Mechanism of low-salt surimi gelation induced by microwave heating combined with l-arginine and transglutaminase: On the basis of molecular docking between l-arginine and myosin heavy chain. (15th October 2022)
- Record Type:
- Journal Article
- Title:
- Mechanism of low-salt surimi gelation induced by microwave heating combined with l-arginine and transglutaminase: On the basis of molecular docking between l-arginine and myosin heavy chain. (15th October 2022)
- Main Title:
- Mechanism of low-salt surimi gelation induced by microwave heating combined with l-arginine and transglutaminase: On the basis of molecular docking between l-arginine and myosin heavy chain
- Authors:
- Shi, Tong
Wang, Xin
Li, Mengzhe
Xiong, Zhiyu
McClements, David Julian
Bao, Yulong
Song, Teng
Li, Jianrong
Yuan, Li
Jin, Wengang
Gao, Ruichang - Abstract:
- Highlights: Arg combined with TGase improved the gel properties of low-salt surimi induced by MW. A compact network of low-salt surimi gel was obtained if Arg was added before TGase. Arg increased proportion of immobilized water and decreased proportion of free water. Arg induced a shift of α-helix bands and increase in definition of β-sheet bands. The binding sites between Arg and myosin were revealed via molecular docking technique. Abstract: The reduction of the salt content of foods is of interest for health reasons. The present study showed that low-salt surimi gels could be produced using a combination of l -arginine (Arg) and transglutaminase (TGase) under microwave (MW) irradiation. The low-salt surimi gels produced by MW had similar physicochemical properties as regular-salt surimi gels produced by conventional two-stage water bath heating. Compared to low-salt surimi gels containing TGase alone, Arg increased the water holding capacity and gel strength ( P < 0.05) and promoted the formation of a more homogeneous and compact three-dimensional gel network. As a result, there was a significant increase in the proportion of immobilized water and decrease in the proportion of free water ( P < 0.05). The nature of the binding sites between Arg and myosin heavy chain was predicted using the molecular docking simulations analysis. These results may be useful for the development of low-salt surimi products.
- Is Part Of:
- Food chemistry. Volume 391(2022)
- Journal:
- Food chemistry
- Issue:
- Volume 391(2022)
- Issue Display:
- Volume 391, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 391
- Issue:
- 2022
- Issue Sort Value:
- 2022-0391-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-10-15
- Subjects:
- Low-salt surimi -- l-arginine -- Transglutaminase -- Protein structure -- Microwave -- Molecular docking
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2022.133184 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
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