Microbial Cell Factories最新文献

{"title":"New Yarrowia lipolytica chassis strains for industrial enzyme production.","authors":"Djamila Onésime, Esteban Lebrun, Goran Stanajic Petrovic, Ewelina Celińska, Jean-Marc Nicaud","doi":"10.1186/s12934-025-02787-w","DOIUrl":"10.1186/s12934-025-02787-w","url":null,"abstract":"<p><strong>Background: </strong>Yarrowia lipolytica has emerged as a well-established platform for producing a wide range of biomolecules, including recombinant proteins (rProteins). Its robust metabolism and resistance to various environmental stressors make it particularly well-suited as a microbial cell factory. However, additional physiological modifications are still required to fully meet industrial demands. Over years of strain development, Y. lipolytica has been engineered to carry auxotrophic markers, streamline the secretory pathway via deletion of native secretory proteins, prevent filamentation, and enable inducible gene expression systems.</p><p><strong>Results: </strong>In this study, we continued the fine-tuning of Y. lipolytica as a platform for rProtein synthesis, building on previous work. Specifically, we: (i) introduced a third auxotrophy to facilitate more complex genetic engineering strategies, (ii) removed bacterial vector elements (including antibiotic resistance genes) from previous constructs, and (iii) carried out extensive deletions of extracellular proteases and a peroxidase gene. The newly constructed chassis strains, JMY9438 and JMY9451/9452, both bear triple auxotrophies. The latter strain additionally lacks proteolytic activity due to the deletion of five protease genes. We evaluated the rProtein production efficiency of these strains harboring one, two or three integrated copies of the target gene. rProtein expression levels increased with copy number up to two; however, no further improvement was observed with three copies. Notably, the strain with protease deletions and a single gene copy showed the highest rProtein production per cell, while the strain retaining proteases but harboring two copies yielded the highest absolute rProtein levels.</p><p><strong>Conclusions: </strong>We present a new generation of Y. lipolytica chassis strains specifically optimized for recombinant protein production. Our results demonstrate that extensive protease deletions can provide a high-performance genetic background, enabling high-level rProtein production without relying on multi-copy expression strategies.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"164"},"PeriodicalIF":4.3,"publicationDate":"2025-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12247380/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144608748","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":"Retraction Note: Isolation, expression, and in silico profiling of a thermostable xylanase from Geobacillus stearothermophilus strain NASA267: insights into structural features and agro-waste valorization.","authors":"Safaa M Ali, Nehad Noby, Nadia A Soliman, Sanaa H Omar","doi":"10.1186/s12934-025-02790-1","DOIUrl":"10.1186/s12934-025-02790-1","url":null,"abstract":"","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"161"},"PeriodicalIF":4.3,"publicationDate":"2025-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12243215/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144608749","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":"Study on the regulatory mechanism of NsdA_sr on rimocidin biosynthesis in Streptomyces rimosus M527.","authors":"Yawen Xie, Yujie Jiang, Yongyong Zhang, Andreas Bechthold, Xiaoping Yu, Zheng Ma","doi":"10.1186/s12934-025-02784-z","DOIUrl":"10.1186/s12934-025-02784-z","url":null,"abstract":"<p><strong>Background: </strong>We previously identified a regulator NsdA_sr, which negatively regulated rimocidin biosynthesis in Streptomyces rimosus M527. However, the exact regulatory mechanism of NsdA_sr on rimocidin production remains unknown.</p><p><strong>Results: </strong>In this study, firstly, transcriptomic data demonstrated that the differentially expressed genes resulting from the over-expression of nsdA_sr were primarily associated with several key metabolic pathways, including glycolysis, oxidative phosphorylation, and ribosome-related genes, all of which were downregulated. This directly impacted the concentrations of CoA and NADH, as confirmed by concentration measurement assays. Subsequently, the results of the ChIP-seq experiments revealed that NsdA_sr directly binds to 49 target genes. Notably, these include RS18275 and RS18290 (both involved in fatty acid degradation) as well as rpoB (related to DNA transcription). The validity of the ChIP-seq assay for these three genes was further supported by in vitro electrophoretic mobility shift assays. Regarding RS18275 and RS18290, the results revealed that the binding of NsdA_sr to these elements led to the downregulation of gene expression. This, in turn, resulted in a decrease in the levels of butyryl-CoA and malonyl-CoA, which are known precursors for rimocidin biosynthesis. Consequently, this negatively impacted on the biosynthesis of rimocidin. In the case of rpoB, the results indicated that NsdA_sr binding led to a downregulation of overall protein levels. This was determined by enzymatic activity of report gene GUS and Western blot assay. Consequently, this resulted in a decrease in rimocidin yield.