Enzyme and Microbial Technology最新文献

{"title":"Psychrophilic insights into petroleum degradation: Gene abundance dynamics","authors":"Hongfei Zhu ,&nbsp;Xiaoshuang Mao ,&nbsp;Shahdev Sajnani ,&nbsp;Haimei Yang ,&nbsp;Ting Li ,&nbsp;Siqi Tan","doi":"10.1016/j.enzmictec.2025.110642","DOIUrl":"10.1016/j.enzmictec.2025.110642","url":null,"abstract":"<div><div>Petroleum degradation by psychrophiles can be enhanced on the basis of omics analyses, which offer better sensitivity than traditional biochemical methods do. A metagenomic analysis focusing on gene abundance comparisons may provide new guidance to optimize soil decontamination under cold environmental conditions. The soil used in this study was sampled from Dalian, from which an indigenous consortium was isolated. The degradative soil systems, initially categorized into control (DLC) and experimental (DLD) groups, were kept at room temperature (20 ± 5 °C) for six weeks. The DLD group was subsequently transferred to a low-temperature environment (5–10 °C) for 90 days and renamed DDL. A petroleum removal rate of 74.59 % was achieved in the process from DLD to DDL groups. Each soil sample was subjected to analysis and metagenomic sequencing. The abundance of genes of interest was compared between pathways to determine trends. The findings demonstrate that psychrophilic degradation is more effective than natural remediation is. The soil microbial community structure displayed site specificity, with 802 genes in DDL associated with 249 pathways, indicating greater abundance of psychrophilic genes in DDL than in DLC. The abundance of key genes was at different orders of magnitude but showed similar trends. The abundance of genes associated with hydrocarbon-related metabolism surpassed that of genes associated with sphingolipid, fatty acid, or benzene metabolism. This study provides valuable insights into psychrophilic microbe-driven petroleum degradation and indicates the need for precise supplementation of biosurfactants to improve remediation efficiency.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110642"},"PeriodicalIF":3.4,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143759310","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Preparation, and enzymatic activity analysis of an engineered capping enzyme","authors":"Zi-Ru Wang,&nbsp;Ling-Ting Li,&nbsp;Fei-Fei Xiong,&nbsp;Li-Bin Zhao,&nbsp;Hui Mao,&nbsp;Man-Yi Zhu,&nbsp;Si-Yuan Su,&nbsp;Zi-Yu Guo,&nbsp;Cheng He","doi":"10.1016/j.enzmictec.2025.110640","DOIUrl":"10.1016/j.enzmictec.2025.110640","url":null,"abstract":"<div><div>The Vaccinia capping enzyme (VCE) and the 2’-O-methyltransferase (VP39) are proteins encoded by the vaccinia virus genome, used for capping viral mRNA to form m⁷GpppN²Me mRNA (Cap1 mRNA). This capping structure is essential for protecting mRNA from degradation, facilitating pre-mRNA splicing and nuclear export, and enabling translation initiation by the eukaryotic initiation factor (eIF4E). Moreover, it helps the virus circumvent innate immune responses, thereby facilitating replication using host cell mechanisms. Currently, the enzymatic capping process employs VCE and VP39 in concert with pre-mRNA to synthesize Cap1 mRNA directly. This study introduces an engineered fusion capping enzyme , created by linking VCE and VP39 via a flexible (GGGGS)₃ linker(D1R-D12L-GS linker-VP39, DDGSV). The aim is to enhance the capping reaction while reducing raw material costs, process complexity, and impurities. The tertiary structure of DDGSV, predicted using AlphaFold2, aligns well with published structures of VCE and VP39, demonstrating no steric hindrance at the enzymatic active sites resulting from the fusion configuration. The expression vector pTolo-EX2-DDGSV was constructed and expressed in <em>Escherichia coli</em> BL21(DE3). The mRNA of the prepared capping enzymes exhibited good integrity on an agarose gel. The capping efficiency of the engineered enzyme DDGSV reached 80.19 % after 2 h of the capping reaction, matching the performance of commercial capping enzymes. Furthermore, the potential of RNA dot blotting for rapid detection of mRNA capping efficiency was explored; however, quantitative methods are also needed. Additionally, GFP mRNA prepared using DDGSV demonstrated high expression levels in HEK 293 T cells. These results indicate that the engineered enzyme can effectively cap Cap1 mRNA, providing a novel approach for mRNA vaccine development.