Journal of Basic Microbiology最新文献

{"title":"Biotechnological Potential of the Fusarium fujikuroi Complex From Amazonian Oenocarpus bacaba: Lipase Production and Characterization.","authors":"Lucely Nogueira Dos Santos, Rafael Firmani Perna, Ana Carolina Vieira, Kalebe Ferreira Furtado, Alex Fernando de Almeida, Cristiane Angélica Ottoni, Leandro Mantovani de Castro, Felipe Mello, Yoannis Domínguez, Nelson Rosa Ferreira","doi":"10.1002/jobm.70067","DOIUrl":"https://doi.org/10.1002/jobm.70067","url":null,"abstract":"<p><p>This study investigates the diversity of filamentous fungi in the Amazon biome, particularly the genus Fusarium, known for producing biotechnologically valuable metabolites. The research aimed to isolate and identify fungi from Oenocarpus bacaba Mart. fruits and analyze the biochemical properties of lipase produced by the strains (maximum activity of 1750 U mL⁻¹). Two isolates, FF1 and FF2, were identified using morphological and molecular techniques, with ITS sequence data suggesting they belong to the Fusarium fujikuroi species complex, though the exact species remains unconfirmed. This is the first report that highlights the biotechnological potential of the F. fujikuroi complex isolated from Oenocarpus bacaba, emphasizing the relevance of Amazonian biodiversity as a source of microorganisms with promising applications in sustainable industrial processes. The results show that native fruits, such as bacaba, are effective matrices for prospecting filamentous fungi producers of enzymes of biotechnological interest, such as lipases. These findings reinforce the importance of rational exploitation of the Amazonian microbiota for the development of bioproducts and eco-efficient industrial processes.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70067"},"PeriodicalIF":3.5,"publicationDate":"2025-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144247978","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of Newly Discovered Polyester Polyurethane-Degrading Methylobacterium aquaticum Strain A1.","authors":"Seong Hyeon Lee, Haemin Jeong, Injun Jung, Myounghyun Choi, Ah-Ram Kim","doi":"10.1002/jobm.70066","DOIUrl":"https://doi.org/10.1002/jobm.70066","url":null,"abstract":"<p><p>In this study, we present Methylobacterium aquaticum A1, a novel strain capable of degrading polyester polyurethane (PE-PUR). The attachment of M. aquaticum A1 to PE-PUR and its degradation capabilities were verified using Scanning Electron Microscopy (SEM) and Fourier-Transform Infrared Spectroscopy (FT-IR). Analysis of the reference genome of M. aquaticum revealed genes encoding enzymes with potential PE-PUR degrading activity, including esterases, lipase, proteases and amidase such as tesA, pgpB, aes, aprE, lon, degQ, and gatA. An esterase activity assay using p-nitrophenyl acetate (p-NPA) showed increased ester bond-cleaving activity when M. aquaticum A1 was exposed to polyurethane diol (PU-diol), suggesting inducible enzymatic activity involved in PE-PUR degradation. These findings highlight the potential of M. aquaticum A1 as a promising biocatalyst for PE-PUR degradation.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70066"},"PeriodicalIF":3.5,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144215836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cover: Journal of Basic Microbiology. 6/2025","authors":"","doi":"10.1002/jobm.70056","DOIUrl":"https://doi.org/10.1002/jobm.70056","url":null,"abstract":"<p><b>Cover illustration:</b></p><p>The cover image shows agar plates that underwent microbial art fixation for microbiology teaching. Each Petri dish was designed with live bacterial cultures such as <i>Escherichia coli, Staphylococcus aureus</i>, and <i>Pseudomonas aeruginosa</i> to form recognizable shapes, symbols, and messages, and was chemically fixed to preserve morphology and pigmentation of microbial colonies for up to 6 months.</p><p>(Photo: Hatice Nur Halipçi Topsakal, Istanbul Atlas University, Istanbul, Turkey)\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":"65 6","pages":""},"PeriodicalIF":3.5,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jobm.70056","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144206886","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Issue Information: Journal of Basic Microbiology. 