A novel EGCG-Histidine complex improves gelling and physicochemical properties of porcine myofibrillar proteins: Insight into underlying mechanisms

[Display omitted] •EGCG-His complex is formed by Michael addition/Schiff base reaction.•EGCG-His complex has excellent antioxidant ability.•EGCG-His complex changes microstructure and structural properties of MP gel.•MP gel with EGCG-His complex at a molar ratio of 1:5 has highest water-binding capa...

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Veröffentlicht in:Food chemistry 2024-08, Vol.448, p.139070-139070, Article 139070
Hauptverfasser: Guo, Xiao, Wang, Renzheng, Han, Bofu, Shao, Wei, Chen, Lin, Feng, Xianchao
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Sprache:eng
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Zusammenfassung:[Display omitted] •EGCG-His complex is formed by Michael addition/Schiff base reaction.•EGCG-His complex has excellent antioxidant ability.•EGCG-His complex changes microstructure and structural properties of MP gel.•MP gel with EGCG-His complex at a molar ratio of 1:5 has highest water-binding capacity. Herein, an EGCG-Histidine complex is prepared, characterized, and further used to improve gel properties of myofibrillar proteins (MP). Results of FTIR, XRD, UV–Vis spectroscopy showed that histidine is covalently bound to EGCG by Michael addition or Schiff base reaction to form EGCG-Histidine complex, and antioxidant activity of EGCG-Histidine complex is significantly increased compared to EGCG or histidine alone (P 
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2024.139070