Microbial Biotechnology最新文献

{"title":"A Novel Chitin-Based Purification System Using GAL1 Fusion Tags: Enhancing Recombinant Protein Production While Retaining Biological Activity","authors":"Yao-Kuang Tseng,&nbsp;Yun-Heng Lu,&nbsp;Yun Liu,&nbsp;Zhi-Wei Weng,&nbsp;Yu-Tzu Lin,&nbsp;Chih-Hsuan Tsai,&nbsp;Yueh-Lung Wu,&nbsp;Rong-Nan Huang","doi":"10.1111/1751-7915.70157","DOIUrl":"https://doi.org/10.1111/1751-7915.70157","url":null,"abstract":"<p>Efficient and economical purification methods are crucial for the commercial production of recombinant proteins with biomedical applications. In this study, we developed an affinity chromatography system that leverages the polysaccharide-binding properties of galectin-1 (GAL1) as a protein tag. The known GAL1-binding material, chitin, was used as the purification matrix. Melittin (MELT), a bee venom peptide known for its antimicrobial and anti-inflammatory properties with commercial potential, was chosen to validate this system. The GAL1–MELT fusion protein was expressed in <i>Escherichia coli</i> (<i>E. coli</i>) and successfully purified using a chitin-based matrix with sodium dodecyl sulfate (SDS) as a removable eluant. This method demonstrated higher purification efficiency compared to the His-tag/Ni-NTA approach, indicating that the GAL1/chitin system could serve as a superior alternative. The GAL1–MELT fusion protein retained strong antibacterial and anti-inflammatory activities, as well as collagen content modulation effects, confirming that MELT maintained its bioactivity. Apart from that, the GAL1–DsRed fusion protein was used as an additional protein target to evaluate the efficiency of the chitin-based column. Notably, all experiments were conducted without tag cleavage, showing that enzyme treatments for MELT isolation were unnecessary. This study highlights the potential of GAL1–polysaccharide interactions as a cost-effective and highly efficient alternative method for recombinant protein purification.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70157","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143950215","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":"Disarming the Pathogenicity of Methicillin-Resistant Staphylococcus aureus via Osmundacetone-Mediated Inhibition of Sortase A","authors":"Rong Wang,&nbsp;Chunhui Zhao,&nbsp;Dongbin Guo,&nbsp;Yueying Wang,&nbsp;Luanbiao Sun,&nbsp;Xinyao Liu,&nbsp;Yun Sun,&nbsp;Da Liu,&nbsp;Jiyu Guan,&nbsp;Li Wang,&nbsp;Bingmei Wang","doi":"10.1111/1751-7915.70119","DOIUrl":"https://doi.org/10.1111/1751-7915.70119","url":null,"abstract":"<p>Methicillin-resistant <i>Staphylococcus aureus</i> (MRSA) is a major global health threat due to its resistance to multiple antibiotics, making conventional treatments ineffective. The rise in antibiotic resistance highlights the urgent need for new therapies. Sortase A (SrtA), a key virulence factor in <i>Staphylococcus aureus</i> (<i>S. aureus</i>), facilitates bacterial adhesion and infection by anchoring surface proteins to host cells, making it a promising drug target. In this study, we investigated the potential of osmundacetone (OSC), a natural compound from Osmundae Rhizoma, as an SrtA inhibitor. Using fluorescence resonance energy transfer (FRET), OSC was found to inhibit SrtA with an IC₅₀ of 1.29 μg/mL (7.24 μM). Further in vitro assays confirmed the effectiveness of OSC in inhibiting SrtA-mediated bacterial adhesion, invasion and biofilm formation. Fluorescence quenching and molecular docking pinpointed the binding site of OSC on SrtA. In vivo, OSC improved survival rates in MRSA-infected mice and <i>Galleria mellonella</i> (<i>G. mellonella)</i> while reducing bacterial loads in infected tissues. These results suggest OSC as a promising candidate for anti-MRSA therapies.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70119","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143938955","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":"Peroxiredoxin Tsa1 Regulates the Activity of Trehalose Metabolism-Related Enzymes During Wine Yeast Biomass Propagation","authors":"Víctor Garrigós,&nbsp;Emilia Matallana,&nbsp;Cecilia Picazo,&nbsp;Agustín Aranda","doi":"10.1111/1751-7915.70154","DOIUrl":"https://doi.org/10.1111/1751-7915.70154","url":null,"abstract":"<p>Trehalose metabolism plays a crucial role in yeast stress tolerance during biomass propagation and dehydration, but its regulatory mechanisms under these industrial conditions remain incompletely understood. This study analyses the role of an antioxidant enzyme, the cytosolic peroxiredoxin Tsa1, in modulating trehalose metabolism in <i>Saccharomyces cerevisiae</i> wine strains during biomass production in molasses. Through comparative analyses in three commercial genetic backgrounds (L2056, T73, EC1118), we demonstrate that <i>TSA1</i> deletion generally leads to increased intracellular