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Journal of Agricultural and Food... Apr 2022Four new carotane sesquiterpenoids, byssocarotins A-D (-), two new nor-sesquiterpenoids, byssofarnesin () and byssosesquicarin (), and three new polyketides,...
Four new carotane sesquiterpenoids, byssocarotins A-D (-), two new nor-sesquiterpenoids, byssofarnesin () and byssosesquicarin (), and three new polyketides, byssoketides A and B ( and ) and (8)-paecilocin A (), were obtained from a macroalga-associated strain (RR-dl-2-13) of the fungus . These isolates were identified by a combination of spectroscopic methods, including mass spectroscopy, nuclear magnetic resonance, electronic circular dichroism, and X-ray diffraction. Compounds - greatly contribute to the diversity of rarely occurring 2,15-epoxycarotane sesquiterpenoids, while and are degradation products of farnesane and sesquicarane precursors, respectively. Compound is a structurally unique furan fatty acid derivative that possesses an aldehyde group and a large conjugated unit, and features a hemiketal group. During antimicrobial assays, showed antagonism against the phytopathogenic fungi , f. sp. , and f. sp. and the marine-derived bacteria and with MIC values of 13 to 50 μg/mL.
Topics: Anti-Bacterial Agents; Byssochlamys; Fungi; Molecular Structure; Polyketides; Terpenes
PubMed: 35384660
DOI: 10.1021/acs.jafc.2c00259 -
Journal of Fungi (Basel, Switzerland) May 2021Two novel xylanolytic enzymes, a xylanase and a β-xylosidase, were simultaneously isolated and characterized from the extracellular medium of ATHUM 8891 (anamorph...
Two novel xylanolytic enzymes, a xylanase and a β-xylosidase, were simultaneously isolated and characterized from the extracellular medium of ATHUM 8891 (anamorph ATHUM 8891), grown on Brewer's Spent Grain as a sole carbon source. They represent the first pair of characterized xylanolytic enzymes of the genus and the first extensively characterized xylanolytic enzymes of the family . In contrast to other xylanolytic enzymes isolated from the same family, both enzymes are characterized by exceptional thermostability and stability at low pH values, in addition to activity optima at temperatures around 65 °C and acidic pH values. Applying nano-LC-ESI-MS/MS analysis of the purified SDS-PAGE bands, we sequenced fragments of both proteins. Based on sequence-comparison methods, both proteins appeared conserved within the genus . Xylanase was classified within Glycoside Hydrolase family 11 (GH 11), while β-xylosidase in Glycoside Hydrolase family 3 (GH 3). The two enzymes showed a synergistic action against xylan by rapidly transforming almost 40% of birchwood xylan to xylose. The biochemical profile of both enzymes renders them an efficient set of biocatalysts for the hydrolysis of xylan in demanding biorefinery applications.
PubMed: 34072339
DOI: 10.3390/jof7060430 -
Preparative Biochemistry & Biotechnology 2018The objective of the present study was to optimize parameters for the cultivation of Lichtheimia corymbifera (mesophilic) and Byssochlamys spectabilis (thermophilic) for...
The objective of the present study was to optimize parameters for the cultivation of Lichtheimia corymbifera (mesophilic) and Byssochlamys spectabilis (thermophilic) for the production of β-glucosidases and to compare the catalytic and thermodynamic properties of the partially purified enzymes. The maximum amount of β-glucosidase produced by L. corymbifera was 39 U/g dry substrate (or 3.9 U/mL), and that by B. spectabilis was 77 U/g (or 7.7 U/mL). The optimum pH and temperature were 4.5 and 55 °C and 4.0 and 50 °C for the enzyme from L. corymbifera and B. spectabilis, respectively. β-Glucosidase produced by L. corymbifera was stable at pH 4.0-7.5, whereas the enzyme from B. spectabilis was stable at pH 4.0-6.0. Regarding the thermostability, β-glucosidase produced by B. spectabilis remained stable for 1 h at 50 °C, and that from L. corymbifera was active for 1 h at 45 °C. Determination of thermodynamic parameters confirmed the greater thermostability of the enzyme produced by the thermophilic fungus B. spectabilis, which showed higher values of ΔH, activation energy for denaturation (E), and half-life t. The enzymes were stable in the presence of ethanol and were competitively inhibited by glucose. These characteristics contribute to their use in the simultaneous saccharification and fermentation of vegetable biomass.
Topics: Byssochlamys; Catalysis; Cellulases; Culture Techniques; Enzyme Inhibitors; Ethanol; Fungal Proteins; Glucose; Hydrogen-Ion Concentration; Kinetics; Mucorales; Temperature; Thermodynamics
PubMed: 30303453
DOI: 10.1080/10826068.2018.1509083 -
European Journal of Medicinal Chemistry Feb 2018Bysspectin A (1), a polyketide-derived octaketide dimer with a novel carbon skeleton, and two new precursor derivatives, bysspectins B and C (2 and 3), were obtained...
