Biotechnology for Biofuels最新文献

{"title":"Machine learning-guided dual optimization of the substrate specificity and thermostability of yeast alcohol dehydrogenase","authors":"Yuki Ogawa,&nbsp;Akihiko Kondo,&nbsp;Tomokazu Shirai","doi":"10.1186/s13068-026-02839-2","DOIUrl":"10.1186/s13068-026-02839-2","url":null,"abstract":"<div><h3>Background</h3><p>Yeast alcohol dehydrogenase I (YADH) catalyzes the reversible reduction of aldehydes to primary alcohols. Thermostable YADH variants with broad substrate specificities at elevated temperatures are desirable for industrial biocatalysis. In this study, we aimed to alter the substrate specificity of YADH to efficiently catalyze the reduction of the non-native substrate, <i>trans</i>-2-nonenal, to <i>trans</i>-2-nonenol, while simultaneously enhancing thermostability. Residues around the substrate-binding site were identified by docking simulation and subjected to saturation and random mutagenesis. Measured activity and thermostability were used to train a machine-learning model to predict YADH variants with improved activity while maintaining thermostability.</p><h3>Results</h3><p>The machine learning-guided approach identified variants with improved properties. Four variants showed increased specific activity toward <i>trans</i>-2-nonenal compared with the wild type, and one variant also exhibited improved thermostability. The best-performing variant showed a more than twofold increase in specific activity along with retained thermal resistance. Variants that lost activity toward the native substrate acetaldehyde while gaining higher activity toward <i>trans</i>-2-nonenal were also obtained, indicating altered substrate specificity. These results demonstrate efficient identification of beneficial mutations from a limited dataset.</p><h3>Conclusions</h3><p>Overall, this study presents a machine learning–guided framework that integrates docking and multi-model evaluation for simultaneously optimizing substrate specificity and thermostability in YADH.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13729590/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149328549","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparison of synthetic and post-synthetic molecular genetic methods of reducing xylan glucuronidation in hybrid aspen for biorefinery applications","authors":"Pramod Sivan,&nbsp;János Urbancsok,&nbsp;Madhavi L. Gandla,&nbsp;Evgeniy N. Donev,&nbsp;Marta Derba-Maceluch,&nbsp;Melissa Roach,&nbsp;Leif J. Jönsson,&nbsp;Francisco Vilaplana,&nbsp;Ewa J. Mellerowicz","doi":"10.1186/s13068-026-02830-x","DOIUrl":"10.1186/s13068-026-02830-x","url":null,"abstract":"<div><h3>Background</h3><p>The pattern of xylan backbone substitution by 4-<i>O</i>-methylglucuronic acid (mGlcA) and <i>O</i>-acetyl groups generated during biosynthesis in the Golgi apparatus plays a key role in molecular interactions between secondary cell wall polymers in hardwoods, thus regulating biorefinery properties of woody biomass. This study aims at comparing the effects of two different approaches to reduce xylan glucuronidation, targeting either xylan biosynthesis by RNAi suppression of <i>GLUCURONIC SUBSTITUTION OF XYLAN1</i> genes (denoted Gux1RNAi) or by xylan post-synthetic modification in the secondary cell wall by apoplastic wood-specific expression of a fungal α-glucuronidase from family GH67 (denoted WP:GH67) in hybrid aspen (Populus tremula L. x tremuloides Michx.). The effects of reducing xylan glucuronidation by these two approaches on xylan acetylation and solubility, and recalcitrance of wood to enzymatic hydrolysis were compared.</p><h3>Results</h3><p>Both approaches reduced mGlcA/xylose (Xyl) ratio by approx. 30% without altering Xyl content in alkali extracts, while xylan acetyl content in subcritical water extracts was increased only in Gux1RNAi lines. The Gux1RNAi lines showed reduced glucuronidation in the major xylan domain containing evenly-spaced mGlcA, whereas the WP:GH67 lines were affected in both odd and even glucuronidation patterns. Interestingly, the arrays containing mGlcA every second xylosyl unit were not affected by any modification, whereas an increase in xylo-oligosaccharides containing <i>O</i>-2,3 diacetylated Xyl was found in Gux1RNAi lines only. Neither modification consistently affected glucose or Xyl yields in saccharification without or with acid pretreatment, whereas xylan extractability in subcritical water was increased in Gux1RNAi, but not in WP:GH67 lines.</p><h3>Conclusion</h3><p>Our study supports the hypothesis that acetylation competes with glucuronidation by GUX1 during biosynthesis, and increased acetylation caused by <i>GUX1</i> suppression rather than reduced xylan glucuronidation per se improves xylan extractability. The 30% reduction in glucuronidation did not affect enzymatic saccharification, supporting the concept that cell wall structure and recalcitrance in transgenic lines are maintained by xylan domains which were not affected by either transgenic modification.