Fungi in Focus: Fungal Enzyme and Fungal Metabolism

A special issue of Journal of Fungi (ISSN 2309-608X). This special issue belongs to the section "Fungal Cell Biology, Metabolism and Physiology".

Deadline for manuscript submissions: closed (31 July 2026) | Viewed by 7347

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Guest Editor
Institute of Biology, Leiden University, Sylviusweg 72, 2333 BE Leiden, The Netherlands
Interests: bioremediation; utilization of renewable resources; carbon and nitrogen metabolism; aromatic compounds; microbial plastic degradation; lignin; pollutants
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Special Issue Information

Dear Colleagues,

Fungi are remarkable organisms with extraordinary metabolic capabilities and powerful enzymatic systems that drive key ecological processes and open exciting opportunities in biotechnology, medicine, and industry. From breaking down complex plant polymers to producing valuable secondary metabolites, fungal enzymes and metabolic networks continue to inspire innovative applications in energy, health, and environmental sustainability. With rapid advances in genomics, metabolomics, and enzyme engineering, the study of fungal metabolism is entering a new era of discovery and application.

This Special Issue, “Fungi in Focus: Fungal Enzyme and Fungal Metabolism”, invites researchers to contribute original research articles, reviews, and perspectives that explore the diversity, mechanisms, and potential of fungal enzymes and metabolic pathways. We welcome submissions spanning fundamental biology, novel enzyme characterization, metabolic regulation, synthetic biology, and applied biotechnology. By sharing cutting-edge findings and forward-looking insights, this collection aims to stimulate collaboration, spark new ideas, and highlight the transformative role of fungi in science and industry. Join us in uncovering the hidden potential of fungal metabolism and shaping future directions in fungal research.

Dr. Ronnie Lubbers
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-anonymized peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Journal of Fungi is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • fungal enzymes
  • fungal metabolism
  • biotechnology
  • secondary metabolites
  • bioconversion
  • enzyme engineering
  • metabolomics
  • environmental remediation
  • drug discovery

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Published Papers (5 papers)

