{"title":"Application of wood sawdust microbial transformation for the utilization of long-term stored bark-wood waste.","authors":"Ludmila Aleksandrovna Belovezhets, Dmitry Sergeevich Belousov, Nadezhda Vladimirovna Filinova, Ekaterina Olegovna Pristavka, Aleksey Aleksandrovich Pristavka","doi":"10.1007/s10529-026-03730-8","DOIUrl":"10.1007/s10529-026-03730-8","url":null,"abstract":"<p><p>The issue of bark-wood waste (BWW) utilization is challenging for the regions adjacent to pulp and paper mills. Bark is difficult to recycle, and the additives used in paper production further complicate this process. This work focuses on the potential application of wood sawdust microbial transformation, the technology of which was developed at the Irkutsk Institute of Chemistry SB RAS, for the processing of bark-wood waste into environmentally safe soil. Laboratory experiments revealed that long-term stored BWW can undergo microbial degradation. The best results were obtained with the BWW/sawdust mixture. The substrate neutralization conditions were selected to simultaneously lower the pH and introduce the necessary mineral additives for microbial function. A semi-industrial experiment with a BWW/sawdust mixture of 20 m<sup>3</sup> (3:1 ratio) was performed. The experiment demonstrated that pH stabilization occurred more efficiently than in the laboratory experiment. A temperature increase, which is characteristic of aerobic processing of lignocellulosic waste was also observed. The product obtained was non-toxic to both plants and Chlorella vulgaris (hazard class 5). The processing improved of the agrochemical parameters of the substrate, such as hydrolytic acidity, cation exchange capacity, and the sum of absorbed bases. The increase in humic acid content indicates a deep microbial degradation of the lignin component of BWW. Consequently, the microbial transformation of BWW was successfully implemented to produce a non-toxic soil. This technology can be scaled up for large volumes of BWW at storage sites.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 3","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147643537","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}
Priyanka Sonar, K R Mathuvanti, Amoha Venkataramanan, Harish Reddy, Abhishek Mohanty
{"title":"Medical biotechnology and artificial intelligence powered companion diagnostics: indispensable pillars driving next generation precision health care.","authors":"Priyanka Sonar, K R Mathuvanti, Amoha Venkataramanan, Harish Reddy, Abhishek Mohanty","doi":"10.1007/s10529-026-03732-6","DOIUrl":"10.1007/s10529-026-03732-6","url":null,"abstract":"<p><p>Medical biotechnology serves as a foundational platform for identifying disease markers and developing specific diagnostic assays. Complementing this, biosensors and medical devices translate these biomarkers into quantifiable signals enabling real-time health assessment. Artificial intelligence (AI) augments this framework by processing vast datasets to recognize patterns and generate predictive insights thereby aiding clinicians in decision-making and streamlining personalized disease management. The integration of molecular-based companion diagnostics, biosensor technology, and medical AI forms the cornerstone of contemporary, data-driven precision medicine. This review explores the synergistic convergence of these fields specifically examining how AI-based approaches enhance molecular diagnostics and biosensor devices to optimize clinical outcomes. This interdisciplinary collaboration facilitates advancing precision medicine. Consequently, these discovery technologies profoundly impact disease prevention, early diagnosis, and targeted therapeutic strategies. Despite challenges such as data privacy and technology accessibility, this cross-disciplinary approach holds tremendous potential for transforming the future of precision healthcare.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 3","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147643838","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}
Soumya Mukundan, Jose Savio Melo, Archana Mishra, Kuber Chandra Bhainsa