</p><p><strong>Conclusion: </strong>This study reveals NsdA_sr's dual role in limiting rimocidin production by suppressing metabolic precursors and modulating protein expression. Integrated transcriptomic and ChIP-seq analyses provide critical insights into its regulatory mechanisms.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"162"},"PeriodicalIF":4.3,"publicationDate":"2025-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12243394/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144608750","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":"Development of an efficient heterologous protein expression platform in Aspergillus niger through genetic modification of a glucoamylase hyperproducing industrial strain.","authors":"Fufan Gou, Dandan Liu, Chaohui Gong, Kefen Wang, Xingji Wang, Yefu Chen, Qian Liu, Chaoguang Tian","doi":"10.1186/s12934-025-02786-x","DOIUrl":"10.1186/s12934-025-02786-x","url":null,"abstract":"<p><strong>Background: </strong>Aspergillus niger is widely used in industrial enzyme production due to its strong secretion capacity and the status of generally recognized as safe (GRAS). However, heterologous protein expression in A. niger is frequently constrained by high levels of background endogenous protein secretion, limited access to native high transcription loci, and limitations in the efficiency of the secretory machinery. To address these limitations, this study genetically engineered a chassis strain based on an industrial glucoamylase-producing A. niger strain AnN1 for constructing the improved heterologous protein expression.</p><p><strong>Results: </strong>In this study, by using CRISPR/Cas9-assisted marker recycling, we deleted 13 of the 20 copies of the heterologous glucoamylase TeGlaA gene and disrupted the major extracellular protease gene PepA, resulting in the low-background strain AnN2. Compared to the parental strain AnN1, AnN2 exhibited 61% less extracellular protein and significantly reduced glucoamylase activity, while retaining multiple transcriptionally active integration loci. Four diverse proteins were integrated into the high-expression loci originally occupied by the TeGlaA gene in the chassis AnN2. These recombinant protein included a homologous glucose oxidase (AnGoxM), a thermostable pectate lyase A (MtPlyA), a bacterial triose phosphate isomerase (TPI), and a medical protein Lingzhi-8 (LZ8). All target proteins were successfully expressed and secreted within 48-72 h, with yields ranging from 110.8 to 416.8 mg/L in 50 mL shake-flasks cultivation. The enzyme activities of AnGoxM, MtPlyA and TPI reached ~ 1276 - 1328 U/mL, ~ 1627. 43 - 2105.69 U/mL, and ~ 1751.02 to 1906.81 U/mg after 48 h, respectively. Additionally, Overexpression of Cvc2, a COPI vesicle trafficking component, further enhanced MtPlyA production by 18%, highlighting the benefit of combining transcriptional and secretory pathway engineering.</p><p><strong>Conclusions: </strong>Our results demonstrated that the chassis AnN2 served as a robust, modular, and time-efficient platform for heterologous protein expression in A. niger. Through site-specific integration of target genes into native high-expression loci and strategic modulation of the secretory pathway, we successfully enabled the rapid production of functional enzymes and bioactive proteins from diverse origins. This dual-level optimization strategy, which integrates rational genomic engineering with targeted enhancement of the secretory pathway, enabled high-yield expression while minimizing background interference. Together, these findings offer a practical framework for constructing versatile fungal expression systems and highlight the potential of combining genetic and cellular engineering to improve recombinant protein production in filamentous fungi.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"160"},"PeriodicalIF":4.3,"publicationDate":"2025-07-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12236015/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144591770","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":"Biological activities of optimized biosynthesized selenium nanoparticles using Proteus mirabilis PQ350419 alone or combined with chitosan and ampicillin against common multidrug-resistant bacteria.","authors":"Laila A Elshikiby, Zakaria A M Baka, Mohamed M El-Zahed","doi":"10.1186/s12934-025-02783-0","DOIUrl":"10.1186/s12934-025-02783-0","url":null,"abstract":"&lt;p&gt;&lt;strong&gt;Background: &lt;/strong&gt;One of the most common issues in the world is bacterial resistance and biofilms, which can prolong the healing period and the need for self-medication. Additionally, they may be linked to unsuccessful therapies, which raises death rates, healthcare expenses, and the need for additional hospitalization. Therefore, to protect the environment and improve human health, there is a need for the creative synthesis of novel antibacterial materials. Proteus mirabilis strain PQ350419 was isolated, identified, and utilized as an efficient bio-nano-factory for biosynthesizing selenium nanoparticles (Se NPs) and optimizing procedures. This study showcases a simple and cost-effective approach for green-synthesizing a selenium/chitosan/ampicillin nanocomposite (Se/CS/AMP) as a novel antibacterial and antibiofilm agent. Several analyses, such as transmission electron microscopy (TEM), X-ray diffraction (XRD), Fourier-transform infrared (FTIR) spectroscopy, zeta analysis, and ultraviolet-visible (UV-Vis) spectroscopy, were utilized to confirm and characterize the production of Se NPs