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Research

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23 pages, 5815 KB  
Article
Heat-Stress Induced Apoptosis: A New Biotechnological Strategy to Enhance Ganoderic Acids Production in Ganoderma lucidum
by Meng-Hsuan Lai, Ni Tien, Hsiao-Lien Yang, Jun-He Huang, Miin-Huey Lee and Bang-Jau You
J. Fungi 2026, 12(5), 364; https://doi.org/10.3390/jof12050364 - 15 May 2026
Viewed by 888
Abstract
Ganoderma lucidum is a medicinal fungus widely utilized in traditional medicine and functional foods. Its primary bioactive constituents are ganoderic acids (GAs), a group of triterpenoid compounds. While chemical-induced apoptosis has previously been shown to enhance GAs production, this study investigates the role [...] Read more.
Ganoderma lucidum is a medicinal fungus widely utilized in traditional medicine and functional foods. Its primary bioactive constituents are ganoderic acids (GAs), a group of triterpenoid compounds. While chemical-induced apoptosis has previously been shown to enhance GAs production, this study investigates the role of physical stress in this regulatory pathway. We demonstrate that heat-induced apoptosis significantly increases GAs production in G. lucidum. To determine whether apoptosis directly regulates this process, we overexpressed the human anti-apoptotic gene Bcl-2 in G. lucidum, confirming expression via RT-PCR and Western blot analysis. Upon heat-induced apoptosis, these Bcl-2 overexpression mutants exhibited increased mycelial cell viability, accompanied by reduced metacaspase activity and, notably, decreased GAs production. Furthermore, we identified a Type I metacaspase gene in G. lucidum, Glmca1, which contains highly conserved catalytic domains common across fungal species. Silencing of Glmca1 followed by heat-induced apoptosis led to results similar to Bcl-2 overexpression: enhanced cell viability, suppressed metacaspase activity, and a significant reduction in GAs yield. These findings provide compelling evidence that apoptosis functions as a critical regulatory mechanism for secondary metabolite production in G. lucidum. Consequently, modulating apoptotic pathways through physical induction offers a promising strategy for enhancing the production of bioactive ingredients in medicinal fungi. Full article
(This article belongs to the Special Issue Fungi in Focus: Fungal Enzyme and Fungal Metabolism)
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14 pages, 2358 KB  
Article
Structural Insights into the Glycosylphosphatidylinositol Mannosyltransferase I Complex from Candida glabrata
by Hui Sun, Weihong Wu, Xiaomei Li, Yang Deng, Jiarong Huang, Meng Yin and Zhaofeng Yan
J. Fungi 2025, 11(11), 819; https://doi.org/10.3390/jof11110819 - 19 Nov 2025
Viewed by 1447
Abstract
The global rise in resistance to first-line antifungal agents highlights the urgent need for new therapeutic strategies. Glycosylphosphatidylinositol (GPI)-anchored protein biosynthesis is an attractive target. The GPI mannosyltransferase I (GPI-MT-I), composed of Gpi14 and Pbn1, catalyzes the essential first mannose transfer from dolichol-phosphomannose [...] Read more.
The global rise in resistance to first-line antifungal agents highlights the urgent need for new therapeutic strategies. Glycosylphosphatidylinositol (GPI)-anchored protein biosynthesis is an attractive target. The GPI mannosyltransferase I (GPI-MT-I), composed of Gpi14 and Pbn1, catalyzes the essential first mannose transfer from dolichol-phosphomannose (Dol-P-Man) to the GPI precursor. This initial mannosylation is critical for fungal cell wall integrity, yet the molecular basis of GPI-MT-I assembly and substrate recognition remains poorly understood. Here, we present the cryo-EM structure of Candida glabrata GPI-MT-I in complex with Dol-P-Man, revealing how Gpi14 and Pbn1 form a stable complex and engage the mannose donor. An AlphaFold3-predicted acceptor-bound model further defines the structural basis of acceptor substrate recognition and suggests a plausible catalytic mechanism. Comparison with structural homologs highlights a distinct mode of substrate engagement by GPI-MT-I. Together, these findings establish a mechanistic framework for GPI-MT-I function with broader implications for the GPI-MT family. Full article
(This article belongs to the Special Issue Fungi in Focus: Fungal Enzyme and Fungal Metabolism)
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16 pages, 1984 KB  
Article
Upcycling Oat Hulls via Solid-State Fermentation Using Edible Filamentous Fungi: A Co-Culture Approach with Neurospora intermedia and Rhizopus oryzae
by Laura Georgiana Radulescu, Mikael Terp, Christian Enrico Rusbjerg-Weberskov, Niels Thomas Eriksen and Mette Lübeck
J. Fungi 2025, 11(11), 810; https://doi.org/10.3390/jof11110810 - 14 Nov 2025
Cited by 3 | Viewed by 2087
Abstract
The global challenge of food insecurity requires innovative approaches for sustainable food production and waste valorization. This study investigates the valorization of oat hulls, an abundant lignocellulosic by-product from oat manufacturing, by solid-state fermentation using edible filamentous fungi. Oat hulls sourced from oatmeal [...] Read more.
The global challenge of food insecurity requires innovative approaches for sustainable food production and waste valorization. This study investigates the valorization of oat hulls, an abundant lignocellulosic by-product from oat manufacturing, by solid-state fermentation using edible filamentous fungi. Oat hulls sourced from oatmeal industrial side-streams were used as the sole substrate in co-cultures of Neurospora intermedia and Rhizopus oryzae. The fermentation process was optimized and upscaled, with fungal growth monitored via CO2 efflux and modeled to assess substrate utilization. Comprehensive analyses revealed a significant increase in protein concentration (p < 0.05) in the fermented oat hulls compared to the non-fermented controls. The resulting product was successfully incorporated into granola bars, which underwent sensory evaluation and received positive feedback, demonstrating its potential as a value-added food ingredient. These findings highlight the feasibility of using edible fungi to upcycle cereal processing by-products into nutritionally enhanced alternative protein sources, supporting both food system sustainability and circular bioeconomy objectives. Full article
(This article belongs to the Special Issue Fungi in Focus: Fungal Enzyme and Fungal Metabolism)
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23 pages, 5443 KB  
Article
Effects of Temperature, pH, and Relative Humidity on Growth of Penicillium crustosum OM1 Isolated from Pears and Its Penitrem A Production
by Shengming Gao, Sung-Yong Hong, Gyu-Mi Jung and Ae-Son Om
J. Fungi 2025, 11(10), 741; https://doi.org/10.3390/jof11100741 - 16 Oct 2025
Cited by 3 | Viewed by 2017
Abstract
Penitrem A, an indole–diterpenoid neurotoxin, is produced by several species of Penicillium on cereal grains, meat, dairy products, and fruits. Penicillium crustosum is a well-known penitrem A producer, but much is unknown about physiological characteristics of P. crustosum. In this study, we [...] Read more.
Penitrem A, an indole–diterpenoid neurotoxin, is produced by several species of Penicillium on cereal grains, meat, dairy products, and fruits. Penicillium crustosum is a well-known penitrem A producer, but much is unknown about physiological characteristics of P. crustosum. In this study, we isolated penitrem A-producing P. crustosum OM1 from pears, and investigated the influence of temperature, pH, and relative humidity [RH] on its growth and penitrem A production. The fungal species exhibited the highest growth at 25 °C and pH 4.5 on mYES4 under RH 98%, whereas it produced the highest level of penitrem A at 22 °C and pH 6.5 on the same media under RH 98%. Furthermore, RT-qPCR analysis of six penitrem A biosynthetic genes (ptmB, ptmJ, ptmK, ptmO, ptmS, and ptmT) expression in P. crustosum OM1 showed that the four penitrem A biosynthetic genes (ptmJ, ptmK, ptmO, and ptmS) were up-regulated in mYES4 (penitrem A conducive medium), whereas they were not in mMEB (penitrem A non-conducive medium). Our results demonstrated that the three key environmental factors significantly affected the growth of P. crustosum OM1 and its penitrem A production. These findings could help find efficient methods to prevent penitrem A contamination from fresh fruits including pears. Full article
(This article belongs to the Special Issue Fungi in Focus: Fungal Enzyme and Fungal Metabolism)
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Review