{"title":"Isolation of Achromobacter sp. SM123 and immobilization of tributyl phosphate-degrading phosphatase enzyme for bioremediation application.","authors":"Soumya Mukundan, Jose Savio Melo, Archana Mishra, Kuber Chandra Bhainsa","doi":"10.1007/s10529-026-03726-4","DOIUrl":"10.1007/s10529-026-03726-4","url":null,"abstract":"<p><p>Tributyl phosphate (TBP) is a solvent and plasticizer commonly used in nuclear fuel reprocessing plants. However, it poses significant environmental challenges due to its stability, persistence, and unique physicochemical properties. To address this, the present study focuses on the biodegradation of TBP by an organism isolated from soil, capable of utilizing TBP as its sole carbon source. Isolated bacteria (Achromobacter sp. SM123) demonstrated efficient TBP degradation, achieving 96% degradation in 29 h following adaptation to butanol. The crude extract contains phosphatase enzyme, responsible for TBP degradation was immobilized onto hydroxyappetite matrix. Various immobilizing parameters were investigated, and storage stability study showed that the immobilized crude extract maintained 69% of its initial activity up to 65 days however the free enzyme retained only 27% activity over 23 days. The phosphatase activity present in crude extract was confirmed by zymogram analysis as a distinct purple band. This work highlights the potential application of isolated bacteria and its immobilized crude extract which contains phosphatase enzyme activity in the bioremediation of TBP-contaminated environment.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147607757","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":"Immobilized Aspergillus niger lipase over hydrogen titanate nanotubes as a biocatalyst for biodiesel production.","authors":"Fatma Ahmed, Mai Raslan, A H Zaki","doi":"10.1007/s10529-026-03710-y","DOIUrl":"10.1007/s10529-026-03710-y","url":null,"abstract":"<p><strong>Background: </strong>Immobilization of lipase enzyme is a promising approach towards cost-effective production of biodiesel to protect the enzyme from denaturation during the transesterification process.</p><p><strong>Methods: </strong>In the present study, hydrogen titanate nanotubes (HTNTs), synthesized by simple hydrothermal method, was used to immobilize lipase from Aspergillus niger via physical adsorption with the following ratios of HTNTs and lipase; 1 T: 1 L, 1 T: 0.75 L, 1 T: 0.5 L, and 1 T: 0.25 L. All prepared samples were characterized by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), and scanning electron microscopy (SEM). The catalytic activities of free and immobilized lipases were evaluated for biodiesel production using sunflower oil, methanol to oil molar ratio of 4: 1 at 40 °C for 90 min.</p><p><strong>Results: </strong>The biodiesel yields (0% water content, 0.877 g/cm<sup>3</sup> density, and 0.041 mg acid value) were 79.2 ± 0.01, 82.3 ± 0.9, 79.1 ± 1.2, 81.97 ± 1.4, 78 ± 0.1 percent for 1 T: 1 L, 1 T: 0.75 L, 1 T: 0.5 L, 1 T: 0.25 L, and free lipase (1 L), respectively. Compared with the control (1 L), immobilizing lipase using (HTNTs) enabled a 50- 75% reduction in lipase required quantity while maintaining or even increasing biodiesel production levels. The work establishes a promising method for lipase immobilization in biodiesel production that can be evaluated for large-scale application in further studies.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147526156","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":"Eco-friendly azo dye removal via a robust laccase from Acinetobacter baumannii KMSP005: a thermo-alkaliphilic biocatalytic approach.","authors":"Kalyanee Bera, Mainak Mukhopadhyay","doi":"10.1007/s10529-026-03725-5","DOIUrl":"10.1007/s10529-026-03725-5","url":null,"abstract":"<p><p>The enzymatic breakdown of synthetic azo dyes is a potential and environmentally acceptable way to remove harmful contaminants commonly produced by the textile and dye industries. In this study, laccase-producing bacteria were isolated from soil samples collected from the Eastern Himalayan region and molecularly identified as Acinetobacter baumannii KMSP005 by 16S rDNA gene sequencing. The primary objective was to optimise laccase production using response surface methodology, while a secondary objective was to evaluate the efficiency of the bacterial laccase in degrading azo dye methyl red. Under optimised conditions, ~ 96% degradation of methyl red was achieved within 18 h, with a maximum laccase activity of 3.49 IU mL⁻1. Using coconut husk, a cheap agricultural waste, as a substrate for laccase production produced an impressive enzyme activity of 4.9 IU mL⁻1. When using agro-waste, laccase production increased by about 1.40-fold. Analysis of the breakdown products using gas chromatography-mass spectrometry revealed that methyl red was changed into simpler, less toxic, mediational compounds, proving the process' effectiveness and environmental safety. The maximal activity of 2.25 IU mL⁻1 at 50 °C and 2.50 IU mL⁻1 at pH 9 demonstrated the thermostable and alkali-tolerant characteristics of this laccase. The laccase exhibited thermo-alkaliphilic stability, retaining 82.05% of its initial activity at 50 °C and 86.66% activity at pH 9.