Journal of Industrial Microbiology & Biotechnology最新文献

{"title":"Thermostability and pH Differentiation in Geobacillus Hydrolases: A Comparative Perspective.","authors":"Elifnur Akbiyik, Ayse Varol, Zehra Betul Tekgul, Berna Genc, Ahmet Adiguzel","doi":"10.1093/jimb/kuag027","DOIUrl":"https://doi.org/10.1093/jimb/kuag027","url":null,"abstract":"<p><p>Thermostable enzymes are central to high-temperature industrial processes because they combine catalytic efficiency with structural resilience under demanding conditions. Among thermophilic bacteria, Geobacillus has emerged as a prominent source of industrially relevant enzymes, particularly hydrolases such as proteases, lipases, and carbohydrate-active enzymes. Although many individual enzymes have been characterized in detail, comparative synthesis across catalytic classes within the genus remains limited. In this review, we integrate biochemical data and structural evidence to explore whether thermostability in Geobacillus reflects isolated enzyme-specific traits or recurring functional patterns across enzyme classes. Reported Tmax and pHmax values from purified and partially purified hydrolases were systematically compiled to assess class-level tendencies. Temperature optima cluster within a relatively narrow thermophilic range across enzyme groups, supporting high-temperature activity as a common feature within the genus. In contrast, pH optima display clearer functional differentiation, with proteases and lipases consistently shifted toward alkaline values relative to carbohydrate-active hydrolases. Recurrent stabilizing elements, including reinforced hydrophobic cores, expanded electrostatic interaction networks, and a balanced rigidity-flexibility profile, are observed across multiple enzyme classes, indicating shared structural trends rather than independent enzyme-specific variation. By situating catalytic optima within a comparative framework and relating them to shared structural determinants, this review provides a comparative interpretation of patterns observed across Geobacillus-derived enzymes, linking structure, catalysis, and functional adaptation.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149136857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploration of yeast biodiversity from Thai flowers and optimization of carotenoid production by a promising isolate.","authors":"Pirapan Polburee, Thippawan Kodpan, Krittawan Tondee, Nontakorn Wimoolchat","doi":"10.1093/jimb/kuag003","DOIUrl":"10.1093/jimb/kuag003","url":null,"abstract":"<p><p>Microbial synthesis of carotenoids has garnered significant attention as an eco-friendly alternative to conventional synthetic methods and its facile extraction for impressive yield. This study delves into the efficacy of carotenoid production from a red yeast strain, as well as the biodiversity of yeast species from Thai flowers. The research involved the collection of flower samples within Thailand, along with 12 yeast species from 10 genera of Ascomycetes and 4 genera of Basidiomycetes which were isolated by identifying the D1/D2 domain of the large subunit rRNA gene. Unexpectedly, Rhodotorula paludigena SWU-FKT03 emerged as the top performing yeast strain, boasting an impressive carotenoid production rate of 183.30 ± 5.00 mg/L among the 36 red yeast strains isolated. Subsequently, a further investigation was performed, focusing on optimized culture conditions for carotenoid production from this yeast strain. The results were promising, as carotenoid production surged to 288.27 mg/L when 20 g/L of glucose and 10 g/L of monosodium glutamate served as the carbon and nitrogen sources, respectively. These findings underscore the potential of the R. paludigena SWU-FKT03 as a high-yield carotenoid producer when cultivated in shaking flasks, exhibiting a three-fold increase in carotenoid content when under optimized conditions. These results hint at the potential of this approach for future large-scale carotenoid production. One-sentence summary A novel red yeast, Rhodotorula paludigena SWU-FKT03, isolated from Thai floral ecosystems, demonstrated high-yield carotenoid production of 288.27 mg/L after fermentation optimization, establishing a significant potential for industrial applications.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12883991/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145933580","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bio-inspired designer cellulosomes show strongest synergy on industrial substrates under natural-like conditions.","authors":"Babette Lamote, Julie Vanderstraeten, Nette De Ridder, Kenan Meert, Wout Boerjan, Yves Briers","doi":"10.1093/jimb/kuag004","DOIUrl":"10.1093/jimb/kuag004","url":null,"abstract":"<p><p>Designer cellulosomes (DCs) are engineered multienzyme complexes inspired by natural cellulosomes, designed to improve lignocellulose breakdown. Their modular architecture enables the spatial colocalization of diverse catalytic activities, potentially enhancing depolymerization efficiency compared to free enzymes. Although conceptually promising, little is known about how they perform on complex lignocellulosic substrates. In this study, we developed a tetravalent DC using a modular VersaTile assembly approach, incorporating endoglucanase, cellobiohydrolase, β-glucosidase, and endoxylanase activities. The process involved (i) delineating catalytic modules from Cellvibrio japonicus enzymes, (ii) generating docking enzyme variants via combinatorial cloning, and (iii) selecting optimal candidates based on expression, activity, and cohesin-dockerin binding before assembling them onto a scaffoldin