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37 pages, 1757 KB  
Review
Fungal Hydrophobins: Taxonomic Distribution, Functional Roles, Physicochemical Properties, and Biotechnological Applications
by Sandra de Camargo Lameu, Matheus Henrique Galvão, Isabelle Teixeira Mello and Fabio Marcio Squina
J. Fungi 2026, 12(8), 587; https://doi.org/10.3390/jof12080587 - 7 Aug 2026
Viewed by 248
Abstract
Hydrophobins are small, cysteine-rich amphipathic proteins predominantly produced by filamentous fungi, known for their ability to self-assemble at hydrophobic–hydrophilic interfaces. These proteins are essential for fungal development, surface interactions, pathogenicity, and environmental adaptation, and they have attracted growing interest for biotechnological applications. In [...] Read more.
Hydrophobins are small, cysteine-rich amphipathic proteins predominantly produced by filamentous fungi, known for their ability to self-assemble at hydrophobic–hydrophilic interfaces. These proteins are essential for fungal development, surface interactions, pathogenicity, and environmental adaptation, and they have attracted growing interest for biotechnological applications. In this work, we provide a narrative review of fungal hydrophobins, based on a systematic literature search and manual curation of eligible studies integrated with protein database records from Ascomycota and Basidiomycota. Information was compiled from peer-reviewed publications selected according to predefined eligibility criteria and complemented with UniProt records, covering taxonomic distribution, functional and biophysical properties, and physiological and pathogenic roles. Significant diversity in molecular features and physicochemical profiles was observed, indicating functional specialization across different ecological niches and lifestyles. Additionally, the compiled data highlight various biotechnological applications, such as surface modification, enzyme immobilization, drug delivery systems, biomaterial development, and environmentally sustainable technologies. By consolidating molecular, functional, and applied information across a wide range of fungal species, this review provides a comprehensive reference framework for hydrophobin research and biotechnological innovation. Full article
(This article belongs to the Special Issue Fungi in Focus: Fungal Enzyme and Fungal Metabolism)
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