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Physiologia Plantarum 2024Edible mushrooms are an important food source with high nutritional and medicinal value. They are a useful source for studying phylogenetic evolution and species... (Review)
Review
Edible mushrooms are an important food source with high nutritional and medicinal value. They are a useful source for studying phylogenetic evolution and species divergence. The exploration of the evolutionary relationships among these species conventionally involves analyzing sequence variations within their complete mitochondrial genomes, which range from 31,854 bp (Cordyceps militaris) to 197,486 bp (Grifolia frondosa). The study of the complete mitochondrial genomes of edible mushrooms has emerged as a critical field of research, providing important insights into fungal genetic makeup, evolution, and phylogenetic relationships. This review explores the mitochondrial genome structures of various edible mushroom species, highlighting their unique features and evolutionary adaptations. By analyzing these genomes, robust phylogenetic frameworks are constructed to elucidate mushrooms lineage relationships. Furthermore, the exploration of different variations of mitochondrial DNA presents novel opportunities for enhancing mushroom cultivation biotechnology and medicinal applications. The mitochondrial genomic features are essential for improving agricultural practices and ensuring food security through improved crop productivity, disease resistance, and nutritional qualities. The current knowledge about the mitochondrial genomes of edible mushrooms is summarized in this review, emphasising their significance in both scientific research and practical applications in bioinformatics and medicine.
Topics: Genome, Mitochondrial; Agaricales; Phylogeny; Evolution, Molecular; Genome, Fungal
PubMed: 38837786
DOI: 10.1111/ppl.14363 -
International Journal of Biological... Jun 2024Dictyophora indusiata is a common edible mushroom with great potential in the field of medicine against metabolic disorders, inflammation, and immunodeficiency. Our...
Dictyophora indusiata is a common edible mushroom with great potential in the field of medicine against metabolic disorders, inflammation, and immunodeficiency. Our previous studies have shown that different fractions of the polysaccharide from Dictyophora indusiata (DIP) have various structural characteristics and morphology. However, the impact of the structural features on the protective effects of DIP against metabolic syndrome remains unclear. In this study, three distinct polysaccharide fractions have been extracted from Dictyophora indusiata and a high-fat diet-induced metabolic syndrome (MetS) was constructed in mice. The effects of these fractions on a range of MetS-associated endpoints, including abnormal blood glucose, lipid profiles, body fat content, liver function, intestinal microbiota and their metabolites were investigated. Through correlation analysis, the potential link between the monosaccharide composition of the polysaccharides and their biological activities was determined. The study aimed to explore the potential mechanisms and ameliorative effects of these polysaccharide fractions on MetS, thereby providing statistical evidence for understanding the relationship between monosaccharides composition of Dictyophora indusiata polysaccharides and their potential utility in treating metabolic disorders.
Topics: Animals; Metabolic Syndrome; Mice; Diet, High-Fat; Fungal Polysaccharides; Male; Monosaccharides; Polysaccharides; Gastrointestinal Microbiome; Basidiomycota; Liver; Blood Glucose; Disease Models, Animal; Agaricales
PubMed: 38834122
DOI: 10.1016/j.ijbiomac.2024.132744 -
Regulation of dye-decolorizing peroxidase gene expression in grown on glycerol as the carbon source.PeerJ 2024Dye-decolorizing peroxidases (DyPs) (E.C. 1.11.1.19) are heme peroxidases that catalyze oxygen transfer reactions similarly to oxygenases. DyPs utilize hydrogen peroxide...
