Biotechnology Letters最新文献

{"title":"Quantitative analysis of genome truncation patterns in oversized adeno-associated virus vectors.","authors":"Yifan Yang, Dongxin Wang, Yun Yuan, Chun Zhang, Xiaomei Liu","doi":"10.1007/s10529-026-03687-8","DOIUrl":"10.1007/s10529-026-03687-8","url":null,"abstract":"<p><p>Adeno-associated virus (AAV), a 4.7 kb single-stranded DNA virus, is widely used as a gene therapy vector, but its limited packaging capacity poses challenges for delivering large genes, always resulting in truncation during packaging. Quantifying truncation is difficult because both strands of the plasmid can be packaged from the 3' end. In this article, we aim to first produce single-polarity AAV and then explore its truncation pattern. To address this, we modified one of the ITRs and created an oversized self-complementary AAV, which functions as a single-polarity vector to some extent. Using this modified backbone, we generated a series of oversized single-polarity AAV (spAAV) vectors of varying lengths and sequences, analyzing DNA truncation patterns via quantitative PCR (qPCR). The results show that as the distance from the 3'-ITR increased, less DNA was detected. At 3000 bp from the 3'-ITR, 70% of the genomic DNA remained; this dropped to 50% at 4000 bp, 20% at 4500 bp, and almost none beyond 5000 bp. Additionally, reporter gene expression significantly decreased when the expression cassette extended to 4.5 kb compared to 2.7 kb under identical in vitro conditions. Our results show that DNA will be truncated far earlier before 4.5 kb during the packaging of very large genomes. This study provides important insights into the truncation patterns of AAV genomes, which is crucial for optimizing AAV vector design in gene therapy.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"27"},"PeriodicalIF":2.1,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146099582","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 and production optimization of genistein by the novel endophytic fungus Aspergillus sydowii J11 isolated from pigeon pea (Cajanus cajan) and its antibacterial and antioxidant properties.","authors":"Bin-Bin Li, Xuexia Gao, Min Lv, Wen-Juan Ning, Jing-Tao Liang, Xin-Yu Fan, Xin-Ming Lv, Jin-Feng Song, Xiao-Han Yuan, Cheng-Bo Gu","doi":"10.1007/s10529-025-03685-2","DOIUrl":"10.1007/s10529-025-03685-2","url":null,"abstract":"<p><p>Genistein, a bioactive isoflavone predominantly found in legumes, has garnered considerable attention for its diverse health-promoting benefits. Given the limitations of conventional plant extraction and chemical synthesis, microbial production offers a sustainable and efficient alternative. Endophytic fungi represent a promising reservoir of bioactive metabolites. However, reports on genistein-producing fungal endophytes remain scarce. In this study, the genistein-producing capabilities of endophytes isolated from pigeon pea (Cajanus cajan) were investigated. Five endophytes including three strains of Fusarium solani (G6, G34, G38), F. oxysporum (G44), and Aspergillus sydowii (J11), were identified as novel genistein producers, with A. sydowii J11 being the most effective. Genistein was identified through UV spectroscopy, HPLC, UPLC-MS/MS, and NMR analysis. Under optimized fermentation conditions (potato dextrose broth supplemented with 2% fructose and 1% beef extract, pH 6.0, 28 °C, 10 days), A. sydowii J11 produced genistein at 128.85 mg/L-a 5.4-fold increase over the baseline and the highest microbial genistein yield reported to date. The fungal-derived genistein demonstrated potent antibacterial activity against Staphylococcus aureus and Bacillus subtilis (MIC = 6.25 mg/L), and moderate activity against Escherichia coli and Serratia marcescens (MIC = 12.5 mg/L). Additionally, it exhibited significant antioxidant capacity, with an EC₅₀ of 156.81 mg/L in the DPPH assay. These findings position A. sydowii J11 as a promising candidate for large-scale genistein production and a natural source of antibacterial and antioxidant agents for food and pharmaceutical applications. This work represents the first report of genistein biosynthesis by endophytic fungi from pigeon pea, highlighting the potential of A. sydowii J11 as a sustainable microbial platform for high-yield genistein production.