with four cohesins and a cellulose-binding module. The resulting DC was tested on two industrially relevant substrates: agro-industrial wheat fibers and genome-edited low-lignin poplar biomass under controlled laboratory conditions. It achieved cellulose-to-glucose conversion yields of 24.98% (150 pmol DC/ml) and 0.82% (200 pmol DC/ml), respectively, under the test conditions. By comparing the saccharification efficiencies of the enzymes in their free and complexed forms, we found that colocalization on a common scaffoldin significantly enhanced synergistic activity. This effect was most pronounced under low enzyme concentrations and when acting on complex lignocellulosic substrates, increasing glucose release compared to free enzymes. These observations highlight that the benefits of colocalization are substrate-dependent and occur under conditions that mimic the natural environment of biomass degradation, conditions that differ from typical industrial settings. This work advances our understanding of DC behavior on real-world substrates, providing essential insights for evaluating their economic viability in industrial applications. One-sentence summary Natural-like conditions helped customized DC release more sugars from biomass than standard industrial setups.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12963819/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146064306","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The biosynthetic gene cluster landscape of the oral microbiome across health and dental caries.","authors":"McKenna Loop Yao, Peijun Lin, Kailey Hua, Wenjun Zhang","doi":"10.1093/jimb/kuag005","DOIUrl":"10.1093/jimb/kuag005","url":null,"abstract":"<p><p>Specialized metabolites encoded by biosynthetic gene clusters (BGCs) in the oral microbiome remain largely unexplored in the context of oral health and disease. Previous genome-centric surveys have identified hundreds of uncharacterized BGCs in the oral cavity associated with health and disease, but these studies relied on reference genomes and did not capture strain-level variation or the native distribution of BGCs. Here, we assembled three independently sourced metagenomic datasets from healthy and dental caries samples, extracted BGCs and quantified their metagenomic abundance and transcriptional activity. We found that aryl polyene, ribosomally synthesized and posttranslationally modified peptide, and nonribosomal peptide encoding BGCs were the most prominent BGCs identified across the three metagenomic datasets. We grouped the identified BGCs into homology-based gene cluster families (GCFs) and found that specific GCFs were consistently associated with either health or caries across diverse taxa, suggesting that some specialized metabolites may perform conserved ecological functions. Conversely, other BGCs showed more restricted taxonomic distributions and were linked to disease-associated taxa, such as Propionibacterium acidifaciens, suggesting niche-specific biosynthetic capacities within the oral environment. Applying elastic-net regression to the metatranscriptomic dataset further identified a subset of 51 BGCs out >3,000 that distinguished healthy from caries samples, reinforcing the discriminatory power of BGC expression patterns. These results demonstrate that BGCs can provide functional resolution beyond taxonomic profiling and that BGC expression, rather than genomic presence alone, can differentiate oral microbial community states. This underscores the relevance of specialized metabolism to oral health and supports the use of BGC-centric analyses to interrogate microbial interactions underlying community stability and disease-associated shifts. One-sentence summary Specialized metabolites in oral bacteria are differentially expressed in healthy and cavity-affected communities.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13455363/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146064296","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Demonstration of an integrated process for manure-based nitrogen recovery using the biopolymer cyanophycin.","authors":"Kevin Fitzgerald, Hang Dong, Edward Apraku, Md Aminul Islam Prodhan, Dylan Hakken, George Wells, William Tarpeh, Keith Tyo","doi":"10.1093/jimb/kuag023","DOIUrl":"10.1093/jimb/kuag023","url":null,"abstract":"<p><p>The trend toward concentrated animal feeding operations (CAFOs) has served to concentrate not only livestock animals but the waste they produce to comparatively smaller areas. The point-source nature of this waste is an opportunity for the recovery and valorization of the nitrogen therein. Such a process would be viable on small to intermediate scales and require minimal inputs at the CAFO. In this study, we demonstrate the potential of the biopolymer cyanophycin to serve as a medium for manure-nitrogen recovery. In the first step, genetically modified strains of Escherichia coli produce intracellular cyanophycin from mock manure hydrolysates. Next, cyanophycin is recovered from microbial biomass via acid solubilization and base precipitation using electrochemically generated acids and bases. Finally, to improve both the yield and recoverable fraction of cyanophycin produced, we leverage the tunability of our genetically engineered system to probe the impacts of cyanophycin synthetase solubility, N-domain activity, and cyanophycin molecular weight on cyanophycin recoverability. Collectively, this work serves as a proof of concept for nitrogen recovery from agricultural waste, aligning with global sustainability initiatives. One sentence summary Mock manure-derived substrates can be converted to cyanophycin and recovered, supporting the feasibility of nitrogen recovery at potentially decentralized sites of waste production.