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110640"},"PeriodicalIF":3.4,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143783097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Improved thermal stability of manganese superoxide dismutase from Staphylococcus equorum through formation of artificial oligomer","authors":"Ratna Annisa Utami ,&nbsp;Muhammad Dika Fadillah ,&nbsp;Nanik Aryani Putri ,&nbsp;Hiromi Yoshida ,&nbsp;Debbie Soefie Retnoningrum ,&nbsp;Anita Artarini ,&nbsp;Wangsa Tirta Ismaya","doi":"10.1016/j.enzmictec.2025.110641","DOIUrl":"10.1016/j.enzmictec.2025.110641","url":null,"abstract":"<div><div>Manganese superoxide dismutase (MnSOD) is an important enzyme to remove reactive oxygen species (ROS). It is active as a dimer, but increasing the temperature leads to dimer dissociation, which in turn reduces enzyme activity. In <em>Staphylococcus equorum</em> MnSOD, the dimer dissociates at approximately 55°C, while the monomer unfolds at around 67°C. Previous attempts to strengthen interactions at the dimer interface have typically resulted in reduced enzyme activity and/or reduced stability. Recently, introducing an additional interaction near the interface successfully raised the dimer dissociation temperature. However, since this interaction was non-covalent, the monomers still separated at high temperatures. To prevent dissociation, a covalent bond might be required. Here, we show that introducing intermolecular disulfide bonds by the D47C and D47CE115C mutations promoted oligomer formation. The mutant enzymes exhibited enhanced resistance to dissociation, significantly improved the dimer’s thermal stability, and retained enzymatic activity compared to the wild type, maintaining their functional integrity at high temperature, thus paving the way for application of the enzyme in biotechnology and medicine.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110641"},"PeriodicalIF":3.4,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Prodigiosin As N-heterocyclic compound: Production optimization, bioactivity evaluation, and in-silico docking against key enzymes related to inflammation, obesity, diabetes, and the insulin signaling pathway","authors":"Walaa I. El-Sofany ,&nbsp;Tahani D. Alanezi ,&nbsp;Salman Latif ,&nbsp;Ola Abdelhedi ,&nbsp;Khaled Hamden","doi":"10.1016/j.enzmictec.2025.110639","DOIUrl":"10.1016/j.enzmictec.2025.110639","url":null,"abstract":"<div><div>Diabetes is known to cause severe pancreatic inflammation and reduce insulin levels, leading us to investigate the effects of prodigiosin (PG), a red, heterocyclic bacterial compound extracted from Serratia marcescens. The physicochemical and nutritional conditions, along with the extraction solvents for PG, have been optimized for efficient production. PG was produced through bacterial culture, purified by high-performance liquid chromatography (HPLC) and thin-layer chromatography (TLC), characterized by Fourier-transform infrared spectroscopy (FTIR) and ultraviolet (UV) spectroscopy. <em>In vitro</em>, PG effectively inhibited key inflammatory enzymes, such as phospholipase A2 (PLA2) and elastase (ELA), in a dose-dependent manner, achieving maximum inhibition rates of 85.3 and 91.4 % at concentrations of 320 µg/mL, with IC₅₀ values of 63 µg/mL and 54.7 µg/mL, respectively. PG also exhibited a maximum inhibition of 82.4 % for myeloperoxidase (MPO) at a concentration of 160 µg/mL, with an IC₅₀ value of 25.9 µg/mL. This indicates that PG is a good candidate for treating these two metabolic diseases. Moreover, PG shows a significant ability to activate insulin signaling through its capacity to stimulate protein tyrosine phosphatase 1B (PTP1B) and inhibit dipeptidyl peptidase-4 (DPP-4), with IC₅₀ values of 67 and 28 µg/mL, respectively, compared to the specific inhibitors CLM and STG (with IC₅₀ values of 19 and 27 µg/mL, respectively). These powerful affinities, stability, and the durability of PG inhibition of these enzymes are confirmed by the determination of binding energy, ligand efficiency, and estimated inhibition constant (Ki). Conclusion: PG benefits from sustainable, cost-effective biological production and exhibits potent anti-inflammatory, antioxidant, and anti-diabetic properties, positioning it as a promising candidate for pharmaceutical and food applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110639"},"PeriodicalIF":3.4,"publicationDate":"2025-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767925","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhancing catalytic activity of thermostable 4-α-glucanotransferase from Thermus filiformis through semi-rational design","authors":"Qian Wang ,&nbsp;Jiao Li ,&nbsp;Heyue Li ,&nbsp;Jingyu Zhang ,&nbsp;Erbing Hua ,&nbsp;Huimin Qin ,&nbsp;Peng Chen ,&nbsp;Yuanxia Sun","doi":"10.1016/j.enzmictec.2025.110631","DOIUrl":"10.1016/j.enzmictec.2025.110631","url":null,"abstract":"<div><div>4-α-glucanotransferases (4GT) are valuable enzymatic tools with application in the food and pharmaceutical industries, particularly for producing thermoreversible starch gels. The screening of thermostable 4GT enzymes with high catalytic activity presents a significant challenge. In this study, a comprehensive screening of potential 4GT in the UniProt database led to the identification of a 4GT from <em>Thermus