and Se/CS/AMP. The absorption peaks for Se NPs and Se/CS/AMP were identified to be between 350 and 360 nm. The XRD data revealed the crystalline composition of the Se NPs loaded with CS and AMP. The FTIR spectra confirmed the presence of proteins that act as supporting and binding agents during synthesis. The stability of the prepared nanomaterials is improved by a strong negative surface charge of - 24.27 mV for Se NPs and - 23.92 mV for Se/CS/AMP. The particle sizes of Se NPs and Se/CS/AMP are shown by TEM to be in the ranges of 88-98 nm and 86-129 nm, respectively. Se NPs, either alone or in combination with chitosan (CS) and ampicillin (AMP), exhibited strong antibacterial activity against methicillin-resistant Staphylococcus aureus ATCC 43,300, Bacillus cereus ATCC 14,579, Klebsiella pneumoniae ATCC 11,296, and P. mirabilis PQ350419 in a dose-dependent manner. Compared to Se NPs and the common antibiotic AMP, the Se/CS/AMP combination demonstrated superior antibacterial activity. In comparison to Se NPs (40, 70, 110, and 150 µg/ml, respectively), the nanocomposite produced MIC values of 30, 40, 60, and 100 µg/ml against B. cereus, S. aureus, K. pneumoniae, and P. mirabilis. When compared to untreated cells, treated cells exhibited significant morphological changes and deformities, such as cell wall distortion, the separation of the cell wall from the plasma membrane, the formation of vacuoles, and complete cell lysis, according to TEM ultrastructure studies of bacteria treated with nanocomposite. Se/CS/AMP at 100 µg/ml was sufficient to prevent biofilm formation by up to 50% in S. aureus, K. pneumoniae, and P. mirabilis. The cell viability of the Vero cell line was significantly reduced (p˂0.05) in the cytotoxicity test of Se NPs alone at a concentration of 40.95 ± 2.34 µg/ml, and in its nanocomposite at a concentration of 199.09 ± 2.61 µg/ml. Thi","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"159"},"PeriodicalIF":4.3,"publicationDate":"2025-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12228243/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144567634","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":"Regulatory mechanism of Haa1p and Hap4p in Saccharomyces cerevisiae to mixed acetic acid and formic acid when fermenting mixed glucose and xylose.","authors":"Xin-Yu Xiao, Bo Li, Zi-Yuan Xia, Quan Zhang, Cai-Yun Xie, Yue-Qin Tang","doi":"10.1186/s12934-025-02764-3","DOIUrl":"10.1186/s12934-025-02764-3","url":null,"abstract":"<p><strong>Background: </strong>Acetic and formic acid are two common inhibitors that coexist with glucose and xylose in lignocellulosic hydrolysates, which impair the fermentation performance of Saccharomyces cerevisiae. Enhancing yeast tolerance to these inhibitors is crucial for efficient industrial bioethanol production. Previous transcriptomic studies have indicated the involvement of the transcription factors Haa1p and Hap4p in the cellular response to mixed acetic and formic acid stress. This study aimed to further elucidate their regulatory roles in conferring tolerance to this combined stress condition. Comparative transcriptomic analysis was conducted using the engineered strains s6H3 (HAA1-overexpressing) and s6P5 (HAP4-overexpressing), in comparison with the original strain s6.</p><p><strong>Results: </strong>Both HAA1 and HAP4 overexpression improved fermentation performance, both in the presence and absence of inhibitors. HAA1 overexpression led to a greater number of differentially expressed genes (DEGs) under mixed acid stress compared to non-inhibitory conditions. Genes involved in glycolysis, the pentose phosphate pathway (PPP), necroptosis, and ribosome biogenesis were significantly downregulated, whereas those associated with the glyoxylate cycle, nucleotide metabolism, and RNA polymerase activity were significantly upregulated. In contrast, HAP4 overexpression resulted in fewer DEGs under acid stress conditions, which may be attributed to the intrinsic induction of HAP4 in the original strain s6 under acid exposure. Under these conditions, genes related to metabolic regulation, RNA processing, and transcription were significantly downregulated, while those involved in transport, ribosome biogenesis, genome stability, and sporulation were significantly upregulated. Collectively, both Haa1p and Hap4p appear to regulate other transcription factors, thereby indirectly influencing global gene expression in response to mixed acetic and formic acid stress.</p><p><strong>Conclusions: </strong>This study provides the experimental evidence for the protective role of Haa1p and Hap4p under combined acetic and formic acid stress. Regulatory mechanisms underlying the responses of Haa1p and Hap4p to combined acid stress were identified, expanding current understanding of yeast stress adaptation.