Biotechnology Letters最新文献

{"title":"Correction: Polyhydroxyalkanoate production by Paramecium caudatum isolated from industrial wastewater: a micro eukaryotic host for bioplastic accumulation.","authors":"Usama Shabbir, Itrat Zahra, Ayesha Liaqat, Ayesha Arshad, Shahid Nawaz, Michael Betenbaugh, Roohi Ijaz, Awais Ibrahim, Tuba Arooj, Bushra Muneer, Nazish Mazhar Ali, Uzma Ramzan, Sammi Rasheed, Ayesha Ghauri, Manel Ben Ali, Amor Hedfi, Abdul R Shakoori, Farah R Shakoori","doi":"10.1007/s10529-025-03651-y","DOIUrl":"https://doi.org/10.1007/s10529-025-03651-y","url":null,"abstract":"","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"109"},"PeriodicalIF":2.1,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145111820","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 cloning and modelling of a thermostable α-amylase from a thermophilic Geobacillus sp. DS3.","authors":"Lucia Dhiantika Witasari, Leon Bhagawanta Cahyono, Dina Clarissa Kurniawan, Rohmad Yudi Utomo, Muhammad Nur Cahyanto, Muhammad Saifur Rohman, Irfan Dwidya Prijambada","doi":"10.1007/s10529-025-03647-8","DOIUrl":"https://doi.org/10.1007/s10529-025-03647-8","url":null,"abstract":"<p><p>Thermostable α-amylase from Geobacillus sp. DS3, isolated from the Sikidang Crater, Dieng Plateau, Indonesia, was previously purified and characterized. However, production from thermophilic bacteria requires high-temperature cultivation. This study aimed to clone and express the amy gene encoding α-amylase in Escherichia coli BL21(DE3) for easier enzyme production. The amy gene (1638 bp) was amplified via PCR, TA-cloned, and inserted into the pET-SUMO expression vector, which includes an N-terminal His-tag and SUMO-tag to enhance expression and solubility. The recombinant plasmid (pET-SUMO-amy) was transformed into E. coli BL21(DE3) for protein expression. Homology modelling using MOE software and template PDB ID 1HVX (91.5% identity) revealed a reliable 3D structure. Structural analysis showed altered calcium and sodium ion binding compared to the template, with calcium ions interacting with more residues. Docking studies revealed that maltotetraose binding is stabilized by five key residues: Asp268, His272, Trp300, Asn363, and Asp365. The enzyme displayed optimal activity at 70 °C and retained 60% activity at 90 °C. Kinetic parameters showed a low K_m (6.77 mM) and V_max (0.20 U/mL), indicating high substrate affinity. In conclusion, the recombinant α-amylase exhibited thermostability and substrate affinity suitable for industrial applications such as starch liquefaction and porous starch production at elevated temperatures.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"108"},"PeriodicalIF":2.1,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145111749","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":"Correction: Identification and characterisation of subtype-specific anti-N-CoR OSGEP protease in acute myeloid leukaemia (AML-M5) cell lineage.","authors":"S Annie Jeyachristy, Eshan Rosly Nazem, Ramesh Thevendran, Ahsas Goyal, Kavita Goyal, Solayappan Maheswaran, Atreyi Pramanik, Gaurav Gupta, Neeraj Kumar Fuloria, Shivkanya Fuloria, Md Sadique Hussain","doi":"10.1007/s10529-025-03650-z","DOIUrl":"https://doi.org/10.1007/s10529-025-03650-z","url":null,"abstract":"","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"110"},"PeriodicalIF":2.1,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145111696","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":"Potential applications of lactic acid bacteria from Egyptian dairy products as novel antioxidant and anticancer agents.","authors":"Reham A Madian, Amel A Ibrahim, Mohamed Yacout, Sameh Awad, Sarah A Aggag","doi":"10.1007/s10529-025-03648-7","DOIUrl":"https://doi.org/10.1007/s10529-025-03648-7","url":null,"abstract":"<p><strong>Purpose: </strong>Several scientific studies have revealed the role of probiotic lactic acid bacteria and their metabolites, including antioxidant activity, which is required for reducing oxidative stress, and have implications for cancer treatment. This study evaluated the ability of isolates to exert antioxidative and in vitro anti-tumor effects against the HCT-116 colon cancer cell line, with fewer side effects compared to chemotherapy.