Biotechnology Letters最新文献_第2页

Isolation of Achromobacter sp. SM123 and immobilization of tributyl phosphate-degrading phosphatase enzyme for bioremediation application. SM123无色杆菌的分离及磷酸三丁酯降解磷酸酶的固定化。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-04-02 DOI: 10.1007/s10529-026-03726-4

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":"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.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"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}

引用次数: 0

Immobilized Aspergillus niger lipase over hydrogen titanate nanotubes as a biocatalyst for biodiesel production. 钛酸氢纳米管固定化黑曲霉脂肪酶作为生物柴油生产的生物催化剂。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-27 DOI: 10.1007/s10529-026-03710-y

Fatma Ahmed, Mai Raslan, A H Zaki

{"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":"Background: Immobilization of lipase enzyme is a promising approach towards cost-effective production of biodiesel to protect the enzyme from denaturation during the transesterification process.Methods: 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.Results: The biodiesel yields (0% water content, 0.877 g/cm3 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.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"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}

引用次数: 0

Eco-friendly azo dye removal via a robust laccase from Acinetobacter baumannii KMSP005: a thermo-alkaliphilic biocatalytic approach. 利用鲍曼不动杆菌KMSP005的强力漆酶去除偶氮染料：一种热亲碱生物催化方法。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-26 DOI: 10.1007/s10529-026-03725-5

Kalyanee Bera, Mainak Mukhopadhyay

{"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":"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.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"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}

引用次数: 0

The potential of a Lactiplantibacillus plantarum strain to improve yield of tea tree seed oil through fermentation process. 一株植物乳杆菌发酵提高茶树籽油产量的潜力。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-25 DOI: 10.1007/s10529-026-03724-6

Peng-Ming Yang, Jin-Zhong Jiang

{"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":"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.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"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}

引用次数: 0

Advancing the frontier of plant-based therapeutics: critical innovations in molecular farming and bioprocess Integration. 推进植物疗法的前沿：分子农业和生物过程整合的关键创新。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-23 DOI: 10.1007/s10529-026-03723-7

Kalidas Gowtham, Balamurugan Shanmugaraj, Lohith Saran Thangavel, Aksittha Srinivasan, Ashwini Malla

引用次数: 0

Stability of recombinant baculoviruses for biopharmaceutical applications in chemically defined medium. 生物制药用重组杆状病毒在化学定义介质中的稳定性。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-18 DOI: 10.1007/s10529-026-03720-w

Rodrigo Jorge Atanes Netto, Fernanda Angela Correia Barrence, Júlia Públio Rabello, Milena Miyu Teruya, Vanessa Farias, Eutimio Gustavo Fernández Núñez

{"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":"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 (23). The primary quality attribute evaluated in this study was the one-log10 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.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"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}

引用次数: 0

Oligosaccharide oxidase for the enzymatic synthesis of glucosaminic acids. 低聚糖氧化酶，用于酶促合成氨基葡萄糖酸。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-17 DOI: 10.1007/s10529-026-03721-9

Olanrewaju Raji, Thu V Vuong, Nadia Davoudvandi, Emma R Master

引用次数: 0

Screening of a xylanase-producing Trichoderma strain and optimization of its enzyme production conditions. 产木聚糖酶木霉菌株筛选及产酶条件优化。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-16 DOI: 10.1007/s10529-026-03718-4

Lili Fan, Kehe Fu, Jiameng Hu, Xin Liu

引用次数: 0

Challenges, optimization, and delivery strategies in the heterologous expression of aldehyde dehydrogenase: therapeutic applications for acetaldehyde detoxification. 乙醛脱氢酶异源表达的挑战、优化和递送策略：乙醛解毒的治疗应用。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-15 DOI: 10.1007/s10529-026-03714-8