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147519702","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":"The potential of a Lactiplantibacillus plantarum strain to improve yield of tea tree seed oil through fermentation process.","authors":"Peng-Ming Yang, Jin-Zhong Jiang","doi":"10.1007/s10529-026-03724-6","DOIUrl":"10.1007/s10529-026-03724-6","url":null,"abstract":"<p><p>Great mass of tea tree seeds (TTS) are naturally rotted away as agricultural waste because there is no suitable technology used for extracting oil from TTS. The fermentation method is a new process and that can simultaneously recover oil, starch and saponins from TTS. In this study, a key bacterial strain named JJZ21 was isolated from fermented TTS milk (ground TTS and water) by the serial dilution method and identified as Lactiplantibacillus plantarum strain through molecular analyses. The production of cellulase, pectinase, amylase and protease of JJZ21 were visualized on agar plates containing specific enzyme substrates. Compared with the control, addition treatment with JJZ21 dramatically improved the activities of cellulase, pectinase, amylase and protease, reduced content of soluble sugar, protein and dry matter and pH in the TTS milk, shortened the fermentation time and increased the yield of TTS oil. Meanwhile, the addition of JJZ21 had no significant effect on quality of TTS oil. However, the yield of TTS oil decreased with excessive fermentation. Response surface methodology was used to evaluate the optimum conditions for fermentation process to obtain the maximum oil yield.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147509385","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":"Advancing the frontier of plant-based therapeutics: critical innovations in molecular farming and bioprocess Integration.","authors":"Kalidas Gowtham, Balamurugan Shanmugaraj, Lohith Saran Thangavel, Aksittha Srinivasan, Ashwini Malla","doi":"10.1007/s10529-026-03723-7","DOIUrl":"10.1007/s10529-026-03723-7","url":null,"abstract":"<p><p>Plant molecular farming (PMF) has emerged as a promising strategy for producing biopharmaceuticals and high-value biomolecules in plant systems. In this review, we present a comprehensive synthesis of current methodologies while introducing novel approaches to genetic transformation, protein expression, glycan engineering, and downstream processing. We offer in-depth analyses of recent advancements such as CRISPR/Cas9-mediated pathway editing, synthetic biology frameworks for optimizing protein yield and quality, and integrated bioprocessing solutions that enhance purification efficiency. Further, detailed case studies are discussed to illustrate actionable strategies, and future research directions are proposed to bridge current gaps. By focusing on transformative techniques and critical problem-solving perspectives, this review aims to guide researchers toward more effective and scalable PMF applications.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147502838","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":"Stability of recombinant baculoviruses for biopharmaceutical applications in chemically defined medium.","authors":"Rodrigo Jorge Atanes Netto, Fernanda Angela Correia Barrence, Júlia Públio Rabello, Milena Miyu Teruya, Vanessa Farias, Eutimio Gustavo Fernández Núñez","doi":"10.1007/s10529-026-03720-w","DOIUrl":"10.1007/s10529-026-03720-w","url":null,"abstract":"<p><p>Insect cell-baculovirus expression vector systems (IC-BEVS) are valuable tools in pharmaceutical bioprocesses for producing complex proteins like immunogenic virus-like particles. In this context, standardization is key to guarantee consistency in process yield, productivity, and product quality attributes. The study investigates the nine-month stability of the main biotechnological input used in IC-BEVS, the recombinant baculovirus vectors produced in chemically defined medium. Viral