filiformis</em> (TfGT) with superior catalytic activity and thermal stability. To further improve its catalytic efficiency, a semi-rational design approach based on protein sequence conservation analysis was employed. The optimized mutant, M3 (Q60S/Y452I/R455K), exhibited a 3.76-fold increase in specific activity compared to the wild type (WT) enzyme and retained more than 50 % of its activity after incubation at 70 ℃ for 24 h. Additionally, molecular dynamics simulations revealed that the enhanced activity of M3 was largely due to the reshaping of the substrate tunnel, which facilitated substrate entry to the active pocket and promoted the reaction. This study not only provides a robust approach for enhancing 4GT enzyme performance but also paves the way for broader industrial applications of 4GT enzymes.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110631"},"PeriodicalIF":3.4,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143786304","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chemical modification and immobilization of cellulase for simultaneous pretreatment and saccharification of lignocellulosic biomass in ternary deep eutectic solvent","authors":"Yue Zhang ,&nbsp;Chi Lei ,&nbsp;Liangzhi Li ,&nbsp;Bin Zou ,&nbsp;Tao Xu ,&nbsp;Lishi Yan","doi":"10.1016/j.enzmictec.2025.110638","DOIUrl":"10.1016/j.enzmictec.2025.110638","url":null,"abstract":"<div><div>In this study, chemical modification coupled with immobilization of cellulase was developed for simultaneous pretreatment and saccharification (SPS) of lignocellulosic biomass in ternary deep eutectic solvent (DES). Cellulase was firstly modified with acid anhydrides to form citraconic anhydride modified cellulase (CA-Ce) and phthalic anhydride modified cellulase (PA-Ce), respectively. Then the modified cellulases were immobilized on amino-functionalized mesoporous silica nanoparticles (MSN-NH₂) to fabricate CA-Ce@MSN-NH₂ and PA-Ce@MSN-NH₂. A series of physiochemical characterizations were employed to characterize modified cellulases or immobilization carriers. Thermodynamic analysis and deactivation kinetics in ternary DES (NMMO/Bet/OA) revealed that CA-Ce@MSN-NH₂ had desired thermal stability and solvent tolerance, which maintained 80.5 % initial activity at 70 °C and 77.8 % initial activity in 50 % NMMO/Bet/OA. The SPS of bagasse in NMMO/Bet/OA via CA-Ce@MSN-NH₂ resulted in 84.1 % total reducing sugar (TRS) yield at optimal condition.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110638"},"PeriodicalIF":3.4,"publicationDate":"2025-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143725344","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Simultaneous production of linear α-olefins and 2,5-furandicarboxylic acid by combining two recombinant enzymes OleT-ELP and HMFO-ELP","authors":"Yaqi Fu ,&nbsp;Siyu Mao ,&nbsp;Tianyue Liao ,&nbsp;Wei Feng","doi":"10.1016/j.enzmictec.2025.110637","DOIUrl":"10.1016/j.enzmictec.2025.110637","url":null,"abstract":"<div><div>The enzyme OleT can utilize H₂O₂ as the co-substrate, and this biocatalysis is an H₂O₂-driven enzymatic catalysis. In this work, OleT was recombinated by being fused to an elastin-like polypeptide (ELP). The recombinant enzyme OleT-ELP exhibits higher stability and resistance to H₂O₂ interference compared to native OleT. OleT-ELP showed improved catalytic efficiency in producing α-olefins via fatty acid decarboxylation. The recombinant 5-hydroxymethylfurfural oxidase <strong>(</strong>HMFO-ELP) catalyzes the oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-furandicarboxylic acid (FDCA), generating H₂O₂ as a byproduct. Combining OleT-ELP with HMFO-ELP enabled simultaneous conversion of fatty acids and HMF. The <em>in situ</em> H₂O₂ generated by HMFO-ELP was transferred to OleT-ELP, enhancing catalytic efficiencies for both α-olefins and FDCA production.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110637"},"PeriodicalIF":3.4,"publicationDate":"2025-03-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143724520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alcalase immobilization in iota-carrageenan-matrix hydrogel beads derived from the macroalga Solieria filiformis","authors":"Alan Portal D'Almeida ,&nbsp;Luciana Rocha Barros Gonçalves ,&nbsp;Tiago Lima de Albuqueque da Silva ,&nbsp;Roberto Fernandez-Lafuente ,&nbsp;Ivanildo José da Silva Jr.","doi":"10.1016/j.enzmictec.2025.110636","DOIUrl":"10.1016/j.enzmictec.2025.110636","url":null,"abstract":"<div><div>This study aims to immobilize <em>Bacillus licheniformis</em> (Alcalase) protease in iota-carrageenan (ιCAR) matrix hydrogels via adsorption. CAR was extracted from macroalgae <em>Solieria filiformis</em> and used to produce hydrogels using Al^3 + as the gelling agent. Subsequently, enzyme immobilization was performed at 25ºC, for 120 min using particles of ∼2.0 mm diameter, varying the medium pH values (7.0, 8.0, and 9.0). The immobilization at pH 8.0 resulted in the biocatalyst with the highest immobilization yield (100 %), expressed activity (88.9 %), and mass activity (10.4 U/g) for 1.0 mg/g of enzyme loading. When using particles with different diameters (1.0, 2.0, and 3.0 mm), the best results were obtained using 1.0 mm particles. This permitted a 100 % immobilization yield, 95.8 % expressed activity, and high mass activity (11.2 U/g). The lyophilized biocatalyst presented varying macro-pore diameters, ranging from 21 to 126 µm. The immobilized biocatalyst was 11 times more stable than the soluble enzyme at 60ºC and pH 8.0 and presented &gt; 80 % retained activity in the pH range 6.0–9.0.