</p><p><strong>Methods: </strong>The in vitro antioxidative capacity of LAB isolates was quantified against DPPH free radicals. The cytotoxicity effects against the HCT-116 cells were analyzed using the MTT assay, microscopic fluorescence, flow cytometry, and qRT-PCR analysis of immunomodulatory cytokines and cancer-related gene expression.</p><p><strong>Results: </strong>Seven LAB isolates exhibited potent antioxidant activity, scavenging 51.20 to 78.29% of DPPH free radicals. Lactobacillus delbrueckii subsp. bulgaricus (RE 254) demonstrated superior activity, with 78.29% scavenging and a ferric-reducing activity power of 38.04%. Conversely, Lactiplantibacillus plantarum (RE 298) showed 53.67% and 16.08% activity, respectively. At a concentration of 25 × 10³ CFU/ml, both strains induced pronounced cytotoxic effects on HCT-116 cells after 72 h (71.1% for RE 254 and 62.5% for RE 298). This cytotoxicity was mediated by apoptosis, driven by the upregulation of IL-2 and the concomitant downregulation of key genes, including BCL-2, PARK, TARC, LIF, IL-4, IL-6, CD1A, and CD1B.</p><p><strong>Conclusion: </strong>The findings strongly suggest that RE 254 and RE 298 are compelling candidates for use as functional supplements and adjunctive therapeutics in colon cancer management. Their efficacy, demonstrated through multifaceted anti-tumor mechanisms, warrants further validation through in vivo studies to assess their clinical potential.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"107"},"PeriodicalIF":2.1,"publicationDate":"2025-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145079422","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":"Gene pyramiding for enhancing resistance to blast and bacterial blight disease in rice through maker assisted selection.","authors":"Mohammad Abdul Latif, Omar Kayess, Rakibul Hasan","doi":"10.1007/s10529-025-03646-9","DOIUrl":"https://doi.org/10.1007/s10529-025-03646-9","url":null,"abstract":"<p><p>Diseases are a global threat to rice production. Among them, rice blast and bacterial blight (BB) are most significant. To enhance targeted disease resistance, the marker-assisted backcross breeding (MABB) approach was employed to pyramid two blast (Pi9 and Pb1) and three BB resistant (R) genes (Xa4, xa13, and Xa21) into a high-quality rice cultivar BRRI dhan100. The donor parents Pi9-US2 (Pi9), Pb1-US2 (Pb1), and IRBB58 (Xa4, xa13, and Xa21) contributed these five genes. We followed a triple-cross breeding strategy, followed by backcrossing, selfing, and foreground selection to produce BC₃F₅ progenies. Chi-square analysis of 420 BC₃F₂ individuals confirmed the inheritance patterns of blast and BB resistance were controlled by a simple Mendelian fashion. Finally, we selected 38 advanced lines (ALs), and among them, twelve lines possessed all 5 candidate R genes, while fifteen consisted of 4 genes in different combinations. The disease rating scale of these ALs varied from 0 to 3 for both blast and BB diseases, while BRRI dhan100 ranging from 7 to 9. The G23, G13, G5, G10, G15, and G29 ALs exhibited higher yields ranging from 7.22-7.34 ton ha^-1 compared to the check, BRRI dhan100. Marker-trait association analysis displayed molecular markers negatively associated with disease susceptibility. Therefore, gene introgression by MABB could effectively identify and functionally validate the candidate R genes with high accuracy to develop a resistant variety to multiple diseases in rice breeding programs.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"106"},"PeriodicalIF":2.1,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145074476","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":"Selection of lyoprotectants for the stabilization of the freeze-dried probiotic Limosilactobacillus reuteri CRL 1098 by an accelerated inactivation assay.","authors":"María Inés Torino, Graciela Font, María José Fornaguera, María Pía Taranto","doi":"10.1007/s10529-025-03645-w","DOIUrl":"https://doi.org/10.1007/s10529-025-03645-w","url":null,"abstract":"<p><p>The high potential of the probiotic L. reuteri CRL 1098, as hypocholesterolemic and vitamin B₁₂ producer strain, would require addressing freeze-drying studies of the microorganism as well as its stability during storage. L. reuteri CRL 1098 was freeze-dried with glutamate, maltodextrin and trehalose as lyoprotectants and an accelerated inactivation assays under isothermal conditions (50, 60 and 70°C) was used to evaluate the stability of