Proteomic and Functional Profiling of Trichoderma reesei, Pichia guilliermondii, and Hericium erinaceus.
5 affiliations
- 1Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, Edith Cowan University, School of Science, PerthWA 6027, Australia.
- 2Centre of Crops and Horticultural Analytics for Nutrition and Climate Excellence, School of Science, Edith Cowan University, 270 Joondalup Dr, JoondalupWA 6027, Australia.
- 3CSIRO Agriculture and Food , St Lucia, QLD4067, Australia.
- 4CSIRO Agriculture and Food , Werribee, VIC3030, Australia.
- 5Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, Queensland4072, Australia.
Abstract
Fungi relevant to food systems and biotechnology differ in physiology, yet their condition-specific intracellular proteomes have rarely been compared using a common workflow. We hypothesized that harmonized extraction and data-independent acquisition mass spectrometry would reveal distinct functional signatures across Trichoderma reesei, Pichia guilliermondii, and Hericium erinaceus. Overall, 199, 889, and 1456 proteins were identified, respectively, revealing species-associated differences in protein biosynthesis, bioenergetics, redox metabolism, carbohydrate catabolism, proteostasis, and RNA-associated functions. Orthogroup and enzyme analyses identified conserved and species-specific functional features. Proteomes displayed hydrophilic and acidic profiles. Crude extracts exhibited concentration-dependent ACE inhibitory, ABTS radical scavenging, reduced glutathione, and l-glutaminase readouts. In silico screening identified 119, 1035, and 1431 sequence-derived candidate assignments, respectively, without establishing endogenous peptide occurrence or causal links to extract activities. These strain- and condition-specific intracellular proteomic data sets provide hypotheses for food and biotechnology studies but do not represent complete species proteomes, secretomes, or validated endogenous bioactive peptides.
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BibTeX
@article{ahmed2026proteomic,
title = {{Proteomic and Functional Profiling of Trichoderma reesei, Pichia guilliermondii, and Hericium erinaceus.}},
author = {Tanvir Ahmed and Angéla Juhász and Utpal Bose and Netsanet Shiferaw Terefe and Lai Yue Chan and David J Craik and Michelle L Colgrave},
journal = {Journal of agricultural and food chemistry},
year = {2026},
month = oct,
doi = {10.1021/acs.jafc.6c09785},
url = {https://europepmc.org/article/MED/42915781},
note = {CC BY-NC-ND},
}
RIS
TY - JOUR
TI - Proteomic and Functional Profiling of Trichoderma reesei, Pichia guilliermondii, and Hericium erinaceus.
AU - Tanvir Ahmed
AU - Angéla Juhász
AU - Utpal Bose
AU - Netsanet Shiferaw Terefe
AU - Lai Yue Chan
AU - David J Craik
AU - Michelle L Colgrave
PY - 2026
DA - 2026/10/01
JO - Journal of agricultural and food chemistry
DO - 10.1021/acs.jafc.6c09785
UR - https://europepmc.org/article/MED/42915781
AB - Fungi relevant to food systems and biotechnology differ in physiology, yet their condition-specific intracellular proteomes have rarely been compared using a common workflow. We hypothesized that harmonized extraction and data-independent acquisition mass spectrometry would reveal distinct functional signatures across Trichoderma reesei, Pichia guilliermondii, and Hericium erinaceus. Overall, 199, 889, and 1456 proteins were identified, respectively, revealing species-associated differences in protein biosynthesis, bioenergetics, redox metabolism, carbohydrate catabolism, proteostasis, and RNA-associated functions. Orthogroup and enzyme analyses identified conserved and species-specific functional features. Proteomes displayed hydrophilic and acidic profiles. Crude extracts exhibited concentration-dependent ACE inhibitory, ABTS radical scavenging, reduced glutathione, and l-glutaminase readouts. In silico screening identified 119, 1035, and 1431 sequence-derived candidate assignments, respectively, without establishing endogenous peptide occurrence or causal links to extract activities. These strain- and condition-specific intracellular proteomic data sets provide hypotheses for food and biotechnology studies but do not represent complete species proteomes, secretomes, or validated endogenous bioactive peptides.
SN - 0021-8561
SN - 1520-5118
ER -