Structure-dependent modulation of Morchella esculenta protein by ferulic and chlorogenic acids: Improving techno-functionality and digestibility of a fungal alternative protein.
Aug 2026· Food Research International· Vol 242 Pt 5, pp.
120233
· 0 citations· 75 references
Medicine
Abstract
Fungal proteins face poor processing functionality and low digestibility limiting their use in emulsified and structured foods. Here, Morchella esculenta protein (MP) was modified by ferulic acid (FA) and chlorogenic acid (CA) at 0.0375-1 mg/mL. Both phenolics bound MP concentration-dependently, CA exhibited stronger binding affinity (Ka = 3.242 × 106 L/Mol) and deeper conformational rearrangement, while FA relied on hydrophobic and π-π interactions. Moderate phenolic addition maximized MP performance: EAI rose from 2.44 to 3.99 m2/g and digestibility from 45.33% to 58.31%, with CA delivering superior antioxidant capacity (DPPH scavenging 69.67%). Excess phenolics triggered severe protein aggregation and weakened interfacial stability. This work clarifies structure-dependent differential regulation of MP by two phenolics, defines optimal concentration thresholds, and provides theoretical support for clean-label fungal protein food ingredients.
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