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"156"},"PeriodicalIF":4.3,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12231699/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564851","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":"Multiplex metabolic engineering of yeast for high-efficiency all-trans-retinoic acid production.","authors":"Wenhao Li, Dong Wang, Tingting Yang, Xiaochen Ma, Xueli Zhang, Zhubo Dai","doi":"10.1186/s12934-025-02782-1","DOIUrl":"10.1186/s12934-025-02782-1","url":null,"abstract":"","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"157"},"PeriodicalIF":4.3,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12226859/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564849","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":"Regulation of the tagatose catabolic gene cluster and development of a tagatose-inducible expression system in the probiotic Escherichia coli Nissle 1917.","authors":"Keunha Park, Youngshin Kim, Dohyeon Kim, Su Min Oh, Tae Jeong Koo, Seung Min Yoo, Sung Ho Yoon","doi":"10.1186/s12934-025-02771-4","DOIUrl":"10.1186/s12934-025-02771-4","url":null,"abstract":"<p><strong>Background: </strong>The probiotic Escherichia coli Nissle 1917 (EcN) is a promising microbial chassis for therapeutic and industrial applications. However, its broad utility is limited by a lack of reliable inducible gene expression systems that precisely control gene expression.</p><p><strong>Results: </strong>We developed a tagatose-inducible expression system in EcN using D-tagatose, a naturally occurring sugar with established safety in humans, as a metabolizable inducer. Through differential RNA sequencing and sequence analysis, we identified the key regulatory elements governing D-tagatose catabolism in EcN and demonstrated that the DeoR family regulator (TagR) functions as a tagatose-responsive repressor. The developed system exhibited a strong dose-dependent response to D-tagatose, ensuring uniform and tunable gene activation across cell populations. Additionally, a catabolite repression-enabled auto-induction strategy facilitated robust biomass accumulation, followed by targeted protein production. This expression system was successfully applied to overexpress recombinant proteins under both aerobic and anaerobic conditions.</p><p><strong>Conclusions: </strong>D-Tagatose is a naturally occurring low-calorie sugar that can serve as an inducer in vivo, including within the human gut microbiome. Thus, the tagatose-inducible expression system provides EcN with an additional tunable option for gene regulation, which may be valuable in applications such as synthetic biology and metabolic engineering.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"158"},"PeriodicalIF":4.3,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12226905/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564850","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":"Streamlined production of immobilized D-psicose 3-epimerase via secretion in Pichia pastoris: a new paradigm for industrial D-psicose production.","authors":"Pimsiriya Srila, Phitsanu Pinmanee, Boontiwa Ninchan, Nisit Watthanasakphuban","doi":"10.1186/s12934-025-02763-4","DOIUrl":"10.1186/s12934-025-02763-4","url":null,"abstract":"<p><strong>Background: </strong>D-psicose, a rare sugar with significant health benefits, holds great promise as a low-calorie sweetener. Its synthesis requires the enzyme called D-psicose 3-epimerase (DPEase), which converts D-fructose into D-psicose. This study focuses on an alternative protein expression system for secretion DPEase production, using Pichia pastoris KM71. The gene encoding DPEase from Bacillus sp. KCTC 13219 was codon-optimized and fused downstream of the α-factor signal peptide. A one-step purification and immobilization method was developed by directly binding crude DPEase to a His-tag affinity column, enhancing both enzyme stability and reusability.</p><p><strong>Results: </strong>The recombinant DPEase was successfully expressed in P. pastoris and efficiently secreted into the culture medium, simplifying downstream processing. The purified DPEase exhibited optimal activity at pH 6.0 and 60 °C, demonstrating remarkable thermostability and maintaining over 80% relative activity across a broad pH range (pH 5.0-11.0) and temperature range (35-70 °C). Purification with 200 mM imidazole elution resulted in a 12.54-fold increase in the purification factor, achieving a specific activity of 3.65 Units/mg. The maximum D-psicose conversion rate of purified DPEase was 17.03% at 120 min reaction with 10% (w/v) D-fructose. The developed DPEase immobilization system showed high binding efficiency, facilitating one-step purification and immobilization for ready-to-use DPEase column. The immobilized enzyme could be reused up to five cycles, maintaining 83.38% relative activity, highlighting the potential of this system for efficient D-psicose production.</p><p><strong>Conclusions: </strong>This study successfully developed a prototype system for extracellular DPEase production in a recombinant microorganism. This streamlined enzyme purification and immobilization, significantly reducing the DPEase production costs. The recombinant DPEase exhibited remarkable stability across a wide range of pH and temperature. This broad stability makes the enzyme highly promising for industrial-scale D-psicose production, resulting in reduced energy costs and simplified synthesis process. The DPEase demonstrated desirable properties for various D-psicose conversion conditions, and the immobilized enzyme exhibited efficient reusability. These findings support the potential application of this system for large-scale production of D-psicose, a rare sugar with promising uses in the food and pharmaceutical industries.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":"24 1","pages":"149"},"PeriodicalIF":4.3,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12220227/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144540902","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":"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}