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13548846/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148794176","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Proteome-wide analysis of protein stability in Escherichia coli under acid stress.","authors":"Onyeka Onyenemezu, Jeffrey N Law, Jetendra K Roy, Chao Wu, Joel Nott, Robert L Jernigan, Laura R Jarboe","doi":"10.1093/jimb/kuag016","DOIUrl":"10.1093/jimb/kuag016","url":null,"abstract":"<p><p>Knowledge of protein acid sensitivity remains sparse and is largely derived from low-throughput, enzyme-specific assays. We used a scalable framework to map acid stability across the Escherichia coli proteome to assess the acid stability of 1,675 unique proteins, estimating pH50 values for over 90% of them. The parameter pH50 was defined as the pH value at which only 50% of the initial protein remains in solution following acid treatment. Proteome-wide pH50 values ranged from 2.28 to 6.33 (median 5.11). Approximately 9% of detected proteins remained stable across all tested pH conditions. Our results align with published data and the assay of citrate synthase (GltA) performed here. Protein acid stability differed significantly by subcellular localization: periplasmic proteins were relatively more abundant in the acid-stable group, cytoplasmic proteins were abundant at pH50 values 4.5-5.5, and inner membrane proteins at higher pH50 between 5.5 and 6.0. Outer membrane proteins were too few to draw strong conclusions regarding enrichment within specific pH50 groups. Notably, the periplasmic binding protein of the molybdate ABC transporter (ModA), was enriched after incubation at low pH. Estimated pH50 values showed no correlation with protein isoelectric point and molecular weight. Together, this work provides the first proteome-wide map of protein acid stability and establishes a general framework for studying different chemical stressors. One sentence summary This paper presents a quantitative map of acid stability of E. coli proteins and established a procedure for the study of protein acid sensitivity that is adaptable to other stressors and other organisms.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13339084/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148361051","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A survey of Burkholderiales secondary metabolites using library-scale stable isotope labeling reveals selective production of methyl-esterified 3-hydroxybutyrate oligomers.","authors":"Liana Zaroubi, Stephanie C Heard, Matthew Sutherland, Alessandra S Eustaquio, Roger G Linington","doi":"10.1093/jimb/kuag026","DOIUrl":"10.1093/jimb/kuag026","url":null,"abstract":"<p><p>Large-scale untargeted bacterial metabolomics studies are often challenging to interpret, particularly for natural product discovery. Complex raw mass spectrometry data contains media components, biotransformation products, workup contaminants, and in-source fragments, making it difficult to resolve true biosynthesized bacterial products from background features. Incorporating stable isotope labels into untargeted workflows enables the selective detection of actively biosynthesized compounds, drastically reducing candidate mass spectrometry features to highlight novel or robustly expressed metabolites. Recently, our lab introduced IsoAnalyst, a parallel stable isotope labeling platform that links secondary metabolites to biosynthetic gene clusters by determining the incorporation rates of a panel of isotopically labeled building blocks. In this study we applied the IsoAnalyst protocol to a library of 114 Burkholderiales strains with the goals of profiling the specialized metabolite chemistry of this bacterial order and connecting detected natural products to their cognate BGCs based on their labeling profiles. While our strain-matching protocol, which evaluates correlations between detected metabolites and BiG-SCAPE-defined gene cluster families, did not yield confident BGC assignments, it successfully highlighted widely distributed metabolites with distinct labeling profiles. We targeted a set of these molecules for isolation, revealing two classes of compounds derived from primary biomolecule metabolism that are implicated in cellular stress responses. The first class of molecules were identified as lysophosphatidyl ethanolamine analogues while the second was characterized via NMR spectroscopy and mass spectrometry as methyl-esterified 3-hydroxybutyrate oligomers (HB6-OMe, HB7-OMe, and HB8-OMe), representing higher-degree polymer units than previously reported. One-sentence summary Large-scale isotope labelling of a panel of 114 Burkholderiales strains reveals the secondary metabolite diversity of this microbial order, leading to the discovery of novel butyric acid polymers.