lyophilizates. Results obtained were analyzed with informatic GInaFiT Ap-inn and traditional predictive tools (D/z and Arrhenius models) for describing both, the inactivation process and the bacterial behaviour. The predicted shelf life of the lyophilized probiotic to obtain 1 × 10⁶ UFC/g was experimentally tested at 30°C. Regardless of the lyoprotectant used, the survival of L. reuteri CRL1098 fitted acceptably to the weilbulian model of Marfat in all heat treatments; the data described curves with up dawn concavities (p < 1) and allowed to identify a more sensitive bacterial population through the first decimal reduction time (δ-value) specially at 50°C in presence of maltodextrin. From the second reduction time, survivors of L. reuteri CRL 1098 fitted to first kinetic order reactions (lineal distribution of data), so D-values (decimal reduction time), k-values (inactivation rate constant), and z-values (intrinsic resistance) as well as the activation energy Ea, were calculated through D/z model and Arrhenius model. From these, a resistant subpopulation of L. reuteri CRL 1098 could be described, mainly when trehalose was used as lyoprotectant, which was characterized by high z-values. These results correlated with higher D-values but lower k-values and Ea in trehalose, which did not show the best stabilizing property along the storage tested at 30°C. Maltodextrine proved to be the best stabilizer lyoprotectant, especially when the shelf life is predicted at low temperatures of conservation.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"105"},"PeriodicalIF":2.1,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145074458","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":"Unveiling the psychrozyme potential of micro-fungi inhabiting the high altitude passes of the trans-Himalayas.","authors":"Arjun Khajuria, Skarma Nonzom","doi":"10.1007/s10529-025-03649-6","DOIUrl":"10.1007/s10529-025-03649-6","url":null,"abstract":"<p><p>Microfungi are known as potent producers of extracellular enzymes, making them crucial in various industrial processes, especially those involving the degradation of organic matter. This study aimed to screen the cold-tolerant microfungi inhabiting the trans-Himalayan region for their potential to produce α-amylase and protease enzymes. Soil samples were collected from two high altitude passes in Ladakh region, India and a total of 68 fungal strains were isolated using serial dilution pour plate method. These isolates were screened qualitatively for enzymatic production using specific agar media, including glucose yeast extract peptone agar (GYPA) for α-amylase and skimmed milk agar (SM agar) for protease activity. Among the screened isolates, 18 fungal species exhibited α-amylase activity, with Aspergillus uvarum, A. sydowii, and Nodulisporium verrucosum showing the largest zones of clearance, 13 fungal species exhibited protease activities, with Penicillium griseofulvum and P. fellutanum showing the largest clear zones. This study highlights the diversity of cold-adapted fungi in this region with significant enzyme producing potential, suggesting their applicability in industrial processes such as bioconversion of starch and protein-rich materials, particularly in cold environments.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"104"},"PeriodicalIF":2.1,"publicationDate":"2025-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145063478","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":"Recently funded actions and current calls in the field of red biotechnology and regenerative medicine under the health cluster of the EU framework programme horizon Europe.","authors":"Bernd Walter Rainer","doi":"10.1007/s10529-025-03639-8","DOIUrl":"10.1007/s10529-025-03639-8","url":null,"abstract":"<p><p>Health-related biotechnology and regenerative medicine are prominent fields for research funding under the European Framework Programme. Based on a bibliometric analysis of projects funded under the current Horizon Europe Programme an overview of scientifically top-ranking projects is presented. The classical collaborative research scheme represented by the Health Cluster prevails in terms of funding source. Biotechnology and regenerative medicine have been recognised as promising fields at both the global and European levels and this is also reflected in the current calls for research proposals in the Health Cluster under Horizon Europe.