{"title":"[Advances in automated enrichment and directed domestication technologies and their applications in the development of environmental functional microorganisms].","authors":"Jiawei Jiang, Zhilin Xing, Tiantao Zhao, Ailing Chen","doi":"10.13345/j.cjb.260466","DOIUrl":"https://doi.org/10.13345/j.cjb.260466","url":null,"abstract":"<p><p>Environmental functional microorganisms play a key role in environmental engineering processes such as pollutant degradation, wastewater treatment, and resource utilization. Conventional enrichment and directed domestication technologies often have limitations such as long operational cycles and low throughput, being difficult to meet the demands for rapid screening, enhancement, and engineering application of functional microorganisms under complex environmental conditions. In recent years, advances in continuous cultivation, high-throughput cultivation, microfluidic chips, intelligent bioreactors, and automated adaptive laboratory evolution (ALE) have provided new approaches for the precise screening, targeted enhancement, and feedback-based process control of environmental functional microorganisms. This review systematically summarizes the basic principles and key platforms of automated enrichment and directed domestication technologies, as well as their application progress in the development of microorganisms for petroleum hydrocarbon and polycyclic aromatic hydrocarbon degradation, wastewater denitrification, heavy metal tolerance, and emerging contaminant degradation. In addition, by integrating our research group's work on targeted environmental microorganism isolation devices, programmable logic controller (PLC)-driven ALE systems, and the screening of functional strains for halogenated organic pollutant degradation, this review analyzes the current limitations of these technologies in <i>in situ</i> simulation, maintenance of mixed microbial community interactions, screening of non-growth-coupled phenotypes, and engineering scale-up. Finally, future directions are proposed for the application of automated enrichment and directed acclimation technologies in the exploration, functional enhancement, and engineering application of environmental functional microbial resources. This review is expected to provide theoretical and methodological support for improving the technological framework of environmental functional microorganism development and facilitating its translation into engineering practice.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"3970-3985"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149026046","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Screening of highly active recombinant bovine enterokinase mutants mediated by green fluorescent protein and its soluble expression in <i>Escherichia coli</i>].","authors":"Changchun Han, Junhao Yue, Yuwen Tu, Zhuhua Chan, Lehe Mei, Changjiang Lyu","doi":"10.13345/j.cjb.260179","DOIUrl":"https://doi.org/10.13345/j.cjb.260179","url":null,"abstract":"<p><p>Bovine enterokinase light chain (EK<sub>L</sub>), a serine protease that specifically recognizes the Asp-Asp-Asp-Asp-Lys (DDDDK) sequence, is widely used for the specific cleavage of affinity tags in recombinant proteins. However, EK<sub>L</sub> contains multiple cysteine residues and four disulfide bonds, making it difficult to fold correctly, and it tends to form inactive inclusion bodies when expressed in <i>Escherichia coli</i>. To achieve efficient soluble expression of EK<sub>L</sub> in <i>E</i>. <i>coli</i> and screen high-activity mutants, co-expression of the DnaK-DnaJ-GrpE and GroES-GroEL molecular chaperones was adopted to enhance its solubility. Subsequently, the DDDDK sequence was site-specifically introduced into the Loop region of superfolder green fluorescent protein (sfGFP) to generate the fluorescent substrate sfGFP<sup>M</sup> for EK<sub>L</sub>. Based on the principle of fluorescence loss, a high-throughput screening method for highly active EK<sub>L</sub> variants was established. Using error-prone PCR, a random mutagenesis library of the <i>EK<sub>L</sub></i> gene was constructed, from which the EK<sub>L</sub>-S42M/I139D mutant was obtained. This mutant showed a 2.56-fold increase in catalytic efficiency and significantly improved thermostability. Molecular dynamics simulations revealed that the S42M/I139D mutations synergistically optimized the stability and activity of EK<sub>L</sub><i>via</i> distal allosteric regulation. Meanwhile, fed-batch fermentation further enhanced the soluble expression level of EK<sub>L</sub>-S42M/I139D, with a yield of 203 mg/L and an enzymatic activity of 7.45×10<sup>4</sup> U/mL. This study not only achieves the soluble expression of EK<sub>L</sub> in <i>E</i>. <i>coli</i> and obtains a highly active mutant, but also provides a visual tool for the rapid detection of EK<sub>L</sub> activity.