Structure-dependent modulation of Morchella esculenta protein by ferulic and chlorogenic acids: Improving techno-functionality and digestibility of a fungal alternative protein

Morchella esculenta protein was evaluated as a fungal alternative protein ingredient. • Ferulic and chlorogenic acids modulated MP structure in a concentration-dependent manner. • Moderate phenolic acid functionalization improved emulsifying, foaming, and digestibility. • Excessive phenolic acid addition induced aggregation and reduced colloidal stability. • Structure-dependent phenolic functionalization offers a strategy for alternative-protein foods. 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 ( K a = 3.242 × 10 6  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 m 2 /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 Download: Download high-res image (139KB) Download: Download full-size image