Dye-decolorizing peroxidases (DyPs) (E.C. 1.11.1.19) are heme peroxidases that catalyze oxygen transfer reactions similarly to oxygenases. DyPs utilize hydrogen peroxide (HO) both as an electron acceptor co-substrate and as an electron donor when oxidized to their respective radicals. The production of both DyPs and lignin-modifying enzymes (LMEs) is regulated by the carbon source, although less readily metabolizable carbon sources do improve LME production. The present study analyzed the effect of glycerol on growth, total DyP activity, and the expression of three genes (-- and -), real-time RT-qPCR, monitoring the time course of cultures supplemented with either glycerol or glucose and Acetyl Yellow G (AYG) dye. The results obtained indicate that glycerol negatively affects growth, giving a biomass production of 5.31 and 5.62 g/L with respective growth rates (micra; m) of 0.027 and 0.023 h for fermentations in the absence and presence of AYG dye. In contrast, respective biomass production levels of 7.09 and 7.20 g/L and growth rates (μ) of 0.033 and 0.047 h were observed in equivalent control fermentations conducted with glucose in the absence and presence of AYG dye. Higher DyP activity levels, 4,043 and 4,902 IU/L, were obtained for fermentations conducted on glycerol, equivalent to 2.6-fold and 3.16-fold higher than the activity observed when glucose is used as the carbon source. The differential regulation of the DyP-encoding genes in s were explored, evaluating the carbon source, the growth phase, and the influence of the dye. The global analysis of the expression patterns throughout the fermentation showed the up- and down- regulation of the three - genes evaluated. The highest induction observed for the control media was that found for the - gene, which is equivalent to an 11.1-fold increase in relative expression (log) during the stationary phase of the culture (360 h), and for the glucose/AYG media was with 8.28-fold increase after 168 h. In addition, glycerol preferentially induced the - and - genes, leading to respective 11.61 and 4.28-fold increases after 144 h. After 360 and 504 h of culture, 12.86 and 4.02-fold increases were observed in the induction levels presented by - and -, respectively, in the presence of AYG. When transcription levels were referred to those found in the control media, adding AYG led to up-regulation of the three genes throughout the fermentation. Contrary to the fermentation with glycerol, where up- and down-regulation was observed. The present study is the first report describing the effect of a less-metabolizable carbon source, such as glycerol, on the differential expression of DyP-encoding genes and their corresponding activity.
Topics: Glycerol; Pleurotus; Coloring Agents; Carbon; Gene Expression Regulation, Fungal; Peroxidases; Glucose
PubMed: 38827301
DOI: 10.7717/peerj.17467 -
Zhonghua Bing Li Xue Za Zhi = Chinese... Jun 2024
Topics: Humans; Male; Young Adult; Granulomatosis with Polyangiitis; Schizophyllum; Schistosomiasis; Cough; Diagnosis, Differential
PubMed: 38825916
DOI: 10.3760/cma.j.cn112151-20230907-00142 -
Biotechnology For Biofuels and... Jun 2024Manganese peroxidases (MnPs) are, together with lignin peroxidases and versatile peroxidases, key elements of the enzymatic machineries secreted by white-rot fungi to...
Structure-function characterization of two enzymes from novel subfamilies of manganese peroxidases secreted by the lignocellulose-degrading Agaricales fungi Agrocybe pediades and Cyathus striatus.
BACKGROUND
Manganese peroxidases (MnPs) are, together with lignin peroxidases and versatile peroxidases, key elements of the enzymatic machineries secreted by white-rot fungi to degrade lignin, thus providing access to cellulose and hemicellulose in plant cell walls. A recent genomic analysis of 52 Agaricomycetes species revealed the existence of novel MnP subfamilies differing in the amino-acid residues that constitute the manganese oxidation site. Following this in silico analysis, a comprehensive structure-function study is needed to understand how these enzymes work and contribute to transform the lignin macromolecule.
RESULTS
Two MnPs belonging to the subfamilies recently classified as MnP-DGD and MnP-ESD-referred to as Ape-MnP1 and Cst-MnP1, respectively-were identified as the primary peroxidases secreted by the Agaricales species Agrocybe pediades and Cyathus striatus when growing on lignocellulosic substrates. Following heterologous expression and in vitro activation, their biochemical characterization confirmed that these enzymes are active MnPs. However, crystal structure and mutagenesis studies revealed manganese coordination spheres different from those expected after their initial classification. Specifically, a glutamine residue (Gln333) in the C-terminal tail of Ape-MnP1 was found to be involved in manganese binding, along with Asp35 and Asp177, while Cst-MnP1 counts only two amino acids (Glu36 and Asp176), instead of three, to function as a MnP. These findings led to the renaming of these subfamilies as MnP-DDQ and MnP-ED and to re-evaluate their evolutionary origin. Both enzymes were also able to directly oxidize lignin-derived phenolic compounds, as seen for other short MnPs. Importantly, size-exclusion chromatography analyses showed that both enzymes cause changes in polymeric lignin in the presence of manganese, suggesting their relevance in lignocellulose transformation.
CONCLUSIONS
Understanding the mechanisms used by basidiomycetes to degrade lignin is of particular relevance to comprehend carbon cycle in nature and to design biotechnological tools for the industrial use of plant biomass. Here, we provide the first structure-function characterization of two novel MnP subfamilies present in Agaricales mushrooms, elucidating the main residues involved in catalysis and demonstrating their ability to modify the lignin macromolecule.
