Weiqing Sun
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Weiqing Sun has a total of 76 co-authors. Here are the top co-authors by number of shared publications:
Jing Ma
College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China
24 shared publicationsKun Yang
College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China; College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, PR China
10 shared publicationsYuanhua Zhou
School of Mechanical Engineering, Yangtze University, Jingzhou, Hubei 434023, PR China
9 shared publicationsDi Wu
College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China
8 shared publicationsYunhua Zhang
School of Mechanical Engineering, Yangtze University, Jingzhou, Hubei 434023, PR China
8 shared publicationsJingjiao Jiang
College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China
7 shared publications
Latest Publications
- 12 June 2026
- Published by Elsevier in Food Chemistry
- Vol. 523, 150039
Mechanism of enhanced salt taste perception in magnetic field-mediated/gum arabic-induced low-salt myofibrillar protein gel
- 12 June 2026
- Published by Elsevier in Food Chemistry
- Vol. 523, 150039
Mechanism of enhanced salt taste perception in magnetic field-mediated/gum arabic-induced low-salt myofibrillar protein gel
- 13 September 2025
- Published by Elsevier in Food Chemistry
- Vol. 495 (Pt 1) , 146351
Mechanism study of delaying thermal aggregation behavior of low-salt myosin by magnetic field pretreatment
- 13 September 2025
- Published by Elsevier in Food Chemistry
- Vol. 495 (Pt 1) , 146351
Mechanism study of delaying thermal aggregation behavior of low-salt myosin by magnetic field pretreatment
- 13 January 2025
- Published by Elsevier in Food Chemistry
- Vol. 472, 142899
Magnetic field-mediated oxidative modification of myoglobin: One effective method for improving the gel properties of myofibrillar protein
- 13 January 2025
- Published by Elsevier in Food Chemistry
- Vol. 472, 142899
Magnetic field-mediated oxidative modification of myoglobin: One effective method for improving the gel properties of myofibrillar protein
- Open Access
- 27 December 2024
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 26 (1) , 139
Development of Sensitive R6G/AuNCs Ratiometric Fluorescent Probes for the Detection of Biogenic Amines in Fish Products
Biogenic amines (BAs), produced in fish and seafood due to microbial contamination, pose significant health risks. This study introduces a novel ratiometric fluorescent probe, synthesized by integrating rhodamine 6G(R6G) and gold nanoparticles (AuNCs), for the sensitive and specific detection of BAs. The probe operates on the principle of BAs hydrolysis, catalyzed by diamine oxidase, to produce hydrogen peroxide (H2O2), which selectively quenches the fluorescence of AuNCs at 620 nm, while the fluorescence of R6Gat 533 nm remains unaffected. The ratio of I620/I553 demonstrated excellent linearity with a wide dynamic range (1–1000 μM) and a low detection limit of 0.1 μM. Validation using grass carp samples showed high recovery rates (97.57% to 104.29%), confirming the probe’s efficacy and potential for practical application in food safety monitoring.
- 27 December 2024
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 26 (1) , 139
Open AccessDevelopment of Sensitive R6G/AuNCs Ratiometric Fluorescent Probes for the Detection of Biogenic Amines in Fish Products
Biogenic amines (BAs), produced in fish and seafood due to microbial contamination, pose significant health risks. This study introduces a novel ratiometric fluorescent probe, synthesized by integrating rhodamine 6G(R6G) and gold nanoparticles (AuNCs), for the sensitive and specific detection of BAs. The probe operates on the principle of BAs hydrolysis, catalyzed by diamine oxidase, to produce hydrogen peroxide (H2O2), which selectively quenches the fluorescence of AuNCs at 620 nm, while the fluorescence of R6Gat 533 nm remains unaffected. The ratio of I620/I553 demonstrated excellent linearity with a wide dynamic range (1–1000 μM) and a low detection limit of 0.1 μM. Validation using grass carp samples showed high recovery rates (97.57% to 104.29%), confirming the probe’s efficacy and potential for practical application in food safety monitoring.
