Tyrosinase-Catalyzed Soy Protein and Tannic Acid Interaction: Effects on Structural and Rheological Properties of Complexes DOI Creative Commons

Yaqiong Pei,

Lei Yuan, Wenjing Zhou

et al.

Gels, Journal Year: 2025, Volume and Issue: 11(3), P. 195 - 195

Published: March 12, 2025

This study investigated the structural, rheological, and microstructural properties of soy protein isolate (SPI) induced by tyrosinase-catalyzed crosslinking with tannic acid (TA) at 25 °C under neutral conditions pH 6.5. The particle size polydispersity index modified SPI progressively increased rising TA concentrations. Tyrosinase-induced polymerization significantly impacted conformational structure SPI, evidenced a notable decrease in intrinsic fluorescence, pronounced red shift, remarkable reduction surface hydrophobicity. FTIR analysis further revealed that, compared to control amide I, II, III bands incubated tyrosinase exhibited varying degrees red-shift or blue-shift. These observations suggested substantial alteration secondary after incubation tyrosinase. apparent viscosity, G′, G″ higher concentrations, indicating that modification presence resulted enhanced covalent crosslinking. Microstructural confirmed levels promoted formation denser more uniform gel-like networks. findings demonstrated tyrosinase-mediated improved functionality making it promising approach for food applications.

Language: Английский

Tyrosinase-Catalyzed Soy Protein and Tannic Acid Interaction: Effects on Structural and Rheological Properties of Complexes DOI Creative Commons

Yaqiong Pei,

Lei Yuan, Wenjing Zhou

et al.

Gels, Journal Year: 2025, Volume and Issue: 11(3), P. 195 - 195

Published: March 12, 2025

This study investigated the structural, rheological, and microstructural properties of soy protein isolate (SPI) induced by tyrosinase-catalyzed crosslinking with tannic acid (TA) at 25 °C under neutral conditions pH 6.5. The particle size polydispersity index modified SPI progressively increased rising TA concentrations. Tyrosinase-induced polymerization significantly impacted conformational structure SPI, evidenced a notable decrease in intrinsic fluorescence, pronounced red shift, remarkable reduction surface hydrophobicity. FTIR analysis further revealed that, compared to control amide I, II, III bands incubated tyrosinase exhibited varying degrees red-shift or blue-shift. These observations suggested substantial alteration secondary after incubation tyrosinase. apparent viscosity, G′, G″ higher concentrations, indicating that modification presence resulted enhanced covalent crosslinking. Microstructural confirmed levels promoted formation denser more uniform gel-like networks. findings demonstrated tyrosinase-mediated improved functionality making it promising approach for food applications.

Language: Английский

Citations

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