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"26"},"PeriodicalIF":2.1,"publicationDate":"2026-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146083999","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":"Discovery of a multi-epitope tuberculosis vaccine targeting phospholipase C virulence factors: an insilico approach.","authors":"Bhavin Maru, Ashish Shah","doi":"10.1007/s10529-026-03690-z","DOIUrl":"10.1007/s10529-026-03690-z","url":null,"abstract":"<p><p>Phospholipase C enzymes (plcA, plcB, plcC) represent critical virulence determination in mycobacterium tuberculosis pathogenesis. These enzymes play pivotal roles in disrupting phagosomal maturation, inducing macrophage necrosis, and facilitating immune evasion mechanisms. Protein sequences of phospholipase C gene plcA, plcB,plcC were collected and screened against human to exclude homologous matches and minimize cross-reactivity. Linear B-cell epitopes and T cell epitopes were identified and evaluated for the ability to produce strong antigenicity, solubility, toxicity and allergenicity. Suitable segments were linked using EAAK for adjuvant fusion, GPGPG between T-cell epitopes, and AAY between cytotoxin T-cell epitopes, with the L7/L12 ribosomal proteins at N-terminus as immunostimulatory adjuvant, The full vaccine structures were modelled in 3-D and improved for accuracy, and interaction of tuberculosis related proteins were analysed. Immunological potent epitopes for all 3 phospholipase C enzymes with favourable physiochemical properties and structural stability were identified. Immune simulation predicted effective stimulation of both humoral and cell-mediated responses. Molecular docking revealed promising interactions with key targets, characterized by favourable binding energies and stable complex formation dominated by hydrogen bonds and electrostatic interactions, suggesting potential functional efficacy of the designed vaccine. The study presents a strong potential of rationally designed multi-epitope vaccine candidate targeting phospholipase C virulence factor of M. tuberculosis. The computational workflow established a rigorous selection process for immunologically relevant epitopes assembled into chimeric construct with predicted vaccine potential. Further experimental validation through invitro antigenicity assay and in-vivo immunization studies is needed to assess the translational potential of this computationally designed vaccine.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"25"},"PeriodicalIF":2.1,"publicationDate":"2026-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146050404","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":"High-cell-density cultivation of Vibrio natriegens N5.3 on chitin monomers: a step toward chitin valorization.","authors":"Tuan Le, Thanh-Hung Nguyen, Duc-Chien Vu, Tran-Ha-Trang Cao, Oanh Thi-Kieu Vu, Tien-Thanh Nguyen, Tuan-Anh Pham, Thanh-Ha Le","doi":"10.1007/s10529-026-03696-7","DOIUrl":"10.1007/s10529-026-03696-7","url":null,"abstract":"<p><p>Chitin valorization through microbial bioprocessing relies on efficient utilization of its monomeric units as fermentation substrates. In this study, the effects of salt concentration and the mixing ratio of N-acetylglucosamine (GlcNAc) to glucosamine hydrochloride (GlcN·HCl) on the specific growth rate of our previously isolated V. natriegens N5.3 was investigated in the shake-flask. Batch and fed-batch fermentations using chitin-derived amino sugars were further performed to assess high-cell-density cultivation potential.Although the maximum specific growth rate ( <math><msub><mi>μ</mi> <mrow><mi>max</mi></mrow> </msub> </math> ) at 60 g/L NaCl was nearly two-fold lower than that at the optimal concentration of 15 g/L, strain N5.3 retained robust