6/2025","authors":"","doi":"10.1002/jobm.70055","DOIUrl":"https://doi.org/10.1002/jobm.70055","url":null,"abstract":"","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":"65 6","pages":""},"PeriodicalIF":3.5,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jobm.70055","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144206638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multifaceted Rhizobacterial Co-Inoculation Enhances Drought-Stress Tolerance in Tomato: Insights Into Physiological, Biochemical, and Molecular Responses.","authors":"Waquar Akhter Ansari, Mohammad Shahid, Zaryab Shafi, Mohammad Abul Farah, Mohammad Tarique Zeyad, Khalid Mashay Al-Anazi, Lukman Ahamad","doi":"10.1002/jobm.70065","DOIUrl":"https://doi.org/10.1002/jobm.70065","url":null,"abstract":"<p><p>Drought-tolerant multifunctional soil bacteria can increase drought tolerance mechanisms in plants. Here, rhizobacteria CRB-4 and SPGPR-11 were isolated and their single and co-inoculation effect was evaluated in drought-stressed tomato plants. Isolates were selected based on their preliminary polyethylene glycol (PEG) screening, and plant growth-promoting properties. Increasing water stress adversely affected growth and physiological attributes of tomato plant. However, plant growth-promoting bacteria (PGPB), particularly their combined inoculation, alleviated drought stress. For instance, CRB-4, SPGPR-11 and their co-inoculation significantly increased root biomass (33.3, 37.5% and 45.4%), total chlorophyll (17.5, 15.6% and 19.2%) and carotenoid content (20, 30.4% and 48.3%) in 3%-PEG-stressed tomatoes. Similarly, co-inoculation of 3%-PEG-treated plants with PGP isolates resulted in a significant increase in Fv/Fm (50%), Fv'/Fm' (29.4%), PS-II (44.4%), Pq (40%), NPQ (40%), and effective electron transfer rate (37.5%). Furthermore, under 5%-PEG stress, CRB-4, SPGPR-11, and their co-inoculation enhanced drought stress resilience in tomato by improving leaf gas exchange attributes. Combined inoculation significantly enhanced gs (19%), Ci (31.2%), transpiration rate (41%), water vapor deficit (38.7%), iWUE (33.7%), and photosynthetic rate (33.3%) in 5%-PEG-stressed tomatoes. Among the treatments, co-inoculations significantly enhanced the antioxidant defense responses in drought-stressed tomatoes. Concurrently, qRT-PCR analysis revealed a significant upregulation in ROS scavenging genes, SOD, CAT, APX, GR, and POD, by 6.53, 14.08, 11.72, 10.12, and 5.95-fold, respectively, in drought-stressed plants co-inoculated with bacterial strains. This study concludes that PGP isolates CRB-4 and SPGPR-11, alone or in combination, offer an effective, eco-friendly solution for improving drought resilience in tomatoes.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70065"},"PeriodicalIF":3.5,"publicationDate":"2025-05-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144187091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evaluating Fungal Metal Tolerance Using MALDI-TOF MS: A Rapid Alternative to Conventional MIC Methods.","authors":"Nicolás Bustamante, Javier Ortiz, Javiera Soto, Nathalia Baptista Dias, Cristian Vega, César Arriagada-Escamilla","doi":"10.1002/jobm.70064","DOIUrl":"https://doi.org/10.1002/jobm.70064","url":null,"abstract":"<p><p>Metal contamination represents a critical environmental challenge, adversely impacting ecosystems and human health. Microorganisms, including fungi, have developed diverse mechanisms to tolerate and resist metal-induced stress, making them valuables for bioremediation. This study evaluates the metal tolerance of Absidia glauca, Penicillium bilaiae, and Trichoderma viridescens using minimum inhibitory concentration (MIC) assay and the alternative minimum profile change concentration (MPCC) approach via MALDI-TOF MS. MIC assay revealed species-specific tolerances to copper, zinc, and cadmium. A. glauca showed the highest tolerance to copper and cadmium (75 and 9 mg L^-1), producing a dry biomass of 0.03 and 0.04 g, respectively. While P. bilaiae exhibited the highest tolerance to zinc (75 mg L^-1) producing a dry biomass of 0.06 g. MALDI-TOF MS provided rapid proteomic information on fungal responses to metals, showing changes in the protein profile as the metal concentration increased. We performed a comparative analysis between the values obtained in the MIC and MPCC, giving a positive correlation in the results of both techniques for Cu, Zn, and Cd (r = 1.00; 0.87 and 0.99 respectively, p < 0.05). In conclusion, MALDI-TOF MS has proven to be an effective method for analyzing fungal proteomic responses to metal exposure, providing more detailed molecular insights than traditional MIC assays. Future studies should investigate the mechanisms underlying metal resistance, particularly focus on the regulation of specific proteins.