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s13068-026-02830-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149189811","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Metabolic engineering strategies for sustainable de novo isobutylamine production by Corynebacterium glutamicum","authors":"Tim Prasun,&nbsp;Susanne Müller,&nbsp;Fynn Stegelmann,&nbsp;Bastian Blombach,&nbsp;Volker F. Wendisch","doi":"10.1186/s13068-026-02831-w","DOIUrl":"10.1186/s13068-026-02831-w","url":null,"abstract":"<div><h3>Background</h3><p>Short-chain primary amines are a versatile group of molecules in biological systems, derived from the decarboxylation of amino acids or the transamination of carbonyl-containing molecules. Isobutylamine, the decarboxylation product of <span>l-</span>valine, has applications in chemical synthesis of pharmaceuticals, herbicides, fungicides and specialized chemicals, where it is especially interesting as a substitute for petrochemical compounds. Since the chemical synthesis of short-chain primary amines is hazardous and environmentally unsustainable, we established an efficient biosynthetic approach in this work.</p><h3>Results</h3><p>The natural amino acid producer <i>Corynebacterium glutamicum</i> is an ideal chassis for the production of amino acid-derived molecules. In this study, we assessed the toxicity of several relevant short-chain primary amines on <i>C. glutamicum</i>. A crude extract assay demonstrated the decarboxylation of <span>l-</span>valine to isobutylamine by the <span>l-</span>valine decarboxylase VlmD_Sv from <i>Streptomyces viridifaciens</i>. This enzyme was instrumental to extend production of pyruvate in three engineered strains to yield <span>l-</span>valine and subsequently isobutylamine. To ensure intracellular <span>l-</span>valine supply, the extracellular <span>l-</span>valine accumulation was decreased up to 20-fold by deletion of the genes for the branched-chain amino acid exporter BrnFE_Cg and/or overexpression of the <span>l-</span>valine importer gene <i>brnQ</i>_<i>Cg</i>. Surprisingly, expression of the transhydrogenase genes <i>pntAB</i>_<i>Ec</i> from <i>Escherichia coli</i> did not improve but drastically reduced isobutylamine production. Biochemical analysis revealed that <i>pntAB</i>_<i>Ec</i> expression depolarized the membrane potential.</p><h3>Conclusions</h3><p>This study demonstrated the highest production of isobutylamine and the highest production of any microbial short-chain primary amine in minimal medium. In shake flask cultivation, an isobutylamine titer of 12.1 g/L and a yield of 0.74 mol isobutylamine/mol glucose were obtained. Transfer to a 3 L fed-batch bioreactor fermentation was successful and a titer of 33.2 g/L was reached within 64 h with a yield of 0.47 mol/mol and a volumetric productivity of 0.52 g/l/h. Moreover, isobutylamine production on a second-generation feedstock was shown, highlighting the potential of sustainable bio-based production of isobutylamine.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13654226/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149171735","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Harnessing shrimp shell waste: enhanced chitinase production through optimization techniques for ecofriendly solutions using bacteria","authors":"Basma T. Abd-Elhalim,&nbsp;Mona A. Ashour","doi":"10.1186/s13068-026-02808-9","DOIUrl":"10.1186/s13068-026-02808-9","url":null,"abstract":"<div><p>Chitinous wastes, particularly shrimp shell residues, represent a major underutilized biomass resource with significant potential for bioconversion into high-value products. In this study, four thermophilic bacterial strains (<i>Bacillus amyloliquefaciens</i> BT 2022, <i>Bacillus licheniformis</i> Basma87, <i>Priestia megaterium</i> AMD 2024, and <i>Streptomyces maritimus</i> MSQ-2021) were screened for their ability to produce chitinase using shrimp shell waste (SSW) as the sole carbon and nitrogen source. Among these, <i>P. megaterium</i> AMD 2024 exhibited the highest chitinolytic activity. Optimization of fermentation parameters was initially performed using the one-variable-at-a-time (OVAT) approach, identifying 5% SSW, 60° C, 72 h incubation, pH 7.0, 200 rpm shaking, and 2% inoculum size as optimal conditions, yielding 93.24 U/mL chitinase activity. Subsequent statistical optimization using response surface methodology (RSM) with Plackett–Burman design (PBD) and central composite design (CCD) significantly enhanced enzyme production, achieving maximum activity of 273.3 U/mL, representing a 2.93-fold increase compared to OVAT. Partial purification via ammonium sulphate saturation (60–80%) resulted in 260.0 U/mL activity with 95.13% relative activity. Cytotoxicity assays using normal human skin cell line HFB4 confirmed the biocompatibility of the purified enzyme at concentrations up to 260.0 U/mL. These findings demonstrate that shrimp shell waste can be efficiently valorized into chitinase through microbial fermentation, providing an eco-friendly solution for waste management and offering safe, sustainable applications in agriculture, industry, and cosmetics.