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110636"},"PeriodicalIF":3.4,"publicationDate":"2025-03-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143704153","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Catalytic tunnel engineering of thermostable endoglucanase of GH7 family (W356C) from Aspergillus fumigatus gains catalytic rate","authors":"Musaddique Hossain,&nbsp;Subba Reddy Dodda,&nbsp;Shalini Das,&nbsp;Kaustav Aikat,&nbsp;Sudit S. Mukhopadhyay","doi":"10.1016/j.enzmictec.2025.110632","DOIUrl":"10.1016/j.enzmictec.2025.110632","url":null,"abstract":"<div><div>Tunnel engineering targets the access tunnels in enzymes, which is crucial for substrate binding and product release. Modifying the tunnels can lead to better biomass-degrading abilities of the lignocellulolytic enzymes. In this report, we have engineered the thermostable GH7 family endoglucanase from <em>Aspergillus fumigatus</em> (<em>Af</em>Egl7). The residues in the open tunnel having the highest bottleneck radius are mutated. Mutations are created (T229F, W356C) in the non-conserved region. The mutant W356C showed a 2-fold increase in product release rate (V_max = 375.8 µM/min) and 2.5-fold higher catalytic activity (K_cat = 75.1 min⁻¹) compared to wild-type (V_max= 232 µM/min; K_cat = 30.9 min⁻¹) using CM cellulose as substrate. The mutant T229F lost both catalytic activity and thermostability. Molecular dynamic simulations and docking studies of W356C revealed a change in structure near the product exit region, which may facilitate faster product release and account for the increased catalytic efficiency of the mutant. This study showed how redesigning the access pathways can be a promising strategy for protein engineering and <em>de novo</em> protein design by tailoring the open tunnel geometry to a ligand-specific manner.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"187 ","pages":"Article 110632"},"PeriodicalIF":3.4,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143697986","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biodegradation of crude oil by newly enriched biosurfactant-producing bacterial consortium","authors":"Jinhui Liu ,&nbsp;Yuke kong ,&nbsp;Junchao Pan ,&nbsp;Mengjiao Qiao ,&nbsp;Xinling Ruan ,&nbsp;Yangyang Wang","doi":"10.1016/j.enzmictec.2025.110635","DOIUrl":"10.1016/j.enzmictec.2025.110635","url":null,"abstract":"<div><div>Crude oil contamination in different environmental media is a global environmental problem, biodegradation is a potential, environmentally friendly method for remediating this pollutant. In the present study, a biosurfactant-producing and crude oil degrading bacterial consortium (S1) was enriched from a contaminated soil, and its degradation efficiency of crude oil in solution and soil under the optimum conditions was studied. The results showed that the predominant species of S1 were <em>Pseudomonadaceae</em> and <em>Alcaligenaceae</em>. S1 could produce surfactant, with the maximum content of 2.27 g/L, which was identified as rhamnolipids. The optimal pH, temperature, and (NH₄)₂SO₄ concentration for crude oil degradation were 7.0, 40 °C, and 3 g/L, respectively, with the maximum degradation efficiency of 51.51 % after 7 days incubation. Plackett-Burman experiment and response surface methodology demonstrated that Cu, Co, and Zn could significantly promote the degradation of crude oil, with their optimum concentration of 0.36, 0.88, and 0.60 mg/L, respectively. Under the optimum conditions, the highest crude oil degradation efficiency reached 53.23 % within 7 days. Kinetic analysis showed that the first-order reaction kinetic was suitable for describing the degradation of crude oil by S1, with a half-life of 4.57 days. Furthermore, S1 also could degrade the crude oil in soil efficiently, with the maximum degradation efficiency of 60.34 % within 56 days. These results indicate that S1 has great potential for practical application in remediation of crude oil contamination.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"187 ","pages":"Article 110635"},"PeriodicalIF":3.4,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143697984","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}