titer (pfu/mL), zeta potential (mV), and mean hydrodynamic particle size (μm), were employed to assess viral inactivation under eight combinations of generation and storage conditions. First-order, Weibull, and biphasic models were applied to describe viral decay. The critical parameters (factors) analyzed were the size of the heterologous gene inserted (719 and 1621 bp), storage temperature (- 80 and 1.5 °C), and infection time used for baculovirus batch generation (48 or 72 h post-infection). They were mainly explored according to a two-level factorial design (2<sup>3</sup>). The primary quality attribute evaluated in this study was the one-log<sub>10</sub> decay time of the viral titer (td), which exhibited an overall mean value of 80 days across eight batches. The biphasic model best fits the dispersion of the viral titer data collected over the assessed time in all considered combinations of factors and was employed to find significant factors over td values. Gene size was the only factor with a statistically significant effect on viral titer decay; additionally, the study indicates the occurrence of particle aggregation over the course of the analysis.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12999813/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147479645","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}
Olanrewaju Raji, Thu V Vuong, Nadia Davoudvandi, Emma R Master
{"title":"Oligosaccharide oxidase for the enzymatic synthesis of glucosaminic acids.","authors":"Olanrewaju Raji, Thu V Vuong, Nadia Davoudvandi, Emma R Master","doi":"10.1007/s10529-026-03721-9","DOIUrl":"10.1007/s10529-026-03721-9","url":null,"abstract":"<p><p>D-Glucosaminic acid is a valuable amino acid useful in food and medical applications. It is a highly sought after enantiopure molecule important for the synthesis of drugs and glycopeptides. Current enzymatic synthesis pathways to D-glucosaminic acid carry disadvantages such as low product yield and long reaction times. Herein, the Auxiliary Activity 7 chito-oligosaccharide oxidase from Lentinus brumalis, LbChi7A, was shown as a potent biocatalyst capable of efficiently converting D-glucosamine (GlcN) and N-acetyl-D-glucosamine (GlcNAc) to their respective C<sub>1</sub>-acids. The substrate specificity of LbChi7A towards GlcN and GlcNAc enabled the conversion of at least 90% GlcN to D-glucosaminic acid and 100% GlcNAc to N-acetyl-D-glucosaminic acid within 60 min. LbChi7A inhibition by the hydrogen peroxide co-product was not detected, even at 860 mM. This single enzymatic conversion offers a clean and efficient process to produce industrially relevant glucosaminic acids, including D-glucosaminic acid and N-acetyl-D-glucosaminic acid.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12996394/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147472585","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":"Screening of a xylanase-producing Trichoderma strain and optimization of its enzyme production conditions.","authors":"Lili Fan, Kehe Fu, Jiameng Hu, Xin Liu","doi":"10.1007/s10529-026-03718-4","DOIUrl":"10.1007/s10529-026-03718-4","url":null,"abstract":"<p><p>Xylanases have attracted considerable attention due to their strong potential for industrial use. In this study, a xylanase-producing strain isolated from soil was identified as Trichoderma semiorbis Tsejk8, and the conditions for xylanase production were optimized. Additionally, two xylanase-related genes were cloned, and their functions were analyzed. The optimal conditions for xylanase production included maltose as the carbon source, peptone as the nitrogen source, an optimal pH of 6.0, and an incubation time of 120 h, yielding an enzyme activity of 40.7 U/mL. Following the purification of xylanase via ammonium sulfate precipitation and ion exchange chromatography, four distinct protein bands were observed. Mass spectrometry analysis of these bands identified 14 associated proteins. Bioinformatics analysis revealed that two of these proteins belong to GH3 (Glycoside Hydrolase family 3) β-xylosidase. In summary, the newly isolated strain Tsejk8 exhibits xylanase activity, offering an effective and eco-friendly means of converting biomass into raw materials for industrial applications.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-03-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147466855","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}