</p><h3>Graphical Abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13595610/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149027159","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anaerobic mono-digestion of wheat straw in a three-stage semi-continuous system inspired by a beetle larva gut","authors":"Bruna G. Schroeder,&nbsp;Rita Bhattacherjee,&nbsp;Maria L. Bonatelli,&nbsp;Ulisses N. da Rocha,&nbsp;Heike Sträuber,&nbsp;Hauke Harms,&nbsp;Marcell Nikolausz","doi":"10.1186/s13068-026-02819-6","DOIUrl":"10.1186/s13068-026-02819-6","url":null,"abstract":"<div><p>Based on the efficient digestive system of the larva of the sun beetle (<i>Pachnoda marginata</i>) in utilizing lignocellulose-rich biomass, a reactor system was designed to partially mimic processes that occur in the larval gut. We aimed developing a process with this system for anaerobic mono-digestion of wheat straw to produce volatile fatty acids (VFAs) and biogas. Three stirred tank reactors connected in series were customized with polyurethane foam and operated at 37 °C. The first two reactors were designed to mimic the midgut of the larva with enhanced VFA production and the third one to resemble the hindgut and optimized for methanogenesis. The system was fed in a semi-continuous regime with ground wheat straw in an alkaline medium. Enrichment cultures from midgut and hindgut of the larva were used as inocula and three conditions with increasing organic loading rate were tested. The highest biomass to methane conversion occurred at the lowest organic loading rate and highest retention time, when a methane yield of 148 mL_Norm g⁻¹_VS was obtained and VS degradation reached 44%. The microbial community was enriched toward cellulose and hemicellulose degrading taxa, including Dysgonomonadaceae, Lachnospiraceae, Marinilabiliaceae and Ruminococcaceae. The methanogenic community shifted from predominance of <i>Methanosarcina</i> to <i>Methanobacterium</i> and <i>Methanoculleus</i>. A comparison with other studies investigating straw utilizing bioreactors confirmed that a core microbiome composed of the phyla Firmicutes, Bacteroidetes and Proteobacteria effectuates the anaerobic digestion of lignocellulose-rich materials, regardless of the source of the inoculum and the process conditions. The designed process was stable and capable to convert wheat straw into methane and carboxylates. Further adaptations are suggested to improve the anaerobic digestion and decrease assembly and operating costs.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s13068-026-02819-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148927733","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biocatalytic upgrading of fusel oil from bioethanol production to levulinate esters as renewable fuel oxygenates","authors":"Yuchen Luo,&nbsp;Mohamed Ismail,&nbsp;Rajni Hatti-Kaul,&nbsp;Sang-Hyun Pyo","doi":"10.1186/s13068-026-02816-9","DOIUrl":"10.1186/s13068-026-02816-9","url":null,"abstract":"<div><h3>Background</h3><p>The transition toward a sustainable bioeconomy requires efficient strategies for converting renewable biomass and industrial side streams into value-added chemicals and fuels. Fusel oil is an important coproduct of bioethanol fermentation and levulinic acid (LA), a key platform molecule derived from lignocellulosic biomass, can be upgraded into alkyl levulinates, which are promising green solvents, specialty chemicals, and fuel-related applications.</p><h3>Results</h3><p>In this study, a solvent-free enzymatic approach was developed for the synthesis of alkyl levulinates via lipase-catalyzed esterification of levulinic acid with bioethanol-derived fusel oil and its major alcohol components, including 2-methyl-1-butanol and 3-methyl-1-butanol, using immobilized <i>Candida antarctica</i> lipase B (Novozym® 435). Under optimized conditions (50 °C, LA:alcohol molar ratio 1:10, enzyme loading 10 wt% and molecular sieve addition equal to substrate mass), quantitative levulinic acid conversion and levulinate yield (~ 98–99%) were achieved within 5 h. In comparison, the secondary alcohol 2-butanol, evaluated for mechanistic comparison, reached a lower conversion (~ 70%) under otherwise identical conditions, consistent with its greater steric hindrance within the enzyme active site. Molecular docking simulations supported experimental observations by elucidating substrate–enzyme interactions and differences in binding affinity. The immobilized enzyme exhibited excellent operational stability, maintaining over 97% LA conversion over five consecutive cycles, and successful operation at 100 mL in a bioreactor highlighted the potential for further scale-up. The solvent-free system reduces process complexity, facilitates downstream processing and enhances process sustainability.