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4038-4051"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Stability and viability optimization for filamentous microorganisms in droplet-based microfluidic screening].","authors":"Xueyan Liu, Chenggang Deng, Linlin Qi, Xiaomei Zheng, Ruitong Lv, Yanjiao Zhai, Ran Tu, Lixian Wang, Meng Wang, Jifeng Liu, Yue Zhang","doi":"10.13345/j.cjb.260126","DOIUrl":"https://doi.org/10.13345/j.cjb.260126","url":null,"abstract":"<p><p>Filamentous microorganisms-encompassing filamentous fungi and actinomycetes-are versatile cell factories for producing proteins and bioactive natural products, playing a critical role in the food and pharmaceutical industries. These microorganisms exhibit slow growth and complex morphological differentiation. Conventional screening methods for strain engineering are hindered by low throughput and an inability to resolve heterogeneity in strain cultivation and growth. Droplet-based microfluidics offers an attractive platform for high-throughput screening at the single-cell level, yet its utility is limited by poor droplet stability and low post-sorting viability. Given the aforementioned technical bottlenecks, this study aims to compare the compatibility between filamentous fungi and actinomycetes and droplet microfluidic technology, optimize post-sorting strain viability, and thereby establish a droplet microfluidic screening platform applicable to diverse filamentous microorganisms. Here, we systematically evaluated and optimized droplet-based microfluidic screening for filamentous fungi-<i>Acremonium chrysogenum</i> and two actinomycetes, <i>Streptomyces lividans</i> and <i>Saccharopolyspora erythraea</i>. Monodisperse spore-suspension preparation protocols and droplet incubation time were optimized for each organism, which revealed that actinomycete-generated droplets were significantly more stable than those of filamentous fungi, with optimal sorting windows dictated by strain-specific growth and morphological traits. Subsequently, we varied sorting voltage and recovery regimens (no treatment, demulsification, or demulsification followed by shaking incubation). Lower sorting voltage markedly improved viability, while demulsification effectively boosted viability. These targeted optimizations establish a practical workflow that converts droplet-based microfluidics into a robust tool for high-throughput screening of filamentous microorganisms.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4225-4238"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025923","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Directed evolution of amine dehydrogenase for the catalytic resolution of (1<i>R</i>,5<i>S</i>)-3-ethylbicyclo [3.2.0] hept-3-en-6-one, a chiral intermediate of mirogabalin].","authors":"Qingxia Luo, Xiaohan Zhang, Jinhui Feng, Qinggang Li, Zixiang Xu, Xi Chen, Qiaqing Wu, Dunming Zhu","doi":"10.13345/j.cjb.260241","DOIUrl":"https://doi.org/10.13345/j.cjb.260241","url":null,"abstract":"<p><p>(1<i>R</i>,5<i>S</i>)-3-ethylbicyclo[3.2.0]hept-3-en-6-one[(1<i>R</i>,5<i>S</i>)-<b>1a</b>] is the key chiral starting material for the synthesis of mirogabalin. Existing chemical and biocatalytic resolution processes both suffer from cumbersome post-processing procedures and high production costs. To achieve the efficient and green resolution of (1<i>R</i>,5<i>S</i>)-<b>1a</b>, the present study employed racemic ketone <b>1a</b> as the substrate and identified <i>Lf</i>AmDH(M0) as the template for directed evolution through enzyme library screening. The substrate binding site and the key amino acid residues around the substrate access channel were selected, and site-directed mutagenesis and iterative mutagenesis were performed in turn to construct a multi-round mutant library. Following library screening, the specific activities of the mutants were elevated to 1.3- to 5.9-fold that of the starting enzyme, demonstrating significantly optimized catalytic performance. The substrate spectrum characteristics of the starting enzyme M0 and the dominant mutants were investigated, revealing that the mutants exhibited appreciable catalytic activity and stereoselectivity toward aliphatic ketones, cyclic ketones, arylalkyl ketones and aromatic ketones. In a 50 mL reaction system, the optimal mutant L40T/L125R/V291A(M3) converted 150 mmol/L of substrate. After the reaction was completed, the product was subjected to extraction and acid washing, affording the chiral ketone with an <i>ee</i> value of 97.1% and a yield of 45.4%. This study successfully developed a novel amine dehydrogenase-catalyzed resolution approach for (1<i>R</i>,5<i>S</i>)-<b>1a</b>, which simplifies the post-processing workflow of the product and reduces the consumption of organic reagents, thereby providing robust technical support for the efficient industrial-scale biomanufacturing of (1<i>R</i>,5<i>S</i>)-<b>1a</b>.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4154-4167"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yuxi Zhang, Jing Yu, Qiuxian Wang, Jiahong Liu, Yue Zhao, Rong Fan, Zhichao Li