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"102"},"PeriodicalIF":2.1,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145039028","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":"Novel TdsD nitroreductase: characterization of kinetics and substrate specificity.","authors":"Benjaminas Valiauga, Dovydė Žulpaitė, Abigail V Sharrock, David F Ackerley, Narimantas Čėnas","doi":"10.1007/s10529-025-03636-x","DOIUrl":"10.1007/s10529-025-03636-x","url":null,"abstract":"<p><p>The reduction of quinones and nitroaromatic compounds catalyzed by Type I nitroreductases is important due to its role in their potential cytotoxic effects and/or biodegradation. The main goal of this work was to investigate the mechanism of catalysis of a TdsD nitroreductase (NR) (TdsD1), a member from an understudied branch of the nitroreductase superfamily, derived from a soil metagenome study. Like the Type I NRs NfsA and NfsB, TdsD1 performed two-electron reduction of quinones and four-electron reduction of nitroaromatic compounds according to a \"ping-pong\" mechanism with a rate-limiting oxidative half-reaction. TdsD1 was also inhibited by the classical inhibitors of other NRs, dicoumarol and Cibacron blue. Despite sharing only a low degree of homology with the NfsA and NfsB subfamily enzymes, sequence comparisons and computer modelling point to the possibility of an analogous FMN isoalloxazine ring location within the intersubunit space of TdsD1. It also possesses similar specificity for nitroaromatic compounds and quinones, in particular the shared characteristic of being especially active with 2-hydroxy-1,4-naphthoquinone derivatives. It is possible that the similar character of binding of oxidants and other ligands relative to the NfsA and NfsB subfamily enzymes may be related to the conserved Arg27 and Ser53 residues in the active site of TdsD1.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"103"},"PeriodicalIF":2.1,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145051766","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":"Development of a biotechnological process for the production of recombinant canine interferon-alpha using the baculovirus-insect cell and larvae system.","authors":"Maria S Rodriguez, Ignacio Smith, Marcela S Villaverde, Joaquin M Birenbaum, Joaquin Poodts, Federico J Wolman, Alexandra M Targovnik, Maria V Miranda","doi":"10.1007/s10529-025-03644-x","DOIUrl":"10.1007/s10529-025-03644-x","url":null,"abstract":"<p><p>Currently, Latin America is experiencing a considerable increase in demand for veterinary products to ensure animal health. In particular, interferons (IFNs) are cytokines that play an important role in small animal clinics for the treatment of viral or oncological diseases. We developed a biotechnological process for the production of recombinant canine interferon CaIFN-α7 (rCaIFN-α7) using the baculovirus-insect cell and larvae system, and evaluated its biological activity, both antiviral and antitumor, for comparison with the veterinary interferon available on the market, feline omega interferon (rFeIFN-ω, Virbagen Omega®). Recombinant rCaIFN-α7 expressed in Sf9 cell culture was purified in a single step by immobilized metal ion chromatography, yielding 4.43 mg/l with 95% purity. The purified rCaIFN-α7 showed antiviral activity against the canine kidney cell line MDCK (NBL-2, Madin Darby canine kidney) derived from Canis lupus familiaris kidney (ATCC NBL-2) infected with Vesicular Stomatitis Virus (VSV, New Jersey strain), with a recovery of 5.34 × 10⁷ AU/ml after purification. Furthermore, rCaIFN-α7 exhibited antitumor activity against canine mucosal melanoma cell lines Ak and Bk. In a typical scale-up process using 200 Rachiplusia nu larvae, biologically active rCaIFN-α7 was obtained, showing an antiviral titer of 4.5 × 10⁷ AU/ml and a yield of 5.36 × 10⁶ AU/g of larvae. This product also showed antitumor activity against canine mucosal melanoma cell line Mc and a high degree of purity from the starting sample, but a yield of 20%, probably due to aggregation or degradation events leading to a decrease in biological activity.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"101"},"PeriodicalIF":2.1,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145039117","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}