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70064"},"PeriodicalIF":3.5,"publicationDate":"2025-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144142646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Genetic Organization Analysis of the Major Cold-Shock Gene deaD in Escherichia coli.","authors":"Soma Jana, Sritapa Basu Mallick, Partha Pratim Datta","doi":"10.1002/jobm.70063","DOIUrl":"https://doi.org/10.1002/jobm.70063","url":null,"abstract":"<p><p>DeaD or CsdA (cold-shock DEAD box protein A), is an ATP-dependent RNA helicase, a major cold-shock protein that plays key roles in translation initiation, ribosome biogenesis, and mRNA decay at low temperatures in bacteria. The DeaD homolog of Escherichia coli is ubiquitously present in eukaryotes, archaea, and bacteria. DeaD has been extensively studied at the protein level in E. coli. However, the complex mechanism of deaD gene regulation is yet to be deciphered. To study deaD gene regulation, we engineered a promoter-less reporter plasmid vector which contains an ORF of green fluorescence protein (GFP) without a promoter region. We performed sequential, incremental, zone-wise cloning of DNA fragments of the upstream region of the deaD ORF and analyzed GFP expression in our promoter-less plasmid vector to identify the promoter region. We found out the promoter around 800 nucleotides upstream of deaD ORF, which was further confirmed by its In Vivo deletion in the E. coli genome. We observed the expression of the deaD gene might also occur from the immediate upstream of the nlpI and pnp gene, revealing the phenomenon of an operon system. Interestingly, we found the short ORF of the gene yrbN overlaps with the ORF of deaD but not in the frame. Subsequently, Multiple Sequence Alignment profiles showed that not only the promoter and the unusually long 5'UTR region but the whole genetic arrangement of the deaD gene, including the overlapping phenomenon of ORF of the yrbN gene, is conserved in Gamma-proteobacteria indicating a conserved gene expression pattern.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70063"},"PeriodicalIF":3.5,"publicationDate":"2025-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144142577","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular Mimicry by Bacterial Effector Proteins.","authors":"Aakar Anshul, Pooja Kumari","doi":"10.1002/jobm.70059","DOIUrl":"https://doi.org/10.1002/jobm.70059","url":null,"abstract":"<p><p>Microorganisms have developed sophisticated mechanisms to invade the host and evade the host's immune surveillance while exploiting the host's resources for their establishment through co-evolution. Many pathogens employ specialized protein secretion systems to transport virulence factors from the bacterial cytosol into host cells. These bacterial protein secretion systems can generally be categorized into different classes based on their structures, functions, and specificity. Notably, some pathogens have evolved proteins that mimic specific eukaryotic cell proteins, enabling them to manipulate host cellular pathways. This phenomenon is known as molecular mimicry. These proteins either closely resemble eukaryotic proteins or possess domains typically found in eukaryotes but generally absent in prokaryotes. This mimicry allows pathogens to interfere with host functions and facilitate their survival and proliferation within the host. Here, we review the fundamental characteristics of these secretion pathways, delve into the remarkable diversity of effector proteins, and explore the molecular mechanisms by which different pathogens rewire cellular pathways. Additionally, we discuss recent findings on strategies to counteract pathogen mimicry and the insights gained for the discovery of new antimicrobials.