Microbial Cell Factories最新文献

{"title":"Cis,cis-muconic acid production from lignin related molecules byAcinetobacter baylyi ADP1.","authors":"Changshuo Liu, Vilja Juvonen, Ella Meriläinen, Elena Efimova, Jin Luo, Milla Salmela, Suvi Santala, Ville Santala","doi":"10.1186/s12934-025-02780-3","DOIUrl":"10.1186/s12934-025-02780-3","url":null,"abstract":"","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"150"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12220188/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"De novo biosynthesis of taxifolin in yeast peroxisomes.","authors":"Qi Wu, Ruibing Chen, Lei Zhang","doi":"10.1186/s12934-025-02773-2","DOIUrl":"10.1186/s12934-025-02773-2","url":null,"abstract":"<p><strong>Background: </strong>Yeast peroxisomes have been engineered as ideal synthetic compartments to enhance the heterologous biosynthesis of natural products, particularly terpenoids and fatty acid derivatives. This advantage is primarily attributed to the rich acetyl-CoA pool generated from the spatially specific fatty acid β-oxidation within peroxisomes. However, their potential for flavonoid biosynthesis has been largely underexplored, primarily due to limited knowledge regarding precursor transport, cofactor availability, and the redox environment in peroxisomes.</p><p><strong>Results: </strong>In this study, we successfully compartmentalized the biosynthesis of taxifolin, a dihydroflavonol, in Saccharomyces cerevisiae peroxisomes. The result indicated that flavonoid biosynthesis in peroxisome offers a more efficient approach compared to its synthesis in the cytosol. This study managed to expand the application scope of peroxisome compartmentalization to flavonoid biosynthesis. By reinforcing the rate-limiting steps, optimizing cofactor supply and activation of fatty acids, we accomplished the de novo synthesis of taxifolin in peroxisomes for the first time, attaining a titer of 120.3 ± 2.4 mg/L in shake-flask fermentation using a minimal medium.</p><p><strong>Conclusion: </strong>These findings highlight the feasibility of peroxisomal compartmentalization for flavonoid biosynthesis, providing new insights and a framework for the biosynthesis of other high-value flavonoids using yeast peroxisomes.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"153"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12220111/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553901","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel function of ribosomal protein RPL14B: regulation of CdSe quantum dots biosynthesis in living Saccharomyces cerevisiae cells.","authors":"Jiye Liu, Yong Li, Jiawei Tu, Daiwen Pang, Lipeng Zhong, Zhixiong Xie","doi":"10.1186/s12934-025-02777-y","DOIUrl":"10.1186/s12934-025-02777-y","url":null,"abstract":"<p><p>Biosynthesis of CdSe quantum dots is the process of converting metal ions into semiconductor nanomaterials. Studies have shown that CdSe quantum dots synthesized by Saccharomyces cerevisiae are rich in ribosomal proteins, but the role of ribosomal proteins in the synthesis of CdSe quantum dots remains unclear. In this paper, ribosomal proteins enriched during the synthesis of CdSe quantum dots by S. cerevisiae were screened, and their effects on the synthesis of quantum dots were detected by gene knockout and over-expression. The results reveal that ribosomal protein RPL14B is involved in the synthesis of quantum dots. RPL14B binds cadmium ions during the nucleation of CdSe quantum dots and acts as a template, ultimately regulating the particle size of CdSe quantum dots by change the incubation time of CdCl₂. In summary, this study elucidates the mechanism of ribosomal protein RPL14B regulation of CdSe quantum dot biosynthesis, laying a foundation for the precise regulation of CdSe quantum dot synthesis.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"152"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12220401/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553903","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"CRISPR-driven enhanced hydrocarbon emulsification in an environmental Pseudomonas aeruginosa strain.","authors":"Luis M Salazar-García, Luis C Damas-Ramos, Luisa M Trejo-Alarcón, Daniela Rago, Linda Ahonen, Pablo Cruz-Morales, Patricia Ponce-Noyola, Cuauhtémoc Licona-Cassani","doi":"10.1186/s12934-025-02769-y","DOIUrl":"10.1186/s12934-025-02769-y","url":null,"abstract":"<p><strong>Background: </strong>Oil spills are a major concern due to the economic impact and severe effects on the ecosystem. To mitigate oil spills, hydrocarbon dispersion through emulsification is a promising approach, as it makes oil more susceptible to degradation by microorganisms. Environmental strains of Pseudomonas aeruginosa have demonstrated significant potential for producing rhamnolipids (RMLs) and pyocyanin (PYO), secondary metabolites associated to hydrocarbon emulsification. In this study, we isolated and characterized an environmental strain from an oil-contaminated site in the Gulf of Mexico. Upon genome sequencing and taxonomic classification, we developed genetic engineering tools and assessed their capacity to produce PYO and RMLs, molecules relevant for hydrocarbon emulsification.