EFFECT OF EMERGING TECHNOLOGIES ON THE TECHNO-FUNCTIONAL PROPERTIES OF FRESH AND POWDERED FUNGAL MYCELIUM: A COMPARATIVE STUDY WITH CONVENTIONAL PROTEINS

Fungal mycelium emerges as a sustainable alternative source of protein, standing out for its fibrous structure, which provides technological and nutritional potential in innovative food formulations. This study aimed to compare the functional properties of conventional proteins with those of fungal mycelium, both untreated and subjected to emerging technologies. Whey protein (WP) (83% protein, DUX), freeze-dried pork loin (PL) (93.19% protein), and freeze-dried egg white (EW) (70% protein) were the conventional sources studied. Fresh mycelium (FM) and powdered mycelium (PM) (15% and 42% protein, respectively) were obtained from Typcal. A 1.5% protein solution of FM was sonicated for 30 min at 400 W (FM-US). PM was irradiated with a 4 kGy dose (PM-RX). Emulsifying activity (EAI), emulsion stability (ESI), foaming capacity and stability (FC and FS), water-holding capacity (WHC), oil-holding capacity (OHC), and gel formation (GF) of the samples were analyzed. Protein concentration was adjusted to 0.5% w/v for EAI and ESI, 1% w/v for FC and FS, and 2–20% for GF by dilution in buffer solution at pH 7. Animal proteins exhibited greater foaming capacity (FC), with whey (53.3%) and EW (13.3%), while mycelium samples showed very low FC (~6.7–8.9%). However, mycelium demonstrated superior foam stability (FS ≈ 97–100%), particularly PM, (100%), attributed to its dense network structure, favorable for aerated formulations. In terms of EAI, EW (13.5 mg²/g) and PM (16.6 mg²/g) achieved the highest values, whereas whey displayed the lowest (1.7 mg²/g) (p < 0.05). While ESI was similar across samples (~16–19.9 min), with PL showing the highest stability. PL and FM-US presented the higher OHC. Ultrasound improved oil and water retention in FM, 2.48 g/g in FM-US vs 0.91 g/g in FM to OHC, and 3.64 g/g in FM-US vs 2.73 g/g in FM to WHC, with FM-US having the highest WHC (p < 0.05) among all samples.  Partial unfolding and denaturation of the protein structure due to US exposes hydrophobic groups, which increases OHC and leads to the formation of larger protein aggregates, which can increase physical water retention, improving WHC. Least Gelling Concentration was 2, 2, 4, 10, 8, 10 and 8% for EW, WP, PL, PM, FM, PM-RX, and PM-US respectively, reflecting that fibrous structure of mycelium restricts protein–protein interactions. Overall, displayed promising functional properties, supporting its application in structured food systems and plant-based formulations. Ultrasound enhances properties, while irradiation effects on fungal proteins require further testing.