Impact of Covalent Binding with p-Coumaric Acid on Pea Protein's Structural and Functional Properties DOI Creative Commons
Xuxiao Gong, Sung‐Hyuk Choi, Yaqi Zhao

et al.

Current Research in Food Science, Journal Year: 2024, Volume and Issue: 9, P. 100916 - 100916

Published: Jan. 1, 2024

This study investigated the effects of covalent bonding between pea protein isolate (PPI) and p-coumaric acid (p-CA) on protein's secondary structure, solubility, foaming properties, emulsifying capacity, thermal stability. Binding p-CA led to alterations in structure PPI, including an increase α-helix random coil a decrease β-turn. Additionally, it resulted reduction SH NH groups, as well particle size. As amount bound increased, increased tendency for aggregation was proposed, resulting formation soluble aggregates through hydrophobic interactions, which confirmed by size proteins after being dissolved SDS. These structural modifications influenced functional with conjugates showing enhanced solubility capacity across various pH levels, but weaker foam Furthermore, exhibited lower initial denaturation temperature higher enthalpy change (ΔH) compared may be attributed unfolding new bonds. highlights potential modification PPI enhance its making more suitable food industry applications.

Language: Английский

Impact of Covalent Binding with p-Coumaric Acid on Pea Protein's Structural and Functional Properties DOI Creative Commons
Xuxiao Gong, Sung‐Hyuk Choi, Yaqi Zhao

et al.

Current Research in Food Science, Journal Year: 2024, Volume and Issue: 9, P. 100916 - 100916

Published: Jan. 1, 2024

This study investigated the effects of covalent bonding between pea protein isolate (PPI) and p-coumaric acid (p-CA) on protein's secondary structure, solubility, foaming properties, emulsifying capacity, thermal stability. Binding p-CA led to alterations in structure PPI, including an increase α-helix random coil a decrease β-turn. Additionally, it resulted reduction SH NH groups, as well particle size. As amount bound increased, increased tendency for aggregation was proposed, resulting formation soluble aggregates through hydrophobic interactions, which confirmed by size proteins after being dissolved SDS. These structural modifications influenced functional with conjugates showing enhanced solubility capacity across various pH levels, but weaker foam Furthermore, exhibited lower initial denaturation temperature higher enthalpy change (ΔH) compared may be attributed unfolding new bonds. highlights potential modification PPI enhance its making more suitable food industry applications.

Language: Английский

Citations

0