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70059"},"PeriodicalIF":3.5,"publicationDate":"2025-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144142579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhanced Antibacterial and Anti-Inflammatory Efficiency of Serratiopeptidase Immobilized on CMC-Silver Nanoparticles.","authors":"Taleeha Roheen, Mehvish Bibi, Muhammad Fayyaz Ur Rehman, Nasir Assad, Humaira Yasmeen Gondal, Muhammad Nadeem, Farhan Ahmad Atif, Fozia Batool, Nazia Perveen, Rahman Qadir, Saif Ur Rehman, Misbah Maqbool, Shahzad","doi":"10.1002/jobm.70060","DOIUrl":"https://doi.org/10.1002/jobm.70060","url":null,"abstract":"<p><p>In the present study, sunlight-mediated Carboxymethyl cellulose silver nanoparticles (CMC-AgNPs) have been synthesized as a carrier for serratiopeptidase immobilization. Morphological behavior of CMC-AgNPs, crystallinity and functional group identification were evaluated using scanning electron microscopy, X-ray diffraction and Fourier transform infrared spectroscopy, respectively. The prepared nanoparticles (NPs) were also subjected to zeta potential, which disclosed the zeta potential value of about-36.06 mV, suggesting their negative charge surface, good stability and polydispersity. SRP was immobilized on synthesized NPs through covalent adsorption using glutaraldehyde as a crosslinker. Immobilized (CMC/Ag-SRP) exhibited 80.95% immobilization efficiency and 79.73% immobilization yield, respectively. Remarkably greater relative activities at broader temperature and pH ranges were attained by SRP after immobilization in comparison to its free counterpart. The K_m value was significantly higher for immobilized enzyme, whereas V_max value was conspicuously lower, indicating that less enzyme was sufficient to achieve maximum velocity. The greater zone of inhibition was displayed by immobilized CMC-AgNPs than that of native NPs against both gram-positive Listeria monocytogenes (12 ± 0.05 mm) and gram-negative Escherichia coli (22 ± 0.12 mm). The bigger zone on casein agar plates for immobilized NPs confirms enhanced caseinolytic activity in comparison to starting materials. In Vitro anti-inflammatory assessment of CMC/Ag-SRP presented more potency than the native NPs, which was comparable to the standard drug. Reusability data demonstrated 50% of initial activity was retained after seven successive cycles. Thereby, it is concluded that incorporation of serratiopeptidase onto CMC-AgNPs presented enhanced effects at lower concentrations with improved anti-inflammatory activity.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70060"},"PeriodicalIF":3.5,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144119730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analysis of Benzoate 1,2-Dioxygenase Identifies Shared Electron Transfer Components With DxnA1A2 in Rhizorhabdus wittichii RW1.","authors":"Igor Ivanovski, Suha Eleya, Gerben J Zylstra","doi":"10.1002/jobm.70061","DOIUrl":"https://doi.org/10.1002/jobm.70061","url":null,"abstract":"<p><p>Rhizorhabdus wittichii RW1 is known for its ability to degrade polycyclic aromatic hydrocarbons, such as dibenzo-p-dioxin (DD) and dibenzofuran (DF). We hypothesized that the R. wittichii RW1 benzoate 1,2-dioxygenase shares electron transfer components with the DD/DF angular dioxygenase (DxnA1A2), similar to many aromatic hydrocarbon degrading sphingomonads. The genes encoding the benzoate oxygenase component (benAB) were identified in the RW1 genome sequence through homology to known benzoate oxygenases. The RW1 benAB genes are upstream from a putative benD gene encoding a cis-benzoate dihydrodiol dehydrogenase. Knockout of the benA gene resulted in a strain unable to grow on benzoate. The knockout strain could be complemented with the cloned benABD genes. Expression of benAB in Escherichia coli along with the fdx3 and redA2 genes, which encode the ferredoxin and reductase components utilized by DxnA1A2, produced a functional benzoate dioxygenase enzyme capable of converting benzoate to benzoate cis-dihydrodiol. Double knockout mutagenesis of the RW1 redA1 and redA2 reductase genes results in a mutant unable to grow on benzoate as the sole carbon source. Based on the gene knockout and heterologous expression experiments the RW1 benzoate 1,2 dioxygenase was identified and shares electron transfer components with DxnA1A2.</p>","PeriodicalId":15101,"journal":{"name":"Journal of Basic Microbiology","volume":" ","pages":"e70061"},"PeriodicalIF":3.5,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144127736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}