Molecular and functional modulation of mycoprotein extract from edible Trametes versicolor via pH cycling and ultrasound-enhanced transglutaminase treatment.

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Citation abstract

This study investigates the structural and functional modification of mycoprotein extract from Trametes versicolor through ultrasound (US) processing combined with either pH cycling treatment or transglutaminase (TGase) cross-linking. Mycoprotein extracts from Trametes versicolor were obtained via ultrasound-assisted extraction and subsequently freeze-dried. Five treatments were compared: pH cycling, ultrasound alone, TGase cross-linking, TGase + US, and pH cycling + US. Molecular and physicochemical characterizations were performed to assess solubility, free sulfhydryl group content, surface hydrophobicity, emulsifying and foaming capacities, thermal behavior, microstructure, and in vitro protein digestibility. The pH cycling + US treatment significantly enhanced solubility (73.53 %), surface hydrophobicity, and emulsion stability, while TGase + US yielded the highest oil absorption (2.09 %), foaming capacity (123.1 %), and foam stability (93.75 %). Differential scanning calorimetry indicated increased thermal stability, with the highest denaturation temperature (T d: 92.7 °C) observed in the pH cycling + US group. Scanning electron microscopy revealed distinct structural fragmentation in treated proteins compared to the smooth, spherical morphology of untreated protein samples. The highest in vitro digestibility was achieved with pH-cycling + US (93.72 %). These findings demonstrate that the targeted structural modifications of mycoproteins via synergistic treatments can significantly improve its functional and digestive properties, offering novel insights into protein modification for food applications.