</p><h3>Conclusion</h3><p>Overall, this work demonstrates an efficient strategy for valorizing fusel oil side stream into high-value levulinate esters, contributing to circular bioeconomy approaches and the development of renewable fuel oxygenates and chemical platforms.</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13551973/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148914514","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Upcycling waste apples into platform chemicals: pilot-scale production of lactic and succinic acids","authors":"Laís Portugal Rios da Costa Pereira,&nbsp;Roland Schneider,&nbsp;Agata Olszewska-Widdrat,&nbsp;Barbara Sturm,&nbsp;Korbinian Kaetzl","doi":"10.1186/s13068-026-02807-w","DOIUrl":"10.1186/s13068-026-02807-w","url":null,"abstract":"<div><p>The conversion of renewable biological resources into value-added products is essential for supporting the transition to a sustainable bioeconomy. This study explores the use of waste apples—a by-product generated in large quantities along the fresh apple supply chain—as feedstock for the production of two industrially relevant platform chemicals: lactic acid (LA) and succinic acid (SA). A screening identified <i>Heyndrickxia coagulans</i> A203 and <i>Actinobacillus succinogenes</i> DSM 22257 as the most suitable strains for LA and SA production from apple mash, the sugar-rich fraction obtained by pressing waste apples (excluding the solid peel and seed residues). A simplified procedure, omitting costly centrifugation and sterilization steps between enzymatic liquefaction and fermentation, was successfully scaled up, resulting in 73.8 g L⁻¹ LA with a yield of 0.91 g g⁻¹ and 36.8 g L⁻¹ SA with a yield of 0.69 g g⁻¹. The results demonstrate the potential of waste apples as a low-cost, effective feedstock for the biotechnological production of high-value platform chemicals, contributing to the valorization of agri-food waste within a sustainable and circular bioeconomy.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13548481/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148908437","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Volatile fatty acids as sustainable feedstocks for tailored microbial lipid production","authors":"Marieke Willing,&nbsp;Max Schneider,&nbsp;Mariia Kornilova,&nbsp;Michel Weber,&nbsp;Dania Awad,&nbsp;Felix Melcher,&nbsp;Michael Paper,&nbsp;Marion Ringel,&nbsp;Daniel Garbe","doi":"10.1186/s13068-026-02814-x","DOIUrl":"10.1186/s13068-026-02814-x","url":null,"abstract":"<div><h3>Background</h3><p>Interest in single-cell oils from oleaginous yeasts is growing with respect to their potential as sustainable alternatives to plant- and fossil-based oils. The yeast <i>Cutaneotrichosporon oleaginosus</i> is a promising candidate for microbial lipid production due to its broad substrate range and high lipid accumulation capacity. Among potential feedstocks, volatile fatty acids (VFAs) derived from organic waste streams have attracted increasing attention as low-cost, sustainable carbon sources. These VFA mixtures typically contain C2–C6 volatile fatty acids, including acetic, propionic, butyric, valeric, isovaleric, and caproic acids. However, a systematic understanding of how individual VFAs affect growth, lipid accumulation, and fatty acid composition in <i>C. oleaginosus</i> is still lacking.</p><h3>Results</h3><p>This study investigates the effects of individual VFAs in fed-batch fermentations with <i>C. oleaginosus</i> ATCC 20509 under controlled, elemental carbon-equivalent conditions, using acetic, propionic, butyric, valeric, and caproic acid as well as the branched-chain acids 2-methylpropionic, 2-methylbutyric, and 3-methylbutyric acid. It was demonstrated that carbon chain length strongly influences these parameters, with growth and lipid production generally decreasing as chain length increases. The highest lipid titers were observed in acetic acid- and butyric acid-based fermentations. Even-chain VFAs primarily resulted in the synthesis of even-chain fatty acids. In contrast, odd-chain VFAs promoted the formation of odd-chain fatty acids, with propionic acid emerging as a particularly promising substrate for the targeted production of odd-chain fatty acids. Fermentations with branched VFAs revealed that growth and lipid accumulation are strongly reduced, potentially due to steric effects associated with methyl substituents. However, the presence of the methyl group did not significantly alter the overall fatty acid profile compared to unbranched carbon chains, as confirmed by NMR analysis.