{"title":"[An integrated system for transient expression and stable transformation in <i>Nicotiana benthamiana</i> suspension cells].","authors":"Yuxi Zhang, Jing Yu, Qiuxian Wang, Jiahong Liu, Yue Zhao, Rong Fan, Zhichao Li","doi":"10.13345/j.cjb.260144","DOIUrl":"https://doi.org/10.13345/j.cjb.260144","url":null,"abstract":"<p><p><i>Nicotiana benthamiana</i> suspension cells, exhibiting advantages such as short growth cycles, facile genetic manipulation, ease of product purification, and suitability for large-scale cultivation, are emerging as a novel industrial biosynthesis platform for plant-derived natural products. Transient expression and stable transformation are core technologies for validating gene function and constructing plant cell factories. However, current methods have been developed primarily for whole-plant systems, systematic investigations in plant suspension cells are lacking, let alone a technological framework for integrating both approaches. Plant suspension cells, by virtue of cultivating characteristics, are suitable to develop integrated systems for transient expression and stable transformation. This study constructed an integrated system for transient expression and stable transformation (ISTS) by incorporating an efficient expression module, a transient expression enhancement module, and a stable integration screening module. ISTS enabled higher transient transformation efficiency and expression intensity in <i>N</i>. <i>benthamiana</i> suspension cells than classical pCAMBIA1300. Moreover, upon selection and cultivation of transiently expressing cells, stably transformed cell lines with efficient target gene integration and high expression levels can be obtained readily. In this study, <i>tHMGR</i>, <i>tGGPPS</i>, and <i>tTS</i> were cloned into ISTS vector individually and co-transformed into <i>N</i>. <i>benthamiana</i> suspension cells, which enabled the one-step multigene transient expression and stable integration. This approach successfully yielded taxadiene-producing tobacco cell lines. ISTS offers advantages such as simplified vector construction, fewer procedural steps, and shorter operational cycle. This work provides key technical support for establishing efficient, stable plant suspension cell factories and facilitating sustainable biosynthesis of complex natural products.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4305-4317"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149026038","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jiaxin Zhou, Haohong Lin, Xiujuan Qian, Anming Xu, Min Jiang
{"title":"[High-level expression of PET depolymerases in <i>Pichia pastoris</i> and construction of a crude enzyme stabilization system].","authors":"Jiaxin Zhou, Haohong Lin, Xiujuan Qian, Anming Xu, Min Jiang","doi":"10.13345/j.cjb.260313","DOIUrl":"https://doi.org/10.13345/j.cjb.260313","url":null,"abstract":"<p><p>Improving the production of polyethylene terephthalate (PET) depolymerases is essential for reducing the cost of enzymatic PET recycling and facilitating its industrial application. To enhance the production of PET hydrolases, the fungal-derived hydrolase HiC and the bacterial-derived hydrolase LCC<sup>ICCG</sup> were employed as model enzymes. Strategies including recombinant strain construction, gene copy number optimization, molecular chaperone-assisted expression, fermentation scale-up, and crude enzyme stabilization were systematically investigated. The strains with secretory expression were generated by chromosomal integration, and multicopy transformants were obtained through high-stringency zeocin selection. To further improve protein production, we introduced PDI, ERO1, SEC53, SEC1, HAC1, and GCN4 as helper factors. GCN4 showed the strongest enhancement effect on HiC production, whereas ERO1 and HAC1 were more effective for LCC<sup>ICCG</sup>. No significant synergistic effect was observed when ERO1 and HAC1 were co-expressed. In 5-L bioreactors, the optimized strains achieved the titers of 2.36 g/L for HiC and 1.72 g/L for LCC<sup>ICCG</sup>. Furthermore, in a 50 L fermenter, the maximum extracellular protein concentration of HiC reached 8.5 g/L. A crude enzyme stabilization system composed of 0.1% Kathon, 10% glycerol, and 0.5% phenoxyethanol was subsequently established. After storage at room temperature for 30 days, HiC and LCC<sup>ICCG</sup> retained 56.43% and 78.11% of their initial activities, respectively. The results demonstrate that coordinated optimization of expression and formulation can improve both the production and storage stability of PET depolymerases, thereby supporting their practical application in enzymatic PET recycling.