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Updated: May 28, 2026

Toxin Induction and Protein Extraction from Fusarium spp. Cultures for Proteomic Studies
Published on: February 16, 2010
Proteomic Evidence Indicates Ultrasound-Assisted Extraction Enhances Recovery of Membrane-Associated Proteins in
Tanvir Ahmed1,2, Angéla Juhász1,2, Utpal Bose1,2,3
1Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, Edith Cowan University, School of Science, Perth, WA 6027, Australia.
Abstract:
Membrane-associated fungal proteins mediate essential functions and contain bioactive proteins with therapeutic potential but are underrepresented in aqueous extracts due to hydrophobicity and lipid associations. Ultrasound-assisted aqueous extraction was applied to Lion's mane (Hericium erinaceus), and the proteins were fractionated by molecular weight (≥30 kDa, 10-30 kDa, 3-10 kDa). Proteomic profiling using data-dependent (DDA) and data-independent (DIA) mass spectrometry identified 1500 and 1702 proteins, respectively (1% global FDR). Ultrasonication induced surface irregularity and a less compact, heterogeneous microstructure. Topology predictions showed higher proportions of transmembrane and secretory proteins in ultrasonicated fractions. Extraction preserved protein integrity (82% molecular-weight retention, 97% tryptic specificity, 26:1 stable-to-degraded ratio). The ≥30 kDa fraction was enriched for the endomembrane system and cytoskeletal components; the 10-30 kDa fraction captured mitochondrial respirasome and vacuolar V-ATPase complexes; the 3-10 kDa fraction contained mainly cytosolic proteins. Ultrasonication-unique proteins showed higher aromaticity, and abundant ≥ 30 kDa proteins displayed membrane-proximal characteristics.
Insights
Ultrasound-assisted extraction effectively recovered membrane-associated fungal proteins from Lion
Area of Science:
- Mycology
- Biochemistry
- Proteomics
Background:
- Membrane-associated fungal proteins are crucial for cell function and possess therapeutic potential.
- These proteins are often underrepresented in aqueous extracts due to their hydrophobic nature and association with lipids.
- Efficient extraction methods are needed to access these valuable biomolecules.
Purpose of the Study:
- To investigate ultrasound-assisted aqueous extraction for recovering membrane-associated proteins from Lion's mane (Hericium erinaceus).
- To characterize the proteomic profile and structural properties of extracted protein fractions.
- To assess the integrity and localization of extracted proteins.
Main Methods:
- Ultrasound-assisted aqueous extraction of Lion's mane mushroom.
- Fractionation of extracted proteins by molecular weight (≥30 kDa, 10-30 kDa, 3-10 kDa).
- Proteomic profiling using data-dependent (DDA) and data-independent (DIA) mass spectrometry.
- Analysis of protein microstructure and topology.
Main Results:
- Proteomic analysis identified 1500-1702 proteins, with higher proportions of transmembrane and secretory proteins in ultrasonicated fractions.
- Ultrasonication altered the microstructure of the fungal material, enhancing protein accessibility.
- Protein integrity was well-preserved during extraction, with distinct protein compositions in different molecular weight fractions.
- The ≥30 kDa fraction was rich in endomembrane and cytoskeletal proteins, while smaller fractions contained mitochondrial and cytosolic proteins.
Conclusions:
- Ultrasound-assisted aqueous extraction is a viable method for obtaining membrane-associated fungal proteins from Hericium erinaceus.
- This technique enhances the recovery of bioactive proteins with potential therapeutic applications.
- The fractionation by molecular weight provides insights into the subcellular localization of extracted proteins.