</p><h3>Conclusion</h3><p>These findings demonstrate that the choice of substrate has a major impact on targeted lipid production. By enabling the modulation of lipid composition and supporting efficient biomass and lipid accumulation, volatile fatty acids offer a high-value alternative to conventional carbon sources. Overall, these results highlight the potential of VFAs to contribute to a circular bioeconomy by converting low-value waste streams into valuable microbial oils.</p><h3>Graphical Abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s13068-026-02814-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148838212","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enzyme discovery and catalytic mechanism insights for mitigating inhibitory effects in tobacco lignocellulose biodegradation: advances, challenges, and perspectives","authors":"Yangyang Li,&nbsp;Chang Liu,&nbsp;Jianan Yan,&nbsp;Zhendong Li,&nbsp;Jian Chen,&nbsp;Jian Mao,&nbsp;Xueqin Lv,&nbsp;Long Liu","doi":"10.1186/s13068-026-02796-w","DOIUrl":"10.1186/s13068-026-02796-w","url":null,"abstract":"<div><p>Tobacco biomass constitutes a substantial yet underexploited lignocellulosic resource with considerable potential for bioconversion. However, its efficient enzymatic utilization is constrained by pronounced structural heterogeneity and the presence of diverse non-structural inhibitory components. This review provides a comprehensive overview of tobacco lignocellulose, emphasizing how tissue-specific variations in cellulose, hemicellulose, lignin, and other cell wall components influence enzyme accessibility and catalytic efficiency. Particular attention is given to tobacco-derived inhibitory compounds, including alkaloids, polyphenols, and pigments, which impair enzymatic hydrolysis through multiple mechanisms. Unlike previous reviews on lignocellulose hydrolysis, this review further summarizes recent advances in inhibitor transformation, enzyme engineering to enhance inhibitor tolerance and degradation activity, and enzymatic system optimization. Looking forward, the integration of advanced metagenomic screening and artificial intelligence-driven design is expected to accelerate the development of more robust lignocellulolytic enzymes with enhanced resistance to inhibitory compounds. Collectively, these insights provide a mechanistic basis for efficient and sustainable utilization of tobacco biomass.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s13068-026-02796-w.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149338871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Efficient preparation of fatty acid methyl esters using liquid lipase from thermotolerant fungus Rasamsonia emersonii via synergistic strategies","authors":"Jiang-Ke Yang,&nbsp;Ying Han,&nbsp;Lin-Jun Wei,&nbsp;De-Ming Rao,&nbsp;Lei Lei","doi":"10.1186/s13068-026-02801-2","DOIUrl":"10.1186/s13068-026-02801-2","url":null,"abstract":"<div><p>Lipase-catalyzed biodiesel preparation in non-aqueous media has the advantages of reduced energy consumption, simplified recovery of fatty acid methyl esters (FAMEs), and minimized environment pollution, etc. To discover a novel thermophilic lipase, achieve its high-level expression, and develop it as an efficient liquid biocatalyst for FAMEs production via methanolysis of plant oils in non-aqueous media, a lipase gene from the thermophilic fungus <i>Rasamsonia emersonii</i> was cloned and efficiently expressed through synergistic strategies including computational codon optimization and increased gene dosage in the host genome. The resulting liquid lipase preparation was directly employed as a biocatalyst for FAMEs production. Under optimized reaction conditions, a conversion rate of approximately 95% was achieved. This study provides a feasible approach for the large-scale production of thermophilic lipase. The strategy of directly using of liquid lipase as a biocatalyst for FAMEs preparation substantially simplifies enzyme immobilization, regeneration, and product recovery processes, offering an efficient alternative for enzymatic FAMEs production.</p></div>","PeriodicalId":494,"journal":{"name":"Biotechnology for Biofuels","volume":"19 1","pages":""},"PeriodicalIF":6.1,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13715122/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149290636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}