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4289-4304"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149026055","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Metabolic engineering of <i>Yarrowia lipolytica</i> for astaxanthin production].","authors":"Shuo Sun, Qun Yang, Ziyue Zhou, Yutong Fan, Yunying Zhao, Yu Deng","doi":"10.13345/j.cjb.260148","DOIUrl":"https://doi.org/10.13345/j.cjb.260148","url":null,"abstract":"<p><p>Astaxanthin, a high-value terpenoid secondary metabolite that exhibits excellent antioxidant activity, has broad application potential in the pharmaceutical and nutraceutical industries. However, its sophisticated biosynthetic pathway poses a great challenge for efficient production and industrial-scale application of astaxanthin. In this study, the unconventional oleaginous yeast <i>Yarrowia lipolytica</i> was employed as the chassis organism, and a multidimensional metabolic engineering strategy combined with fermentation process optimization was used to construct a microbial cell factory for astaxanthin production. Firstly, a heterologous β-carotene biosynthetic pathway was reconstituted, the carbon flux supply of the mevalonate (MVA) pathway was systematically enhanced, and endogenous branch metabolism was blocked, leading to the initial construction of an astaxanthin-producing strain. Subsequently, a RIDD-RIAD protein interaction tag was introduced to optimize the expression patterns of the key rate-limiting enzymes of β-carotene ketolase (CrtW) and β-carotene hydroxylase (CrtZ), thereby effectively improving the efficiency of astaxanthin biosynthesis. Following this, six rounds of iterative targeted metabolic modification combined with shake-flask fermentation significantly enhanced the biosynthetic potential of the engineered strains. The results showed that the engineered strain YAX11 achieved an astaxanthin titer of 107.4 mg/L in shake-flask fermentation, and the titer was increased to 1 148.4 mg/L in a 5 L bioreactor. Through the deep integration of metabolic network remodeling and fermentation process optimization, this study successfully constructed a <i>Y</i>. <i>lipolytica</i> cell factory for astaxanthin production, providing a theoretical reference for the green and large-scale manufacturing of astaxanthin, as well as metabolic engineering strategies for the heterologous synthesis of other terpenoid compounds.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4067-4088"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149026069","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Rational design for improving the thermostability of β-glucosidase from <i>Bacillus thermoamylovorans</i>].","authors":"Panpan Dong, Tong Liu, Keyi Xue, Ruili Wang, Yandie Wang, Modan Qi, Chunsheng Zuo, Guosi Li, Nailiang Zhu","doi":"10.13345/j.cjb.260227","DOIUrl":"https://doi.org/10.13345/j.cjb.260227","url":null,"abstract":"<p><p>The β-glucosidase from <i>Bacillus thermoamylovorans</i> (Bgl52) has been identified as a thermophilic and acidophilic β-glucosidase, which constitutes the most critical component in the cellulolytic enzyme system for cellulose hydrolysis. Although Bgl52 is a thermophilic enzyme, its poor thermal stability at high temperatures restricts its long-term industrial application under elevated-temperature conditions. In this study, rational design strategies, including two free energy calculation programs (Fireprot and FoldX) and homologous sequence alignment, were integrated to perform single-point and multi-point combinatorial mutagenesis on Bgl52. The enzymatic kinetic stability assay and molecular dynamics simulation were conducted to further investigate the catalytic performance and structural variations of positive mutants. After screening, the optimal stacked mutant M5 exhibited increases in <i>T</i><sub>m</sub>, optimal temperature, and <i>T</i><sub>50</sub> by 8.7, 10 and 8℃, respectively, compared with Bgl52 (wild type, WT), and its half-life <i>t</i><sub>1/2</sub> at 80℃ was enhanced by 32.5 folds. The catalytic efficiency (<i>K</i><sub>cat</sub>/<i>K</i><sub>m</sub>) of M5 showed a slight decrease compared with that of the wild-type enzyme. Furthermore, M5 hydrolyzed native cellulose into glucose more efficiently at the high temperature of 85℃. Structural analysis and molecular dynamics simulation revealed that the improved thermostability was attributed to increased hydrogen bonds, the proline effect, additional salt bridges, and enhanced hydrophobic interactions. The results indicate that the multi-strategy integrated rational design approach demonstrates outstanding efficiency and reliability in enzyme engineering modification, enhancing the industrial application potential of β-glucosidase.