</p><p><strong>Results: </strong>Using the CRISPR/Cas9-APOBEC1-UGI system, we generated a targeted cytosine to thymine transition in the rpoS gene to generate a premature STOP codon. The resulting mutant exhibited increased production of PYO and RMLs, along with enhanced gasoline emulsification in cell-free supernatants, demonstrating successful modulation of a key regulatory gene. While the strain IGLPR01 retains certain virulence-associated features, this study contributes to the exploration of environmental isolates as future candidate chassis for biosurfactant production, emphasizing the need for further safety evaluation and rational attenuation strategies.</p><p><strong>Conclusion: </strong>This study provides a successful example of implementing CRISPR-based editing in an environmental P. aeruginosa strain. Despite the technical challenges, a genetic editing system was established and validated through a proof of concept to increase production of relevant metabolites. Our work demonstrates the applicability of genetic engineering tools in non-model environmental isolates, facilitating further developments. Importantly, the presence of virulence-associated features highlights the need for in-depth evaluation of pathogenicity and containment strategies before considering any future biotechnological applications.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"151"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12219457/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553900","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Efficient biodegradation and detoxification of reactive black 5 using a newly constructed bacterial consortium.","authors":"Manar K Abd Elnabi, Mohamed A Ghazy, Sameh S Ali, Marwa Eltarahony, Amr Nassrallah","doi":"10.1186/s12934-025-02768-z","DOIUrl":"10.1186/s12934-025-02768-z","url":null,"abstract":"<p><p>The release of azo dyes into wastewater from textile industries poses a significant environmental challenge due to their toxicity and recalcitrance. Among these dyes, Reactive Black 5 (RB5) is one of the most widely used and environmentally persistent due to its complex aromatic structure, high stability, and extensive use in the textile sector. This study aimed to develop and optimize a highly efficient bacterial consortium for the decolorization and detoxification of RB5. Three bacterial species-Bacillus cereus, Proteus mirabilis, and Stenotrophomonas maltophilia-were isolated from industrial effluents and combined into a consortium based on compatibility testing. The optimization of cultural and incubation conditions using Plackett-Burman Design (PBD) and Central Composite Design (CCD) significantly enhanced RB5 decolorization efficiency, reaching 98.56% under static conditions. Enzymatic analysis revealed the crucial role of NADH-DCIP reductase and azoreductase in azo bond cleavage, while oxidative enzymes facilitated further degradation into non-toxic metabolites. Metabolite characterization using UV-Vis, FTIR, and GC-MS confirmed the breakdown of RB5 into intermediate compounds with reduced toxicity. Toxicity assessments demonstrated a 66.38-21.38% reduction in root growth inhibition, an increase in germination rate from 40 to 93.33%, a decrease in Artemia salina mortality from 86.7 to 23.3%, and a reduction in cytotoxicity from 55.31 to 14.45% in human breast epithelial cells. These findings demonstrate the potential of the developed consortium as an eco-friendly, cost-effective solution for RB5-contaminated wastewater. Future studies should focus on pilot-scale implementation, long-term stability under variable effluent conditions, and regulatory compliance for industrial deployment.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"154"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12218093/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protease production by Serratia liquefaciens NRC1 using fish gut waste as a sustainable approach to antimicrobial peptide generation and combating Candida auris acquired resistance.","authors":"Shaymaa A Ismail, Heba M Shalaby, Amira A Hassan, Marwa Mahmoud, Bahgat Fayed","doi":"10.1186/s12934-025-02767-0","DOIUrl":"10.1186/s12934-025-02767-0","url":null,"abstract":"<p><strong>Background: </strong>The global rise of antimicrobial resistance has accelerated the search for sustainable and eco-friendly therapeutic alternatives. This study evaluates fish gut waste (FGW) as a low-cost, renewable substrate for producing antifungal peptides through the proteolytic activity of Serratia liquefaciens NRC1.</p><p><strong>Result: </strong>Optimization of protease production using statistical designs resulted in a fourfold increase in enzyme yield. The protease demonstrated stability at neutral pH and moderate temperatures (40-50 °C), and efficiently hydrolyzed complex proteins such as collagen and keratin. Peptides generated from FGW hydrolysis exhibited significant antifungal activity against Candida auris (C. auris), with a MIC₅₀ of 5.1 ± 0.08 mg/ml. Unlike fluconazole, repeated peptide exposure did not induce resistance, nor did it alter the expression levels of key resistance genes (CDR1, ERG11), as confirmed by qRT-PCR. Peptide profiling using MALDI-TOF/MS, coupled with in silico analysis via AMPfun, identified multiple candidates with predicted antifungal properties.