Sep 2026· Journal of Agricultural and Food Chemistry· Vol 74, pp. 31253 - 31270· 0 citations· 107 references
TL;DR
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.
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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