Bysspectin A (1), a polyketide-derived octaketide dimer with a novel carbon skeleton, and two new precursor derivatives, bysspectins B and C (2 and 3), were obtained from an organic extract of the endophytic fungus Byssochlamys spectabilis that had been isolated from a leaf tissue of the traditional Chinese medicinal plant Edgeworthia chrysantha, together with a known octaketide, paecilocin A (4). Their structures were determined by HRMS, 1D and 2D NMR spectroscopic analysis. A plausible route for their biosynthetic pathway is proposed. Compounds 1-3 were tested for their antimicrobial activities. Only compound 3 was weakly active against Escherichia coli and Staphyloccocus aureus with MIC values of 32 and 64 μg/mL, respectively. Further, the inhibitory effects on human carboxylesterases (hCE1, hCE2) of compounds 1 and 4 were evaluated. The results demonstrated that bysspectin A (1) was a novel and highly selective inhibitor against hCE2 with the IC value of 2.01 μM. Docking simulation also demonstrated that active compound 1 created interaction with the Ser-288 (the catalytic amino-acid in the catalytic cavity) of hCE2 via hydrogen bonding, revealing its highly selective inhibition toward hCE2.
Topics: Anti-Bacterial Agents; Biocatalysis; Byssochlamys; Carboxylesterase; Carboxylic Ester Hydrolases; Dimerization; Dose-Response Relationship, Drug; Enzyme Inhibitors; Escherichia coli; Humans; Microbial Sensitivity Tests; Molecular Docking Simulation; Molecular Structure; Polyketides; Staphylococcus aureus; Structure-Activity Relationship
PubMed: 29353723
DOI: 10.1016/j.ejmech.2018.01.030 -
Genome Announcements Jan 2014Byssochlamys spectabilis no. 5 (anamorph Paecilomyces variotii no. 5) (NBRC109023) was isolated from a soil sample in 2001 in Kumamoto Prefecture, Japan. This fungus is...
Byssochlamys spectabilis no. 5 (anamorph Paecilomyces variotii no. 5) (NBRC109023) was isolated from a soil sample in 2001 in Kumamoto Prefecture, Japan. This fungus is highly resistant to formaldehyde. Here, we report a draft genome sequence of P. variotii no. 5; this draft was produced with the intent of investigating the mechanism of formaldehyde resistance. This is the first report of the genome sequence of any Paecilomyces species.
PubMed: 24407650
DOI: 10.1128/genomeA.01162-13 -
Applied and Environmental Microbiology Mar 2008Paecilomyces variotii is a common cosmopolitan species that is able to spoil various food- and feedstuffs and is frequently encountered in heat-treated products.... (Comparative Study)
Comparative Study
Paecilomyces variotii is a common cosmopolitan species that is able to spoil various food- and feedstuffs and is frequently encountered in heat-treated products. However, isolates from heat-treated products rarely form ascospores. In this study we examined by using molecular techniques and mating tests whether this species can undergo a sexual cycle and form ascospores. The population structure of this species was examined by analyzing the nuclear ribosomal internal transcribed spacer 1 (ITS1) and ITS2 and the 5.8S rRNA gene, as well as partial beta-tubulin, actin, and calmodulin gene sequences. Phylogenetic analyses revealed that P. variotii is a highly variable species. Partition homogeneity tests revealed that P. variotii has a recombining population structure. In addition to sequence analyses, mating experiments indicated that P. variotii is able to form ascomata and ascospores in culture in a heterothallic manner. The distribution of MAT1-1 and MAT1-2 genes showed a 1:1 ratio in the progeny of the mating experiments. From the sequence analyses and mating data we conclude that P. variotii is the anamorph of Talaromyces spectabilis and that it has a biallelic heterothallic mating system. Since Paecilomyces sensu stricto anamorphs group within Byssochlamys, a new combination Byssochlamys spectabilis is proposed.
Topics: Actins; Adaptation, Physiological; Base Sequence; Calmodulin; Cluster Analysis; Crosses, Genetic; DNA Primers; DNA, Ribosomal Spacer; Food Microbiology; Genetics, Population; Hot Temperature; Molecular Sequence Data; Paecilomyces; Phylogeny; RNA, Ribosomal, 5.8S; Reproduction; Sequence Analysis, DNA; Spores, Fungal; Tubulin
PubMed: 18192427
DOI: 10.1128/AEM.01761-07 -
Applied Biochemistry and Biotechnology Oct 2015Paecilomyces variotii isolated from a broad range of habitats drives the diversification of new high-value-added secondary metabolites that could potentially play an... (Review)
Review
Paecilomyces variotii isolated from a broad range of habitats drives the diversification of new high-value-added secondary metabolites that could potentially play an important role in human and animal health. These metabolites include the anhydride metabolite of the nonadride family, as well as the following compounds: naphthopyranone metabolites, sphingofungins, eicosenoic acids, new branched fatty acids, ascofuranone, polyketides, an anacardic acid analogue, straight-chain peptides, and volatile compounds. These natural products show that P. variotii can provide leading compounds for new drug discoveries, which may include herbicide agents, some of which are important in the agrochemical market. Finally, this review outlines recent developments, trends, and prospects for the chemistry of this ascomycete.
