Characterization of oyster water-soluble protein-EGCG conjugate and its antioxidant effects on linolic acid in emulsion system. (February 2023)
- Record Type:
- Journal Article
- Title:
- Characterization of oyster water-soluble protein-EGCG conjugate and its antioxidant effects on linolic acid in emulsion system. (February 2023)
- Main Title:
- Characterization of oyster water-soluble protein-EGCG conjugate and its antioxidant effects on linolic acid in emulsion system
- Authors:
- Li, Yue
Liu, Xiaoyang
Yin, Fawen
Li, Deyang
Jiang, Pengfei
Song, Liang
Nakamura, Yoshimasa
Zhou, Dayong - Abstract:
- Abstract: (−)-Epigallocatechin-3-gallate (EGCG) is frequently used as a good antioxidant in food systems. In contrast, its antioxidant capacity was limited in the oil-in-water emulsion system due to its high hydrophilicity. Therefore, food-derived proteins with higher hydrophobicity were utilized to bind with EGCG and form new molecules that could stay in the oil-water interface to improve the stability of such emulsions. This study combined water-soluble protein (OWPs) extracted from oysters with EGCG to form the OWPs-EGCG complex. When combined with EGCG, the molecular weight and particle diameter (nearly 180–240 nm) of OWPs slightly increased in a dose-dependent manner by increasing the proportion of EGCG. Moreover, several conformational changes to OWPs by EGCG addition were found, such as the alteration of secondary structures, the fluorescence quenching, and the involvement of binding groups. The OWPs-EGCG complex (1:0.025) exhibited the highest emulsifying activities, while the ratio of 1:0.2 had the highest foaming stability. Furthermore, the OWPs-EGCG complex showed nearly 90% free radical scavenging activities with an increasing ratio of EGCG. In the established temporary storage model of OWPs-EGCG conjugate/linolic acid emulsion system, the OWPs-EGCG complex exhibited enhanced antioxidant effects against the oxidation of OWPs and linolic acid. This study provided a theoretical basis for the potential applications of food-derived proteins/EGCG conjugates onAbstract: (−)-Epigallocatechin-3-gallate (EGCG) is frequently used as a good antioxidant in food systems. In contrast, its antioxidant capacity was limited in the oil-in-water emulsion system due to its high hydrophilicity. Therefore, food-derived proteins with higher hydrophobicity were utilized to bind with EGCG and form new molecules that could stay in the oil-water interface to improve the stability of such emulsions. This study combined water-soluble protein (OWPs) extracted from oysters with EGCG to form the OWPs-EGCG complex. When combined with EGCG, the molecular weight and particle diameter (nearly 180–240 nm) of OWPs slightly increased in a dose-dependent manner by increasing the proportion of EGCG. Moreover, several conformational changes to OWPs by EGCG addition were found, such as the alteration of secondary structures, the fluorescence quenching, and the involvement of binding groups. The OWPs-EGCG complex (1:0.025) exhibited the highest emulsifying activities, while the ratio of 1:0.2 had the highest foaming stability. Furthermore, the OWPs-EGCG complex showed nearly 90% free radical scavenging activities with an increasing ratio of EGCG. In the established temporary storage model of OWPs-EGCG conjugate/linolic acid emulsion system, the OWPs-EGCG complex exhibited enhanced antioxidant effects against the oxidation of OWPs and linolic acid. This study provided a theoretical basis for the potential applications of food-derived proteins/EGCG conjugates on antioxidant effects against lipid oxidation in the emulsifying system. … (more)
- Is Part Of:
- Food bioscience. Volume 51(2023)
- Journal:
- Food bioscience
- Issue:
- Volume 51(2023)
- Issue Display:
- Volume 51, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 51
- Issue:
- 2023
- Issue Sort Value:
- 2023-0051-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-02
- Subjects:
- EGCG -- Protein -- Oyster -- Antioxidant -- Emulsion
OWPs Water-soluble protein derived from oysters -- FTIR Fourier transform infrared spectroscopy -- CD Circular dichroism -- FL Fluorescence spectroscopy -- EAI Emulsion activity index -- ESI emulsion stability index -- FE Foam expansion -- FS Foam stability
Food -- Biotechnology -- Periodicals
Food -- Research -- Periodicals
Aliments -- Biotecnologia -- Revistes
Aliments -- Investigació -- Revistes
Food -- Biotechnology
Food -- Research
Revistes electròniques
Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/22124292 ↗
http://www.sciencedirect.com/ ↗ - DOI:
- 10.1016/j.fbio.2022.102215 ↗
- Languages:
- English
- ISSNs:
- 2212-4292
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 25204.xml