</p><p><strong>Conclusion: </strong>This research highlights the potential of fish gut waste-derived peptides as a sustainable and effective antifungal strategy against C. auris, offering an alternative to conventional antifungal drugs.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"155"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12220321/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553904","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sortase-mediated surface display of a chimeric immunogen on Bacillus subtilis: a chicken necrotic enteritis vaccine candidate.","authors":"Bassima Al-Aneed, Hoang Duc Nguyen, Ali Akbar Masoudi, Saghi Nooraei, Abbas Hajizade, Hossein Tarrahimofrad, Gholamreza Ahmadian, Jamshid Razmyar, Moeen Khatami","doi":"10.1186/s12934-025-02762-5","DOIUrl":"10.1186/s12934-025-02762-5","url":null,"abstract":"<p><p>The application of sortase-mediated surface display technology on Bacillus subtilis represents a novel approach in protein engineering. We developed and evaluated a recombinant chimeric protein (R-anz) integrating truncated forms of three Clostridium perfringens toxins (CPA, NetB, ZMP) displayed on B. subtilis. Bioinformatics analyses using docking demonstrated that the 3D structure of R-anz chimeric protein has the potential to interact with chicken Toll-like receptor 21 (TLR21). Successful expression of the chimeric antigen was confirmed through SDS-PAGE and Western blotting, revealing a 78 kDa band in lysozyme-treated, xylose-induced samples. Oral immunization of chickens with this live bacterial vaccine significantly elevated IgY antibody levels, as assessed by ELISA. Cytokine profiling demonstrated a robust immune response, with marked upregulation of IFN-γ, IL-4, IL-17, and IL-22. Post-challenge with virulent C. perfringens strains, immunized chickens exhibited significantly reduced intestinal lesion scores, indicating partial protection. This study highlights the dual activation of humoral and cellular immune pathways, evidenced by elevated IgY levels and enhanced cytokine responses, particularly IFN-γ, IL-4, and IL-22. While the results demonstrate the potential of the R-anz chimeric protein to mitigate necrotic enteritis (NE), further research is essential to refine its efficacy, explore commercial feasibility, and address industry-specific challenges. This work paves the way for advancing NE vaccines using innovative sortase-mediated surface display technology, offering a promising strategy for sustainable poultry health management.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"147"},"PeriodicalIF":4.3,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12210746/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144540901","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Construction and evaluation of recombinant Lactobacillus plantarum expressing Micropterus salmoides hepcidin.","authors":"Cheng-Long Zhang, Guangtao Chen, Xiang Shan Ji, Jian Teng, Zhi Lei Yao, Chun Lei Hu, Yan Zhao","doi":"10.1186/s12934-025-02778-x","DOIUrl":"10.1186/s12934-025-02778-x","url":null,"abstract":"<p><strong>Background: </strong>Hepcidin is an antimicrobial peptide involved in innate immunity, and the addition of hepcidin or probiotics expressing hepcidin to feed can significantly enhance the disease resistance of farmed animals. Lactobacillus plantarum has the advantages of stable colonization in the animal gut, promotion of intestinal health, and efficient expression of foreign proteins. Previously, we have used L. plantarum (LP37) as a feed additive to promote the growth of Micropterus salmoides and Oreochromis mossambicus. The aim of this study is to construct a recombinant LP37 expressing hepcidin and evaluate its role in improving antibacterial ability and growth promotion in M. salmoides.</p><p><strong>Results: </strong>Based on the expression vector pSIP403, we used green fluorescent protein (GFP) as a reporter gene to compare the effects of four promoters on the expression levels of foreign proteins and selected the promoter TUFA with the highest expression level. By introducing the ribosomal binding site (RBS) and secretory signal peptide sequence (SP-PGH), we constructed a novel vector capable of efficiently expressing M. salmoides hepcidin (MsHep) extracellularly. Transformation of the novel vector into LP37 to obtain the recombinant strain: LP37-MsHep. This recombinant LP37-MsHep demonstrated considerable antibacterial activity against Aeromonas hydrophila and several other microbes. The dietary supplementation of recombinant LP37-MsHep for 60 days significantly enhanced the survival rates of M. salmoides and reduced tissue bacterial load in M. salmoides post infection with A. hydrophila, and regulated gene expression of FPN1, IL-10, TNF- <math><mi>α</mi></math> , and MHC-II involved in iron metabolism and immunity. Similar to LP37, dietary supplementation of recombinant LP37-MsHep also significantly improved the final body weight (FBW), weight gain ratio (WGR), and specific growth rate (SGR) and reduced the feed coefficient rate (FCR).</p><p><strong>Conclusions: </strong>Collectively, the recombinant LP37-MsHep is capable of significantly improving growth performance and disease resistance of M. salmoides, presenting it as a promising green feed additive in aquaculture with broad application potential.