Topics: Animals; Biological Products; Humans; Organic Chemicals; Paecilomyces
PubMed: 26288080
DOI: 10.1007/s12010-015-1783-z -
European Journal of Medicinal Chemistry Nov 2023Human carboxylesterase 2A (hCES2A), the most abundant carboxylesterase in the human gut, plays a crucial role in the metabolic clearance and activation of various...
Human carboxylesterase 2A (hCES2A), the most abundant carboxylesterase in the human gut, plays a crucial role in the metabolic clearance and activation of various ester-bearing drugs, environmental toxins and carcinogens. Inhibition of intestinal hCES2A can alleviate irinotecan-induced gut toxicity and modulate the oral bioavailability of hCES2A-substrate drugs. Bysspectin A, a natural product isolated from the endophytic fungus Byssochlamys spectabilis, has been identified as a highly selective hCES2A inhibitor. Herein, two sets of bysspectin A derivatives have been designed and synthesized, utilizing a Cu-catalyzed domino Sonogashira-cyclization as the key step. Following two rounds of structure activity relationship (SAR) studies and structural optimizations, compound 20w was identified as the most potent hCES2A inhibitor, with an IC value of 1.6 nM, an approximately 1000-fold improvement over bysspectin A. Further investigation showed that 20w potently inhibited hCES2A in a mixed inhibition manner, while this agent could also potently inhibit intracellular hCES2A in living cells and exhibited suitable metabolic stability. In summary, our findings demonstrate that a new bysspectin A derivative (20w) is a promising candidate for the development of clinically used hCES2A inhibitor.
Topics: Humans; Enzyme Inhibitors; Carboxylesterase; Polyketides; Structure-Activity Relationship; Irinotecan
PubMed: 37544184
DOI: 10.1016/j.ejmech.2023.115708 -
Allergy Mar 2022
Topics: Allergens; Byssochlamys; Humans; Paecilomyces
PubMed: 34773271
DOI: 10.1111/all.15176 -
Food Research International (Ottawa,... Feb 2022Daqu and wheat Qu are saccharification and fermenting agents in Chinese huangjiu and baijiu production. This study aimed to investigate the difference between Daqu and...
Daqu and wheat Qu are saccharification and fermenting agents in Chinese huangjiu and baijiu production. This study aimed to investigate the difference between Daqu and wheat Qu in physicochemical indices, microbial communities, functional genes, and the metabolic network of key microbes responsible for flavor synthesis by whole-metagenome sequencing and metabolite analysis. Herein, physicochemical indices indicated that compared with wheat Qu, Daqu exhibited higher protease and cellulase activity and acidity, and lower glucoamylase and amylase enzyme activity. Metagenomic sequencing reveals that although Daqu and wheat Qu community composition have significant differences at species level, they have similar functional genes. Daqu were enriched in Pediococcus pentosaceus, Weissella paramesenteroides, Rasamsonia emersonii and Byssochlamys spectabilis (22.48% of the total abundance), while wheat Qu harbored greater abundances of Saccharopolyspora (54.78%, Saccharopolyspora rectivirgula, Saccharopolyspora shandongensis, Saccharopolyspora hirsuta, Saccharopolyspora spinose, and Saccharopolyspora erythraea). From a functional perspective, the important functions of Daqu and wheat Qu are both amino acid metabolism and carbohydrate metabolism. Meanwhile, a combined analysis among microbiota, functional genes, and dominant flavors indicated S. shandongensis, S. rectivirgula, and S. spinose might be the main contributor to the synthesis of flavor compounds in wheat Qu, while R. emersonii, W. paramesenteroides, Leuconostoc citreum, Leuconostoc mesenteroides, Weissella cibaria and P. pentosaceus may make the greatest contribution to flavor compounds synthesis in Daqu. This study reveals the microbial and functional dissimilarities of Daqu and wheat Qu, and helps elucidating different metabolic roles of microbes during flavor formation.
Topics: Amylases; Fermentation; Metabolic Networks and Pathways; Metagenomics; Microbiota
PubMed: 35181108
DOI: 10.1016/j.foodres.2021.110707