PubMed: 38824538
DOI: 10.1186/s13068-024-02517-1 -
Environmental Science and Pollution... Jun 2024Currently, large quantities of spent mushroom substrate (SMS) are produced annually. Because SMS has high water retention and nutrients, it has great potential to...
Currently, large quantities of spent mushroom substrate (SMS) are produced annually. Because SMS has high water retention and nutrients, it has great potential to replace traditional topsoil for raising seedlings in agricultural production. However, few studies have examined the effects of substituting SMS for paddy soil on rice seedling growth and soil nutrients. SMS was mixed with rice soil in different proportions (20%, 50%, and 80%), and chemical fertilizer, organic fertilizer, and peat substrate were added in addition to equivalent nitrogen as a traditional seedling nursery method for comparison. Compared to traditional paddy soil (CK), the seedling qualities of the three SMS ratio treatments were all higher. Adding SMS at different ratios promoted rice seedling root growth, elevated the soluble protein concentration, and amplified the superoxide dismutase (SOD) enzymatic action in rice seedlings. Total porosity and aeration porosity of the soil increased by 17.40% and 32.90%, respectively. Soil organic carbon (SOC), total nitrogen (TN), and total phosphorus (TP) increased by 21.26-118.48%, 50.44-71.68%, and 23.08-80.17%, respectively. Besides, the relative abundance of Bacillus, Bacteroidetes, and other bacteria as well as the abundance of Ascomycota were all significantly increased. Adding 50% SMS increased the abundance of Pseudomonas by 8.42 times. The seedling quality of the 50% SMS treatment was even higher than chemical fertilizer and organic fertilizer treatments, only second to the peat substrate treatment. In summary, partial substitution of paddy soil with SMS can ameliorate substrate properties, improve seedling quality, and increase microbial diversity, indicating the suitability of SMS as a replacement for rice soil in seedling substrates. The 50% SMS ratio is the best. This study provides a basis for SMS to replace traditional rice soil in seedling cultivation.
Topics: Oryza; Soil; Seedlings; Agaricales; Nitrogen; Fertilizers; Agriculture; Soil Microbiology; Phosphorus
PubMed: 38824472
DOI: 10.1007/s11356-024-33723-x -
Carbohydrate Polymers Sep 2024This study explored the physicochemical properties and structural characteristics of Agrocybe cylindracea polysaccharides at four developmental stages, as well as their...
This study explored the physicochemical properties and structural characteristics of Agrocybe cylindracea polysaccharides at four developmental stages, as well as their dynamic evolution during maturation. Results showed that the polysaccharides from A. cylindracea water extract exhibited similar structural characteristics across all four maturity stages, despite a significant reduction in yields. Four water-soluble heteroglycans, including one high molecular weight (ACPM-Et50-I) and three low molecular weight (ACPM-Et50-II, ACPM-Et60, ACPM-Et80), were isolated from A. cylindracea at each maturity stage. ACPM-Et50-I was identified as branched heterogalactans, while ACPM-Et60 and ACPM-Et80 were branched heteroglucans. However, ACPM-Et50-II was characterized as a branched glucuronofucogalactoglucan at the tide-turning stage but a glucuronofucoglucogalactan at the pileus expansion stage due to the increase of its α-(1 → 6)-D-Galp. In general, although the structural skeletons of most A. cylindracea heteroglycans were similar during maturation as shown by their highly consistent glycosyl linkages, there were still differences in the distribution of some heteroglucans. This work has for the first time reported a glucuronofucogalactoglucan in A. cylindracea and its dynamic evolution during maturation, which may facilitate the potential application of A. cylindracea in food and biomedicine industries.
Topics: Water; Agrocybe; Glucans; Polysaccharides; Molecular Weight
PubMed: 38823906
DOI: 10.1016/j.carbpol.2024.122235 -
Food Research International (Ottawa,... Jul 2024In this study, inactivation of mushroom polyphenol oxidase (PPO) by low intensity direct current (DC) electric field and its molecular mechanism were investigated. In...