Siyue Qiao, Shumei Li, Tongzheng Zhang, Fan Yang, Rui Ling Zhang, Min Li

{"title":"Challenges, optimization, and delivery strategies in the heterologous expression of aldehyde dehydrogenase: therapeutic applications for acetaldehyde detoxification.","authors":"Siyue Qiao, Shumei Li, Tongzheng Zhang, Fan Yang, Rui Ling Zhang, Min Li","doi":"10.1007/s10529-026-03714-8","DOIUrl":"10.1007/s10529-026-03714-8","url":null,"abstract":"The aldehyde dehydrogenase (ALDH) superfamily plays a critical role in acetaldehyde detoxification. The mitochondrial ALDH2 isoenzyme serves as the core enzyme in alcohol metabolism because of its high affinity for acetaldehyde. Loss-of-function mutation (such as ALDH2*2) of the gene is highly prevalent in East Asian populations. These mutations cause acetaldehyde accumulation and significantly increase the risk of alcohol-related diseases. Therefore, it is necessary to develop efficient recombinant ALDH2 supplementation therapies. However, its heterologous expression faces three major bottlenecks: (1) catalytic turnover leading to NAD⁺ depletion; (2) difficulty in functional tetramer assembly; and (3) cytotoxicity of the substrate acetaldehyde, which inhibits cell growth. The review covers rational host selection and multi-level synergistic optimization of transcription, translation, folding, and metabolism. Examples include promoter optimization, codon optimization, terminator optimization, and chaperone co-expression. Ultimately, we explore essential stabilization formulations and innovative delivery strategies, such as nano-encapsulation and engineered probiotics, needed to realize the therapeutic potential of ALDH2. The goal is to promote the industrial production and clinical translation of recombinant ALDH2.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"publicationDate":"2026-03-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147455492","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}

引用次数: 0

Biomimetic mineralization of chemically modified glucose oxidase from Aspergillus niger in ZIF-8. 化学修饰的黑曲霉葡萄糖氧化酶在ZIF-8中的仿生矿化。

IF 2.1 4区生物学

Biotechnology Letters Pub Date : 2026-03-14 DOI: 10.1007/s10529-026-03722-8

Marija Stanišić, Milica Crnoglavac Popović, Marko Radenković, Branimir Bajac, Vojin Tadić, Olivera Prodanović, Radivoje Prodanović

{"title":"Biomimetic mineralization of chemically modified glucose oxidase from Aspergillus niger in ZIF-8.","authors":"Marija Stanišić, Milica Crnoglavac Popović, Marko Radenković, Branimir Bajac, Vojin Tadić, Olivera Prodanović, Radivoje Prodanović","doi":"10.1007/s10529-026-03722-8","DOIUrl":"10.1007/s10529-026-03722-8","url":null,"abstract":"Chemical surface modification of enzymes represents a powerful strategy to improve immobilization and catalytic performance. In this study, glucose oxidase (GOx) from Aspergillus niger was chemically modified via periodate oxidation and reductive amination to incorporate L-aspartate (D-GOx) and L-histidine (H-GOx) residues. These modifications enhanced electrostatic and coordinative interactions with Zn2+ and 2-methylimidazole during biomimetic mineralization, leading to efficient encapsulation in ZIF-8 frameworks. The resulting D-GOx@ZIF-8 and H-GOx@ZIF-8 biocomposites showed significantly improved activity and stability compared to native GOx. H-GOx@ZIF-8 achieved a specific activity of 4551 IU/g, representing a sixfold increase over previously reported systems. Both modified biocomposites also demonstrated greater resistance to detergent washing and retained higher activity after exposure to 65 °C, indicating stronger incorporation into the ZIF-8 matrix. These results highlight the dual advantage of introducing negatively charged and imidazole-functional groups for promoting biomineralization and improving biocatalyst robustness. This strategy provides a mild, scalable route for preparing enzyme@MOF composites with enhanced operational stability, offering direct potential for industrial bioprocesses, continuous-flow catalysis, and biosensing applications.","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 2","pages":""},"PeriodicalIF":2.1,"publicationDate":"2026-03-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147455502","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}

引用次数: 0