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"148"},"PeriodicalIF":4.3,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12211718/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144540900","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Harnessing magnetic cross-linked cell aggregates (CLCAs) for cost-effective preparation of Konjac mannan-oligosaccharide.","authors":"Baoyu Cui, Haiqiang Lu, Xue Liu, Yiran Zhang, Xinxi Gu","doi":"10.1186/s12934-025-02770-5","DOIUrl":"10.1186/s12934-025-02770-5","url":null,"abstract":"<p><p>Konjac mannan oligosaccharides (KMOS) are currently popular in food additives for their health benefits. However, the simple and efficient preparation of KMOS is still a challenge. In this study, A novel gene encoding β-mannanase (CsMan134) from Cellvibrio sp. KY-GH-1 was displayed on the surface of E. coli cells. Subsequently, E.coli cells (3 g/L) expressing the mannanase CsMan134 were immobilized using 8% (w/v) polyvinyl alcohol, 3% (w/v) sodium alginate, and 3.5% (w/v) Fe₃O₄ to construct magnetic cross-linked cell aggregates (mag-CLCAs). The mannanase CsMan134 demonstrated the highest catalytic efficiency towards konjac mannan compared to other mannans. Compared to free enzyme, the mag-CLCAs exhibited enhanced enzymatic activity across a range of temperatures and pH levels. Furthermore, the mag-CLCAs showed improved thermal stability, retaining over 80% of its initial activity after heating at 50 °C for 180 min, whereas the free enzyme retained only 50% of its residual activity. Scanning electron microscopy (SEM) and vibrating sample magnetometry (VSM) analyses indicated that the mag-CLCAs also maintained good operational stability, retaining more than 75% of their initial activity over five cycles. The mag-CLCAs were effective in converting konjac mannan into a substantial amount of oligosaccharides with a degree of polymerization (DP) of 2-4. In conclusion, the mag-CLCAs represent a valuable, efficient, and cost-effective biocatalyst for the production of KMOS for industrial applications.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"146"},"PeriodicalIF":4.3,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12186349/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144476018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production, purification, and characterization of a thermally stable, Acidophilic Cellulase from Aspergillus awamori AFE1 isolated from Longhorn beetle (Cerambycidae latreille).","authors":"Ayoola E Afe, Olusola T Lawal, Olufemi S Bamidele, Farhad Badshah, Bukola R Oyelere, Andrew N Efomah, Mostafa A Abdel-Maksoud, Sabiha Fatima, Abdulaziz Alamri, Mohamed A El-Tayeb, David M Sanni","doi":"10.1186/s12934-025-02755-4","DOIUrl":"10.1186/s12934-025-02755-4","url":null,"abstract":"<p><strong>Background: </strong>The relentless pursuit of cost-effective cellulase, a key enzyme in the biocatalytic conversion of cellulose, has led to exploring insect guts as potential sources of biocatalysts. Herbivorous insects' intestinal tracts are recognized as rich reservoirs of cellulolytic microorganisms. This study investigates cellulase production, purification, and characterization from Aspergillus awamori AFE1, isolated from the gut of longhorn beetles (Cerambycidae latreille). Basic cellulase production parameters were optimized. The cellulase produced under optimum conditions was purified by ammonium sulphate precipitation and chromatographic methods, followed by characterization of the purified enzyme.</p><p><strong>Results: </strong>Optimum cellulase production was observed at pH 5 and 30 °C, using cellulose and NaNO₃ as carbon and nitrogen sources. Cellulase was purified to homogeneity, with a molecular weight of 48.5 kDa. The cellulase exhibited optimal activity at pH 5.0 and maintained stability at an acidic pH of 4.0, showing 80% activity after 2 h and 40% activity remaining after 6 h. The optimal temperature for cellulase activity was 60 °C, with maximal stability at 30 °C, retaining 63% of its initial activity after 2 h. However, significant activity of 50% was noted at 50 °C for 2 h. Interestingly, the enzyme showed great stability against organic solvents up to 4 h and retained significant enzymatic activity after 5 h. Cellulase activity was also enhanced by divalent metal ions, Fe²⁺ and Zn²⁺, but was markedly inhibited by urea and EDTA, and monovalent Na⁺, K⁺, including some divalent metal ions, Cu²⁺ and Mn²⁺. It displayed K_m and V_max values of 3.86 mM and 0.3159 mg/mL/min, respectively.</p><p><strong>Conclusion: </strong>This study has shown Aspergillus awamori AFE1, isolated from the Longhorn beetle gut, as a unique source of acid-stable, thermostable, and organic solvent-resistant cellulase with industrial potential. Its unique enzymatic properties offer promising applications in biofuel production and lignocellulosic biomass conversion.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"145"},"PeriodicalIF":4.3,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12186396/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144476020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}