growth with <math><msub><mi>μ</mi> <mrow><mi>max</mi></mrow> </msub> </math> values of 0.37 h^-1 on GlcN·HCl and 0.66 h^-1 on GlcNAc. Fed-batch cultivation yielded a maximum cell dry weight (CDW) of 42.3 g/L within 9 h on GlcNAc, with <math><msub><mi>μ</mi> <mrow><mi>max</mi></mrow> </msub> </math> of 0.53 h^-1, but with a low biomass yield ( <math><msub><mi>Y</mi> <mrow><mi>X</mi> <mo>/</mo> <mi>S</mi></mrow> </msub> </math> = 0.16 g/g). In contrast, a substrate mixture containing 5% (w/w) GlcNAc and 95% (w/w) GlcN·HCl maintained a high <math><msub><mi>μ</mi> <mrow><mi>max</mi></mrow> </msub> </math> (0.49 h^-1) while substantially improving <math><msub><mi>Y</mi> <mrow><mi>X</mi> <mo>/</mo> <mi>S</mi></mrow> </msub> </math> (0.29 g/g), resulting in a CDW of 35.5 g/L after 9 h. Due to low solubility of both amino sugars, exponential feeding with non-sterilized powders was successfully applied. The absence of contamination demonstrate the feasibility of this approach. These results demonstrate that the mixture of GlcNAc:GlcN·HCl (1:19 ratio) is effective substrate for cultivation of V. natriegens N5.3. This provides a promising foundation for the microbial conversion of chitin-derived feedstocks into high-value products.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"24"},"PeriodicalIF":2.1,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146028356","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":"Preparation, characterization, and enzymatic properties of laccase immobilized on MnO₂ nanoparticles via adsorption method.","authors":"Wanlei Yue, Xin Wang, Zixin Gao, Jiale Zhang, Jia Bao, Mengqin Yao","doi":"10.1007/s10529-026-03694-9","DOIUrl":"10.1007/s10529-026-03694-9","url":null,"abstract":"<p><p>Laccase is an environmentally friendly biocatalyst widely used in wastewater treatment, the food industry, and biosensors. However, free laccase is susceptible to environmental factors such as pH and temperature. Immobilizing it on nanomaterials can significantly mitigate these issues. This approach also enhances the reusability of laccase, demonstrating broad application prospects. Four different morphologies of MnO₂ were compared, with δ-MnO₂ (sheet) demonstrating the most effective immobilization effect as a carrier. Under conditions of pH=5, 30 °C, and laccase concentration of 1 mg/L, the reaction achieves optimal immobilization after 4 h of adsorption. Characterization of δ-MnO₂ and immobilized laccase was performed using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The enzymatic properties of immobilized laccase were also investigated. The results indicate that the optimal temperature for immobilized laccase is 75 °C, with an optimal pH of 3. Compared to free laccase, stability has been significantly enhanced. Furthermore, even after 30 days of storage at -4 °C the relative enzyme activity of the immobilized laccase remained as high as 74.51%. The kinetic constants demonstrate that immobilized laccase not only enhances the maximum reaction rate but also significantly improves substrate affinity. Compared to free laccase, the relative enzyme activity of MnO₂-immobilized laccase (MnO₂@Lac) is significantly enhanced. This may be attributed to the synergistic effect between MnO₂ nanoparticles and laccase during substrate conversion. This study creates favorable conditions for the further application of immobilized laccase in the treatment of organic pollutants.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"23"},"PeriodicalIF":2.1,"publicationDate":"2026-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146017146","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":"Assessment of glycanolytic enzymes producing potentialities of three strains of Penicillium sp.","authors":"Nabanita Kundu, Dilruba Khatun, Ashutosh Kundu, Vivekananda Mandal","doi":"10.1007/s10529-026-03695-8","DOIUrl":"10.1007/s10529-026-03695-8","url":null,"abstract":"<p><p>Strains of Penicillium sp. are known to produce various enzymes with industrial relevance. The primary objective