In this study, inactivation of mushroom polyphenol oxidase (PPO) by low intensity direct current (DC) electric field and its molecular mechanism were investigated. In the experiments under 3 V/cm, 5 V/cm, 7 V/cm and 9 V/cm electric fields, PPOs were all completely inactivated after different exposure times. Under 1 V/cm, a residual activity of 11.88 % remained. The inactivation kinetics confirms to Weibull model. Under 1-7 V/cm, n value closes to a constant about 1.3. The structural analysis of PPO under 3 V/cm and 5 V/cm by fluorescence emission spectroscopy and molecular dynamics (MD) simulation showed that the tertiary structure was slightly changed with increased radius of gyration, higher potential energy and rate of C-alpha fluctuation. After exposure to the electric field, most of the hydrophobic tryptophan (TRP) residues turned to the hydrophilic surface, resulting the fluorescence red-shifted and quenched. Molecular docking indicated that the receptor binding domain of catechol in PPO was changed. PPO under electric field was MD simulated the first time, revealing the changing mechanism of the electric field itself on PPO, a binuclear copper enzyme, which has a metallic center. All these suggest that the low intensity DC electric field would be a promising option for enzymatic browning inhibition or even enzyme activity inactivation.
Topics: Catechol Oxidase; Molecular Docking Simulation; Molecular Dynamics Simulation; Spectrometry, Fluorescence; Kinetics; Electricity; Agaricales; Catechols
PubMed: 38823824
DOI: 10.1016/j.foodres.2024.114325 -
International Journal of Biological... Jun 2024Bacterial Metabolite through a fermentation process is a growing trend and a promising alternative for use as functional components. Non-hydrothermal water-soluble...
Metabolomic differences between non-hydrothermal treated water-soluble (WSPs) and hydrothermally treated water-insoluble (WIPs) Maitake polysaccharides fermented by Lactobacillus acidophilus and L. plantarum.
Bacterial Metabolite through a fermentation process is a growing trend and a promising alternative for use as functional components. Non-hydrothermal water-soluble (WSPs) and hydrothermally treated water-insoluble (WIPs) Maitake polysaccharides were fermented with Lactobacillus acidophilus (LA) and Lactobacillus plantarum (LP). Chemical composition analysis indicated that Maitake polysaccharides contained 58.22 ± 1.35 % total sugar and 31.46 % β-glucan, essential for metabolites production. 6-glucanase was used to degrade the WIPs, and hydrothermally treated WIP fibers exhibited smooth microstructure. Hence, the LA and LP bacteria investigated the potential fermented metabolic activities and differences between WSPs(Sp1)and WIP(Sp3) Maitake polysaccharides using LC-MS, and 887 metabolites were identified. Using Venn, Partial least squares discriminant analysis (PLS-DA), VIP Metabolites, and other multivariate statistical analysis methods, metabolites were expressed differently in all samples. Due to hydrothermal processing, WIP induced the highest growth of LA and LP, with an abundance of isocitrate metabolites. Furthermore, 50 metabolite correlations were identified, leading to the classification of 6 distinct metabolic groups. Thus, the study offers the initial comprehensive analysis of metabolites in Lactobacillus-fermented Maitake polysaccharides, aiding in understanding its metabolic interactions and facilitating progress in food engineering research.
Topics: Lactobacillus plantarum; Lactobacillus acidophilus; Polysaccharides; Fermentation; Water; Solubility; Metabolomics; Metabolome; Shiitake Mushrooms
PubMed: 38815943
DOI: 10.1016/j.ijbiomac.2024.132709 -
Journal of Enzyme Inhibition and... Dec 2024Tyrosinase, a pivotal enzyme in melanin synthesis, is a primary target for the development of depigmenting agents. In this work, and techniques were employed to...
Tyrosinase, a pivotal enzyme in melanin synthesis, is a primary target for the development of depigmenting agents. In this work, and techniques were employed to identify novel tyrosinase inhibitors from a set of 12 anilino-1,4-naphthoquinone derivatives. Results from the mushroom tyrosinase activity assay indicated that, among the 12 derivatives, three compounds (, , and ) demonstrated the most significant inhibitory activity against mushroom tyrosinase, surpassing the effectiveness of the kojic acid. Molecular docking revealed that all studied derivatives interacted with copper ions and amino acid residues at the enzyme active site. Molecular dynamics simulations provided insights into the stability of enzyme-inhibitor complexes, in which compounds , , and particularly displayed greater stability, atomic contacts, and structural compactness than kojic acid. Drug likeness prediction further strengthens the potential of anilino-1,4-naphthoquinones as promising candidates for the development of novel tyrosinase inhibitors for the treatment of hyperpigmentation disorders.
Topics: Monophenol Monooxygenase; Naphthoquinones; Enzyme Inhibitors; Agaricales; Structure-Activity Relationship; Molecular Structure; Dose-Response Relationship, Drug; Molecular Docking Simulation; Molecular Dynamics Simulation
PubMed: 38814149
DOI: 10.1080/14756366.2024.2357174