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13614103/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148919899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Engineering Escherichia coli to produce medium chain oleochemicals from C2 substrates.","authors":"Sri Harsha Adusumilli, Shivangi Mishra, Brian F Pfleger","doi":"10.1093/jimb/kuag018","DOIUrl":"10.1093/jimb/kuag018","url":null,"abstract":"<p><p>Many strategies to create a circular bioeconomy have been proposed. To be successful, CO2 must be reduced with renewable energy into chemical building blocks, from which the chemical industry can be supported. Circular strategies include leveraging photosynthesis to produce sugar and lipid intermediates or renewable electricity to produce hydrogen or other electron carriers to support CO2 reduction. Acetogens can anaerobically reduce CO2 with H2 to produce mixtures of small organic molecules in gas fermentations. We previously demonstrated that acetate, a common product of gas fermentation, can be converted to the model oleochemical dodecanol in engineered Escherichia coli. Here, we explored the conversion of ethanol and mixtures of ethanol and acetate to the same model oleochemicals. Co-feeding ethanol can supply both carbon and additional reducing power relative to acetate alone. In this work, we engineered E. coli to catabolize ethanol and expressed two distinct ethanol metabolism pathways in different operons and combined them with improved engineered acetate activation. We evaluated the performance of these operons in dodecanol-producing strains when fed ethanol or acetate and found ethanol to be a better carbon source when judged by product titers. The engineered strains fed ethanol produced about two-fold more dodecanol than the strains fed acetate. This increase was in part, due to change in product distribution. Cells fed ethanol produced predominantly dodecanol, whereas cells fed acetate generated a mixture of dodecanol and dodecanoic acid. Dodecanol titers were further improved by employing feeding strategies in controlled bioreactors.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13373575/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bacterial contamination in starch-to-ethanol fermentations: Can bacteriocin-producing Saccharomyces cerevisiae offer a solution?","authors":"Michelle Rossouw, Bianca J Campbell, Rosemary A Cripwell, Leon M T Dicks, Marinda Viljoen-Bloom","doi":"10.1093/jimb/kuag011","DOIUrl":"10.1093/jimb/kuag011","url":null,"abstract":"<p><p>Increasing interest in the bioeconomy has spurred the development of integrated methods to convert organic waste streams, particularly starch-rich substrates, into bioethanol. However, starch-based ethanol fermentations are vulnerable to bacterial contamination, particularly by lactic acid bacteria (LAB). Severe contamination can cause significant economic losses due to stuck fermentations and ethanol plant shutdowns. Although bacterial contamination can be managed with antibiotics, this approach is not cost-effective at an industrial scale and may increase the risk of selecting for antibiotic-resistant strains. Natural antimicrobial peptides (AMPs) can inhibit LAB contaminants in yeast fermentations, but commercial applications are limited by their low abundance and high production costs. Engineering Saccharomyces cerevisiae to produce recombinant AMPs might provide a cost-effective strategy to control LAB, thereby boosting ethanol yields during fermentation. Despite a comprehensive toolkit for gene expression in S. cerevisiae, only a few successful cases of bacteriocin expression have been reported. Since starch-to-ethanol fermentation is a key application for recombinant AMPs, this review explores strategies to optimize the expression of bacteriocin-encoding genes in S. cerevisiae. The ideal scenario would be a single yeast strain capable of producing amylases for starch hydrolysis, fermenting glucose to ethanol, and expressing bacteriocins to inhibit LAB contaminants. One-sentence summary: Yeast strains can produce heterologous antimicrobial peptides that help prevent contaminating bacteria from interfering with the starch-to-ethanol fermentation process.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13109847/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147662449","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Genome-guided discovery of clavaic acid, a decalin-containing polyketide encoded by a LovB-like polyketide synthase.","authors":"Yu Ping, Zainab Batool, Zhen Fan, Shaonan Liu, Anirudh Lahiri, Zixuan Pang, Yang Hai","doi":"10.1093/jimb/kuag022","DOIUrl":"10.1093/jimb/kuag022","url":null,"abstract":"<p><p>Fungal iterative type I polyketide synthases (iPKSs) generate structurally diverse natural products. A subset of these assembly line enzymes, exemplified by LovB from Aspergillus terreus, contains a C-terminal condensation domain bearing a noncanonical HRxxxDG motif. While these LovB-like iPKSs are widely distributed in fungi, the majority remain uncharacterized, leaving both their associated polyketide products and the function of their unusual condensation domains largely unexplored. Here, we report the characterization of a LovB-like iPKS from Aspergillus clavatus. Heterologous reconstitution of this PKS system in Aspergillus nidulans led to the discovery of clavaic acid, a previously undescribed polyketide featuring a trimethylated trans-decalin core and an all-E-configured carboxytriene side chain. Functional analysis of the condensation domain in vivo demonstrated that it is essential for clavaic acid biosynthesis. Surprisingly, whereas the conserved arginine residue within the HRxxxDG motif was dispensable for product formation, the conserved aspartate residue was strictly required. These findings expand our understanding of LovB-like iPKSs and establish this enzyme family as a promising source of cryptic fungal polyketides. One-sentence summary Genome-guided discovery of a trans-decalin-containing polyketide encoded by a LovB-like polyketide synthase in Aspergillus clavatus.</p>","PeriodicalId":16092,"journal":{"name":"Journal of Industrial Microbiology & Biotechnology","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13492342/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148706822","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}