trehalose accumulation despite phenotypic variability among strains. Enzymatic assays revealed that Tsa1 does not regulate trehalose synthesis by altering glycolytic/gluconeogenic flux through pyruvate kinase. However, the deletion of <i>TSA1</i> resulted in increased oxidation of trehalose synthesis enzymes, as well as enhanced activity of trehalose-6-phosphate synthase and the trehalases Nth1 and Ath1, suggesting the involvement of peroxiredoxin in the futile cycle of trehalose synthesis and degradation. Scaling up the yeast biomass propagation process to semi-industrial conditions confirmed these findings, with increased trehalose levels in the <i>tsa1</i>∆ mutant correlating with enhanced desiccation resistance of the resulting biomass. These results highlight a novel Tsa1-dependent regulatory mechanism governing trehalose metabolism beyond its canonical antioxidant role. Understanding this pathway provides new insights into optimising yeast biomass propagation for industrial applications.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70154","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143930382","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":"Characterisation and Harnessing of 5-Hydroxymethylfurfural Metabolism in Pseudomonas umsongensis GO16 for the Production of 2,5-Furandicarboxylic Acid","authors":"Rhys Orimaco,&nbsp;Pauric Donnelly,&nbsp;Seán Sexton,&nbsp;Aoife McLoughlin,&nbsp;Sophie Kelly,&nbsp;Kevin E. O'Connor,&nbsp;Nick Wierckx,&nbsp;Tanja Narančić","doi":"10.1111/1751-7915.70159","DOIUrl":"https://doi.org/10.1111/1751-7915.70159","url":null,"abstract":"<p>In the search for biobased alternatives to traditional fossil plastics, 2,5-furandicarboxylic acid (FDCA) represents a potential substitute to terephthalic acid (TPA), a monomer of the ubiquitous polyester, polyethylene terephthalate (PET). <i>Pseudomonas umsongensis</i> GO16, which can metabolise TPA and ethylene glycol (EG), can also oxidise 5-hydroxymethylfurfural (HMF), a precursor to FDCA. The enzymes involved in the oxidation to FDCA, PsfA and PsfG, were identified and characterised. Deletion of FDCA decarboxylase HmfF involved in the conversion of FDCA to furoic acid, and subsequently to a central metabolic intermediate, 2-ketoglutarate, allowed for the accumulation of FDCA. GO16 Δ<i>hmfF</i> cells were grown on glycerol, TPA, EG or mock PET hydrolysate, and the catalyst was then used for the biotransformation of HMF to FDCA. When TPA was used as a growth substrate and to power the biotransformation, the transport of 5-hydroxymethyl-2-furancarboxylic acid (HMFCA) into the cytoplasm represented a rate-limiting step in HMF oxidation. De-bottlenecking transport limitations through <i>in trans</i> overexpression of the HMFCA transporter (HmfT) along with the PsfA aldehyde dehydrogenase and PsfG alcohol dehydrogenase allowed 100% conversion of 50 mM HMF to FDCA within 24 h when TPA, EG or mock PET hydrolysate were used to grow the biocatalyst and subsequently to power the biotransformation. This expands the repertoire of valuable products obtained from engineered <i>P. umsongensis</i> GO16 in the strategy to bio-upcycle post-consumer PET.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70159","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143930429","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 the Ecological and Genomic Adaptability of the Bacterial Genus Massilia for Environmental and Industrial Applications","authors":"Kamyar Amirhosseini,&nbsp;Mehrdad Alizadeh,&nbsp;Hamed Azarbad","doi":"10.1111/1751-7915.70156","DOIUrl":"https://doi.org/10.1111/1751-7915.70156","url":null,"abstract":"<p>The bacterial genus <i>Massilia</i> was first described in 1998, and since then has attracted growing interest due to its ecological plasticity and biotechnological promise. Certain species of the genus <i>Massilia</i> inhabit a variety of ecosystems, from arid deserts to polar glaciers, and exhibit unique adaptations such as resistance to cold and heat. In contaminated environments, some members of <i>Massilia</i> contribute significantly to the detoxification of heavy metals and the degradation of organic pollutants, presenting them as promising agents for bioremediation. In addition, <i>Massilia</i> species improve plant resistance and facilitate pollutant absorption in phytoremediation strategies. New research also highlights their potential as bioindicators of environmental health, given their abundance in anthropogenically influenced ecosystems and airborne microbial communities. In addition to their ecological roles, some <i>Massilia</i> species have potential in biotechnological applications by producing biopolymers and secondary metabolites. Here, we integrate findings across various habitats to present a comprehensive overview of the ecological and biotechnological importance of the genus <i>Massilia</i>. We highlight critical knowledge gaps and propose future research directions to fully harness the potential of this not fully explored bacterial genus to address environmental challenges, including contamination.