treatment was found to be more conducive in improving the gel strength and water-holding capacity (WHC) of surimi gel than H or OP treatments. Moreover, OPH treatment induced an increase in the proportion of myosin ß-sheets and exposed more intramolecular Tyr residues as compared to the other two treatments, which promoted myosin to form large protein clusters through disulfide bonds and hydrophobic interactions, and a honeycomb three-dimensional network structure with larger fractal dimension, lower porosity, smaller water hole diameter, and a greater number of water holes, was obtained. These helped the OPH-induced surimi gel lock in more unfrozen bound water and immobile water, and ultimately rendered better gel properties.


Subject(s)
Fish Products , Water , Animals , Fish Products/analysis , Fishes , Gels/chemistry , Hot Temperature , Myosins/chemistry
4.
Foods ; 10(8)2021 Aug 05.
Article in English | MEDLINE | ID: mdl-34441590

ABSTRACT

The effect of the amount of ice added (20-60%) on the gel properties and water migration of Nemipterus virgatus surimi gel obtained with two-stage heat treatment was studied. The gel strength and water-holding capability (WHC) of the surimi gel with 30% ice added were significantly higher than those of other treatment groups (p < 0.05). The addition of 30% ice was conducive to the increase of protein ß-sheet proportion during heat treatment, exposing more reactive sulfhydryl groups. These promoted the combination of protein-protein through disulfide bonds and hydrophobic-hydrophobic interactions, forming an ordered three-dimensional gel network structure. Meanwhile, the increase in hydrogen bonds promoted the protein-water interaction. Low-field nuclear magnetic resonance analysis showed that more bound water was locked in the gel system, reducing the migration of immobile water to free water and finally showing better gel properties. When the amount of ice added was insufficient (20%), the gel structure lacked the support of immobile water, resulting in deterioration of gel strength. However, excessive addition of ice (>30%) was not conducive to the combination of protein-protein and protein-water, forming a large and rough gel structure, resulting in the migration of immobile water to free water and ultimately exhibited weak gel properties.

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