- 27 December 2024
- Published by Elsevier in Food Chemistry
- Vol. 470, 142681
Magnetic fields improve the gel properties of myofibrillar proteins in low-salt myofibrillar protein emulsion systems
- 27 December 2024
- Published by Elsevier in Food Chemistry
- Vol. 470, 142681
Magnetic fields improve the gel properties of myofibrillar proteins in low-salt myofibrillar protein emulsion systems
- 22 July 2024
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 277 (Pt 1) , 134114
The conformational modification of myofibrillar protein by magnetic field improves its emulsification properties
- 22 July 2024
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 277 (Pt 1) , 134114
The conformational modification of myofibrillar protein by magnetic field improves its emulsification properties
- 13 March 2024
- Published by Elsevier in Food Chemistry
- Vol. 447, 138990
Insight into the mechanisms of combining direct current magnetic field with phosphate in promoting emulsifying properties of myofibrillar protein
- 13 March 2024
- Published by Elsevier in Food Chemistry
- Vol. 447, 138990
Insight into the mechanisms of combining direct current magnetic field with phosphate in promoting emulsifying properties of myofibrillar protein
- 23 February 2024
- Published by Elsevier in Meat Science
- Vol. 212, 109453
Effect of magnetic field mediated CaCl2 on the edible quality of low-sodium minced pork gels
- 23 February 2024
- Published by Elsevier in Meat Science
- Vol. 212, 109453
Effect of magnetic field mediated CaCl2 on the edible quality of low-sodium minced pork gels
- 23 November 2023
- Published by Wiley in Journal of the Science of Food and Agriculture
- Vol. 104 (4) , 2284-2293
Study on the interaction and gel properties of pork myofibrillar protein with konjac polysaccharides
Background: Natural myofibrillar protein (MP) is sensitive to changes in the microenvironment, such as pH and ionic strength, and therefore can adversely affect the final quality of meat products. The aim of this study was to modify natural MP as well as to improve its functional properties. Therefore, the quality improvement effect of konjac polysaccharides with different concentrations (0, 1.5, 3, 4.5 and 6 g kg−1 protein) on MP gels was investigated.Results: With a concentration of konjac polysaccharides of 6 g kg−1 protein, the composite gel obtained exhibited a significant improvement of water binding (water holding capacity increased by 7.71%) and textural performance (strength increased from 29.12 to 37.55 N mm, an increase of 8.43 N mm). Meanwhile, konjac polysaccharides could help to form more disulfide bonds and non‐disulfide covalent bonds, which enhanced the crosslinking of MP and maintained the MP gel network structure. Then, with the preservation of α‐helix structure (a significant increase of 8.11%), slower protein aggregation and formation of small aggregates, this supported the formation of a fine and homogeneous network structure and allowed a reduction in water mobility.Conclusion: During the heating process, konjac polysaccharides could absorb the surrounding water and fill the gel system, which resulted in an increase in the water content of the gel network and enhanced the gel‐forming ability of the gel. Meanwhile, konjac polysaccharides might inhibit irregular aggregation of proteins and promote the formation of small aggregates, which in turn form a homogeneous and continuous gel matrix by orderly arrangement. © 2023 Society of Chemical Industry.
- 23 November 2023
- Published by Wiley in Journal of the Science of Food and Agriculture
- Vol. 104 (4) , 2284-2293
Study on the interaction and gel properties of pork myofibrillar protein with konjac polysaccharides
Background: Natural myofibrillar protein (MP) is sensitive to changes in the microenvironment, such as pH and ionic strength, and therefore can adversely affect the final quality of meat products. The aim of this study was to modify natural MP as well as to improve its functional properties. Therefore, the quality improvement effect of konjac polysaccharides with different concentrations (0, 1.5, 3, 4.5 and 6 g kg−1 protein) on MP gels was investigated.Results: With a concentration of konjac polysaccharides of 6 g kg−1 protein, the composite gel obtained exhibited a significant improvement of water binding (water holding capacity increased by 7.71%) and textural performance (strength increased from 29.12 to 37.55 N mm, an increase of 8.43 N mm). Meanwhile, konjac polysaccharides could help to form more disulfide bonds and non‐disulfide covalent bonds, which enhanced the crosslinking of MP and maintained the MP gel network structure. Then, with the preservation of α‐helix structure (a significant increase of 8.11%), slower protein aggregation and formation of small aggregates, this supported the formation of a fine and homogeneous network structure and allowed a reduction in water mobility.Conclusion: During the heating process, konjac polysaccharides could absorb the surrounding water and fill the gel system, which resulted in an increase in the water content of the gel network and enhanced the gel‐forming ability of the gel. Meanwhile, konjac polysaccharides might inhibit irregular aggregation of proteins and promote the formation of small aggregates, which in turn form a homogeneous and continuous gel matrix by orderly arrangement. © 2023 Society of Chemical Industry.
- 10 October 2023
- Published by Elsevier in Food Chemistry
- Vol. 436, 137691
Effect of magnetic field modification on oxidative stability of myoglobin in sarcoplasm systems
- 10 October 2023
- Published by Elsevier in Food Chemistry
- Vol. 436, 137691
Effect of magnetic field modification on oxidative stability of myoglobin in sarcoplasm systems