of the study is to determine the glycanolytic enzyme-producing potentialities of three Penicillium sp. strains, viz. PDF4, XDF1(i), and XDF7(iii), and to optimize the enzyme production and activity at different pH and temperatures. The efficacy of enzyme production and enzyme activities was tested both qualitatively and quantitatively using different glycan and lignocellulosic substrates under varying pH and temperature conditions. Among the strains, Penicillium oxalicum strain XDF7(iii) (ITS: OR555781; NL: OR555751) was the highest pectinase producer (0.303547 μmol mL^-1min^-1) at pH 3.0 in YP-pectin medium. It also exhibited the highest xylanase activity (0.768501 μmol mL^-1min^-1) in YP-xylan medium at pH 5.0. In contrast, all strains were poor producers of CMCase in all culture conditions. The strain XDF7(iii) also effectively utilized both Musambi peel (MP) and Sugarcane bagasse (SB) and recorded the highest xylanase activity (1.0912764 μmol mL^-1min^-1) and pectinase activity (0.8576 μmol mL^-1min^-1) on the 3^rd day of incubation on MP. Thus, the study concludes that these new environmental strains of Penicillium sp. can produce a high amount of industrial enzymes, such as xylanase and pectinase, under standard fermentation conditions. Furthermore, the low-cost lignocellulose biomass MP could be utilized for large-scale xylanase and pectinase production.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"22"},"PeriodicalIF":2.1,"publicationDate":"2026-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145958584","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":"Biosynthesis of the fragrance compound cinnamyl isobutyrate in Escherichia coli.","authors":"Moshi Liu, Jun Tang, Yanqiao Xue, Huiping Bi, Tao Liu","doi":"10.1007/s10529-026-03692-x","DOIUrl":"10.1007/s10529-026-03692-x","url":null,"abstract":"<p><p>Biosynthesis of the fragrance compound cinnamyl isobutyrate was achieved in Escherichia coli through acyltransferase selection and artificial pathway construction.The acyltransferase CATec3 Y20F responsible for cinnamyl isobutyrate formation was identified. Genes involved in cinnamyl alcohol biosynthesis, including Arabidopsis thaliana phenylalanine ammonia-lyase (AtPAL), Hypericum calycinum cinnamate:CoA ligase (HcCNL), Lolium perenne cinnamyl-CoA reductase (LpCCR1), and the branched-chain α-keto acid dehydrogenase complex (BKD) for isobutyryl-CoA biosynthesis, were introduced along with CATec3 Y20F into E. coli BL21 (DE3). The resulting recombinant strain, BD02, produced 2.6 mg/L cinnamyl isobutyrate and 428.9 mg/L cinnamyl acetate. Subsequently, alsS (encoding acetolactate synthase) from Bacillus subtilis and ilvC (encoding ketol-acid reductoisomerase)/ilvD (encoding dihydroxyacid dehydratase) from E. coli were overexpressed to increase the isobutyryl-CoA level, generating the recombinant strain BD03, which achieved a cinnamyl isobutyrate titer of 7.5 mg/L and 112.4 mg/L of cinnamyl acetate. Thereafter, the panB gene (encoding 3-methyl-2-oxobutanoate hydroxymethyltransferase), the pfkA gene (encoding phosphofructokinase), and the mdh gene (encoding malate dehydrogenase) were knocked out to enhance the supply of isobutyryl-CoA, resulting in the recombinant strain BD04. The strain BD04 produced 17.7 mg/L of cinnamyl isobutyrate and 67.2 mg/L of cinnamyl acetate. De novo biosynthesis of cinnamyl isobutyrate was achieved for the first time in engineered E. coli, thereby establishing a proof-of-concept for its microbial biosynthesis. This process was accompanied by the generation of cinnamyl acetate, which provides a reference for the microbial synthesis of diverse cinnamyl esters.