Optimization of fungal protein extraction and studies on physicochemical properties and functional characteristics

Fungal protein isolate (FPI) was successfully extracted from the mycelium of a strain isolated from traditional Chinese Mao-Tofu under alkaline conditions. Response surface methodology optimized the extraction, achieving a 36.50 % yield with 58.24 % protein content under ideal parameters (pH 11.5, 45 °C, 30 mL/g solvent: solid ratio, 70 min). Protein electrophoretic characterization revealed FPI’s main subunits at 11.7, 35.4, and 56.7 kDa. Critically, FPI exhibited pronounced pH-dependent structural and functional properties: near its isoelectric point (pI ∼3.4), it displayed maximal ordered secondary structure (76 % α-helix & β-sheet at pH 3.0) and formed large aggregates, while alkaline conditions induced high solubility, small particle size, low surface hydrophobicity, and elevated free thiol content. These findings demonstrate FPI’s strong potential as a functional, pH-responsive alternative protein for food industry applications.

Authors

Publication Details

Journal
Future Foods
Published
2025-12-07
DOI
https://doi.org/10.1016/j.fufo.2025.100871
Citations
2
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
2.32
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Optimization of fungal protein extraction and studies on physicochemical properties and functional characteristics

Zhiguo Zhang, Ruobing Shi, Nianping Xue
2 citations
Future Foods
Proteins in Food Systems
2.32
article

Optimization of fungal protein extraction and studies on physicochemical properties and functional characteristics

Zhiguo Zhang, Ruobing Shi, Nianping Xue
article en
2 citations

Abstract

Fungal protein isolate (FPI) was successfully extracted from the mycelium of a strain isolated from traditional Chinese Mao-Tofu under alkaline conditions. Response surface methodology optimized the extraction, achieving a 36.50 % yield with 58.24 % protein content under ideal parameters (pH 11.5, 45 °C, 30 mL/g solvent: solid ratio, 70 min). Protein electrophoretic characterization revealed FPI’s main subunits at 11.7, 35.4, and 56.7 kDa. Critically, FPI exhibited pronounced pH-dependent structural and functional properties: near its isoelectric point (pI ∼3.4), it displayed maximal ordered secondary structure (76 % α-helix & β-sheet at pH 3.0) and formed large aggregates, while alkaline conditions induced high solubility, small particle size, low surface hydrophobicity, and elevated free thiol content. These findings demonstrate FPI’s strong potential as a functional, pH-responsive alternative protein for food industry applications.

Future FoodsVol. 13
Openalex Percentile: Top 10%
Proteins in Food Systems
2.32
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.