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70156","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143909022","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":"Fimsbactin Siderophores From a South African Marine Sponge Symbiont, Marinomonas sp. PE14-40","authors":"Nompumelelo Philile Praiseworth Ikegwuoha,&nbsp;Thea Hanekom,&nbsp;Elzaan Booysen,&nbsp;Corbyn Jason,&nbsp;Shirley Parker-Nance,&nbsp;Michael T. Davies-Coleman,&nbsp;Leonardo Joaquim van Zyl,&nbsp;Marla Trindade","doi":"10.1111/1751-7915.70155","DOIUrl":"https://doi.org/10.1111/1751-7915.70155","url":null,"abstract":"<p>Low iron levels in marine habitats necessitate the production of structurally diverse siderophores by many marine bacterial species for iron acquisition. Siderophores exhibit bioactivities ranging from chelation for iron reduction in hemochromatosis sufferers to antimicrobial activity either in their own right or when coupled to known antibiotics for targeted delivery or for molecular imaging. Thus, marine environments are a sought-after resource for novel siderophores that could have pharmaceutical or industrial application. The fimsbactins A-F (<b>1–6</b>) are mixed catechol-hydroxamate siderophores that have only been reported to be produced by <i>Acinetobacter</i> species with the fimsbactin biosynthetic gene clusters (BGCs) widespread among species within this genus. Here, we identified a putative fimsbactin BGC from an uncharacterized marine isolate, <i>Marinomonas</i> sp. PE14-40. Not only was the gene synteny not conserved when comparing the pathway from <i>Marinomonas</i> sp. PE14-40 to the fimsbactin BGC from <i>Acinetobacter</i> sp., but five of the core biosynthetic genes found in the canonical fimsbactin BGC are located elsewhere on the genome and do not form part of the core cluster in <i>Marinomonas</i> sp. PE14-40, with four of these, <i>fbsBCDL,</i> colocalized. Through ESI-MS/MS analysis of extracts from <i>Marinomonas</i> sp. PE14-40, the known fimsbactin analogues <b>1</b> and <b>6</b> were identified, as well as two new fimsbactin analogues, <b>7</b> and <b>8</b>, containing a previously unreported L-lysine-derived hydroxamate moiety, <i>N</i>_<i>1</i>-acetyl-<i>N</i>_<i>1</i>-hydroxycadaverine. Feeding experiments using stable isotope-label L-lysine provided further evidence of the <i>N</i>_<i>1</i>-acetyl-<i>N</i><i>₁</i>-hydroxycadaverine moiety in <b>7</b> and <b>8</b>. The study demonstrates functional conservation in seemingly disparate biosynthetic pathways and enzyme promiscuity's role in producing structurally diverse compounds.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70155","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143908864","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":"Loop-Mediated Isothermal Amplification (LAMP) for the Diagnosis of Sexually Transmitted Infections: A Review","authors":"Yasaman Ahmadi,&nbsp;Yejiong Yu,&nbsp;Zhanfeng Cui,&nbsp;Wei E. Huang,&nbsp;Monique I. Andersson","doi":"10.1111/1751-7915.70153","DOIUrl":"https://doi.org/10.1111/1751-7915.70153","url":null,"abstract":"<p>Sexually transmitted infections (STIs) remain a significant public health concern. Given the asymptomatic nature of many STIs, diagnostic testing is critical for determining the appropriate treatment, enabling effective tracing and reducing the risk of further transmission. Nucleic acid amplification tests (NAATs) are the most sensitive and the most widely used in well-resourced settings. The majority of available NAATs are based on polymerase chain reaction (PCR), which requires highly trained personnel and costly equipment, making it impractical for resource-limited settings. Loop-mediated isothermal amplification (LAMP) has emerged as a simple, rapid, sensitive and low-cost alternative for pathogen detection, particularly well-suited for point-of-care tests (POCT). In this review, we evaluate LAMP assays reported in the literature for the detection of pathogens linked to the high incidence STIs prioritised by the World Health Organization (WHO) for POCT in 2023. These include <i>Neisseria gonorrhoeae</i>, <i>Chlamydia trachomatis</i>, <i>Trichomonas vaginalis</i>, <i>T. pallidum</i> subspecies <i>pallidum</i>, as well as other common STIs such as herpes simplex virus, hepatitis B virus and human immunodeficiency virus (HIV). For each LAMP assay, we identified and summarised the key elements such as the type and number of tested clinical specimens, chosen target gene, detection system, reference test and clinical outcomes. We highlight the advantages and limitations of these assays and discuss the gaps that should be addressed to improve their applicability for POCT.