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"21"},"PeriodicalIF":2.1,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145951338","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 a GH5 β-1, 4-endo-glucanase from Bacillus subtilis ZS57 and its potential application in brewing industry and agricultural straws saccharification.","authors":"Hongmei Zhang, Minggui Gong, Hang Li, Hangyu Hu","doi":"10.1007/s10529-026-03691-y","DOIUrl":"10.1007/s10529-026-03691-y","url":null,"abstract":"<p><p>To evaluate a novel β-1, 4-endo-glucanase, BsEgl5A, from the bacterium Bacillus subtilis ZS57 isolated from forest soil. The β-1, 4-endo-glucanase (BsEgl5A) gene was cloned and heterogeneously expressed in Escherichia coli. BsEgl5A contained a catalytic domain of glycoside hydrolase family 5 and shared 71% identity with β-1, 4-endo-glucanase from Bacillus sp. IARI-SP-4. The purified endoglucanase had a molecular weight of 55 kDa, as estimated by SDS-PAGE and western blotting. The enzyme exhibited maximum activity at 55℃ and pH 5.0, and showed remarkable stability at 70℃ and pH 3.0-7.0. The activity of BsEgl5A was improved by Mn²⁺ ions and inhibited in the presence of Cu²⁺ ions. BsEgl5A was highly active towards laminarin and barley β-glucan, moderately towards CMC-Na. BsEgl5A degraded cellotetrose, cellopentose and cellohexaose to cellotriose and cellobiose. Moreover, BsEgl5A reduced both the filtration time and the viscosity of the brewer mash. Among tested agricultural straws, BsEgl5A showed highest reducing sugars production (3.54 mg/mL) with corn straw. These characteristics make BsEgl5A as useful candidate for degradation of plant biomass to simple sugars in brewing industry and biofuel production.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"20"},"PeriodicalIF":2.1,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145951362","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":"Metabolic engineering of Bacillus subtilis for enhanced free heme biosynthesis by an enzyme-chassis co-optimization strategy.","authors":"Shuoqi Diao, Haoqiang Zhou, Yang Li, Jingcheng Dai, Dazhong Yan, Jing Wu","doi":"10.1007/s10529-025-03686-1","DOIUrl":"10.1007/s10529-025-03686-1","url":null,"abstract":"<p><p>Heme, an iron-incorporated porphyrin compound, serves as the prosthetic group for numerous proteins involved in diverse biological processes. The prokaryotic heme biosynthetic pathway features a complex cascade of reactions, in which glutamyl-tRNA reductase (GluTR) catalyzes the formation of 5-aminolevulinic acid (ALA) that represents a critical rate-limiting step and determines ultimate heme yield. In this study, OsGluTR^A510V showed enhanced heme synthesis capacity in Oryza sativa and was used for developing microbial cell factories dedicated to free heme production. Through systematic protein engineering involving site-directed mutagenesis and N-terminal modification, OsGluTR^A510V was optimized to improve the structural stability and catalytic efficiency. It yielded the recombinant enzyme GluTR^{A510V/S189T/KK}, which achieved a maximum heme titer of 13.14 mg/L in Escherichia coli, representing a 7.6-fold improvement over that of GluTR^A510V. To establish heme production in Bacillus subtilis, GluTR^{A510V/S189T/KK} was introduced into the ΔhmoAB-hemX chassis, a modified B. subtilis host lacking key heme biosynthesis inhibitors (hmoA, hmoB, and hemX). This engineered system elevated the heme yield from 0.77 to 3.86 mg/L, achieving a 5.0-fold improvement. This study demonstrates a combinatory metabolic engineering strategy that reconstitutes the heme synthetic route in B. subtilis, enabling efficient production of food-grade free heme through enzyme engineering and chassis optimization.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"19"},"PeriodicalIF":2.1,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145951336","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: Inhibition effects of amino acids on polyphenol oxidase activity isolated from medlar fruit.","authors":"Eren Özdemir, Çiğdem Bilen, Emine Karakuş","doi":"10.1007/s10529-026-03689-6","DOIUrl":"10.1007/s10529-026-03689-6","url":null,"abstract":"","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"48 1","pages":"18"},"PeriodicalIF":2.1,"publicationDate":"2026-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145931970","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}