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"4195-4209"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025712","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Research progress in synthesis of cordycepin by microorganisms].","authors":"Ying Tian, Lishuangfei Chen, Yirui Liang, Qiqi Zhu, Chuanbo Zhang, Wenyu Lu","doi":"10.13345/j.cjb.260120","DOIUrl":"https://doi.org/10.13345/j.cjb.260120","url":null,"abstract":"<p><p>Cordycepin is a natural nucleoside antibiotic isolated from the fruiting bodies of <i>Cordyceps militaris</i>. It possesses diverse health-beneficial and medicinal values. However, the conventional fermentation processes for cordycepin production suffer from inherent drawbacks, including low yields, prolonged production cycles, and batch-to-batch inconsistency. These problems result in the exorbitant market price of cordycepin and severely restrict the potential for market application. The advent of synthetic biology has offered a revolutionary approach to address this challenge. This article systematically reviews the development trajectory of cordycepin production, spanning from conventional fermentation to modern synthetic biology-based manufacturing. It focuses on analyzing the breakthrough advancements in the construction of microbial cell factories such as <i>Saccharomyces cerevisiae</i> and cordycepin synthesis. Finally, it provides perspectives on the future development of more efficient, eco-friendly, and intelligent cordycepin biomanufacturing technologies by leveraging enzyme engineering and synthetic biology. And this study offers theoretical support and technical references for constructing high-cordycepin-producing strains, which is critical to facilitate the industrialization of cordycepin.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"3867-3883"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025805","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yanwei Gao, Hongxiu Xu, Chunjiang Ye, Tao Zhu, Xuefeng Lü
{"title":"[Research progress and prospects of cyanobacterial cell factories for ethylene production].","authors":"Yanwei Gao, Hongxiu Xu, Chunjiang Ye, Tao Zhu, Xuefeng Lü","doi":"10.13345/j.cjb.260210","DOIUrl":"https://doi.org/10.13345/j.cjb.260210","url":null,"abstract":"<p><p>Ethylene, a fundamental feedstock in the petrochemical industry, is conventionally produced <i>via</i> energy-intensive steam cracking of fossil fuels, a process associated with high energy consumption and carbon emissions. Constructing photosynthetic cyanobacterial cell factories for the direct, solar-driven conversion of CO<sub>2</sub> to ethylene offers a promising route for the green production of ethylene. This review systematically summarizes recent advances in this field, highlighting the core catalytic mechanism of the ethylene-forming enzyme (EFE), the screening and optimization of key genetic elements, metabolic engineering strategies (including gene copy number amplification, precursor supply enhancement, rewiring of carbon flux, and alleviation of by-product inhibition), and the optimization of cultivation processes. Furthermore, we identify the key challenges currently impeding cyanobacterial production of ethylene, such as low yields and efficiencies, insufficient genetic stability, and bottlenecks in large-scale cultivation. Finally, we outline future development directions-advancing synthetic biology tools, enabling precise regulation of metabolic networks, designing efficient photobioreactors, and integrating industrial technologies, with the aim of providing a theoretical foundation for establishing robust and high-performance cyanobacterial cell factories for ethylene production and facilitating their practical application.</p>","PeriodicalId":21778,"journal":{"name":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","volume":"42 9","pages":"3829-3845"},"PeriodicalIF":0.0,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025813","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}