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70153","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143900902","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":"The Respiratory Tract Microbiome and Human Health","authors":"Patricia Fernández de Córdoba-Ansón,&nbsp;Iván Linares-Ambohades,&nbsp;Fernando Baquero,&nbsp;Teresa M. Coque,&nbsp;Ana Elena Pérez-Cobas","doi":"10.1111/1751-7915.70147","DOIUrl":"https://doi.org/10.1111/1751-7915.70147","url":null,"abstract":"<p>The respiratory tract microbiome (RTM) is a multi-kingdom microbial ecosystem that inhabits various niches of the respiratory system. While previously overlooked, there is now sufficient evidence that the RTM plays a crucial role in human health related to immune system training and protection against pathogens. Accordingly, dysbiosis or disequilibrium of the RTM has been linked to several communicable and non-communicable respiratory diseases, highlighting the need to unveil its role in health and disease. Here, we define the RTM and its place in microbiome medicine. Moreover, we outline the challenges of RTM research, emphasising the need for combining methodologies, including multi-omics and computational tools. We also discuss the RTM's potential for diagnosing, preventing and treating respiratory diseases and developing novel microbiome-based therapies to improve pulmonary health.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70147","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143880148","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":"Recent Advances in Alginate Lyase Engineering for Efficient Conversion of Alginate to Value-Added Products","authors":"Hyo Jeong Shin,&nbsp;Jo Hyun Moon,&nbsp;Sunghwa Woo,&nbsp;Chung Won Lee,&nbsp;Gyoo Yeol Jung,&nbsp;Hyun Gyu Lim","doi":"10.1111/1751-7915.70150","DOIUrl":"https://doi.org/10.1111/1751-7915.70150","url":null,"abstract":"<p>Alginate lyases depolymerize alginate and generate alginate oligosaccharides (AOS) and eventually 4-deoxy-L-erythro-5-hexoseulose uronate (DEH), a monosaccharide. Recently, alginate lyases have garnered significant attention due to the increasing demand for AOS, which exhibit bioactivities beneficial to human health, livestock productivity, and agricultural efficiency. Additionally, these enzymes play a crucial role in producing DEH, essential in alginate catabolism in bacteria. This review explains the industrial value of AOS and DEH, which contribute broadly to industries ranging from the food industry to biorefinery processes. This review also highlights recent advances in alginate lyase applications and engineering, including domain truncation, chimeric enzyme design, rational mutagenesis, and directed evolution. These approaches have enhanced enzyme performance for efficient AOS and DEH production. We also discuss current challenges and future directions toward industrial-scale bioconversion of alginate-rich biomass.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70150","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143880107","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":"Greening the Production of Indigo Blue Exploiting Light and a Recombinant Synechocystis sp. PCC6803 Strain Expressing the Enzyme mFMO","authors":"Giovanni Loprete,&nbsp;David Rubert,&nbsp;Francesco Bellusci,&nbsp;Nikola Lončar,&nbsp;Marco W. Fraaije,&nbsp;Elisabetta Bergantino","doi":"10.1111/1751-7915.70146","DOIUrl":"https://doi.org/10.1111/1751-7915.70146","url":null,"abstract":"<p>Cyanobacteria are emerging as interesting cell factories, offering the significant advantage of their in-built photosynthetic machinery, which generates NADPH to support redox biocatalysis. In this study, we assessed the potential of the cyanobacterium <i>Synechocystis</i> sp. PCC6803 in producing the dye indigo by light-driven whole-cell biotransformation using indole as a starting compound. A stable transgenic strain expressing a flavin-containing monooxygenase from <i>Methylophaga aminisulfidivorans</i> (mFMO) was engineered, enabling light-dependent indigo production. Upon optimising conditions, effective biotransformations could be performed, resulting in 112 mg/L indigo (86% conversion of the furnished indole). Additionally, we present a method for the recovery of the secreted dye directly from the growth medium through solid-phase absorption on polyamide nets. Overall, the effectiveness and sustainability of the biotransformation in <i>Synechocystis</i> sp. PCC6803 performed at the laboratory scale provide a strong basis for further exploring the applicability of the process.</p>","PeriodicalId":209,"journal":{"name":"Microbial Biotechnology","volume":"18 5","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.70146","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143880109","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}