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学者姓名：林娟
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Abstract ：
Baeyer-Villiger monooxygenases (BVMOs) can catalyze the asymmetric sulfoxidation to form pharmaceutical prazoles in environmentally friendly approach. In this work, the thermostable BVMO named PockeMO had high sulfoxidation activity towards rabeprazole sulfide to form (R)-rabeprazole but demonstrated significant overoxidation activity to form undesired sulfone by-product. To address this issue, the enzyme was engineered based on the computer assisted comparison for the substrate binding conformations. A mutant S482Y/L532Q (MU2) was obtained with much alleviated overoxidation activity and enhanced sulfoxidation activity towards rabeprazole sulfide. The catalytic efficiency for (R)-rabeprazole oxidation decreased 35 folds and increased 40 folds for the sulfoxidation of lansoprazole sulfide. The structural mechanism for the selectivity improvement was illuminated to find a selectivity decision pocket that was conservatively present in BVMOs composed of 4 loops. In upscaled reaction system, the substrate loading for MU2 increased from 40 mM to 100 mM for the synthesis of enantiopure (R)-rabeprazole. The sulfone content decreased from 16.6 % to 1.2 % compared to PockeMO. Lansoprazole sulfide could also be fully converted into enantiopure (R)-lansoprazole at 50 mM in 4 h by MU2 while PockeMO almost did not have activity. This work indicated the synthetic applicability of MU2 for active pharmaceutical (R)-prazoles.
Keyword ：
Baeyer-Villiger monooxygenase Baeyer-Villiger monooxygenase ( R )-prazole ( R )-prazole Substrate selectivity Substrate selectivity
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| GB/T 7714 | Xu, Xinqi , Xu, Fahui , Chen, Jingjing et al. Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 296 . |
| MLA | Xu, Xinqi et al. "Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 296 (2025) . |
| APA | Xu, Xinqi , Xu, Fahui , Chen, Jingjing , Wang, Shumin , Wang, Xialian , Su, Bingmei et al. Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 296 . |
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Hydroxytyrosol, a naturally occurring chemical with antioxidant and antiviral properties, is widely used in the nutrition, pharmaceutical, and cosmetic industries. In the present study, a modularized cascade composed of Modules 1 and 2 was designed and implemented to convert L-tyrosine to hydroxytyrosol. Module 1 was a fourenzymatic cascade for converting L-tyrosine to tyrosol. Engineering Module 1 by fine-tuning the expression of the desired enzymes resulted in a robust whole-cell catalyst, BL21 (M1-13), which converted L-tyrosine to tyrosol at high substrate loading. Module 2 involved a 4-hydroxyphenylacetate 3-monooxygenase (HpaBC)-catalyzed reaction to hydroxylate tyrosol to form hydroxytyrosol. The rational design of the HpaB subunit led to a positive variant, HpaB-Mu (T292S/R474A), which was subsequently applied to Module 2 for tyrosol hydroxylation, yielding a robust whole-cell catalyst, BL21 (M2-05). The two designed modules were merged for one-pot conversion of L-tyrosine to hydroxytyrosol by adjusting the ratio and total amount of whole-cell catalyst loading, capable of converting 40 mM of L-tyrosine to 35.8 mM of hydroxytyrosol with a high space-time yield (1.38 g/L/ h). The current study proved that engineering HpaB at the substrate tunnel was a feasible way to boost its activity and proposed an effective method for synthesizing hydroxytyrosol from low-cost substrates, which has great economic potential.
Keyword ：
Enzymatic cascade Enzymatic cascade HpaB HpaB Hydroxytyrosol Hydroxytyrosol Rational design Rational design
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| GB/T 7714 | Liu, Wen-Kai , Ren, Xiu-Xin , Xu, Lian et al. Modular cascade with engineered HpaB for efficient synthesis of hydroxytyrosol [J]. | BIOORGANIC CHEMISTRY , 2025 , 155 . |
| MLA | Liu, Wen-Kai et al. "Modular cascade with engineered HpaB for efficient synthesis of hydroxytyrosol" . | BIOORGANIC CHEMISTRY 155 (2025) . |
| APA | Liu, Wen-Kai , Ren, Xiu-Xin , Xu, Lian , Lin, Juan . Modular cascade with engineered HpaB for efficient synthesis of hydroxytyrosol . | BIOORGANIC CHEMISTRY , 2025 , 155 . |
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4-Acetoxy-azacyclobutanone (4AA) is a highly demanded chemical compound used in the production of Penem and Carbapenem antibiotics. However, its synthesis is constrained by the preparation of methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate [(2S,3R)-BHME]. In light of stringent environmental regulations, there is an urgent need to develop an effective enzymatic method using 2-benzoylaminomethyl-3-oxy-butyrate methyl ester (BOME) as the substrate. This study mined a carbonyl reductase AxSDR from Algoriella xinjiangensis, which asymmetrically reduces BOME to (2S,3R)-BHME using isopropanol (IPA) as a cosubstrate. The mechanisms underlying the high stereoselectivity, substrate selectivity, and limited activity of AxSDR toward BOME were analyzed using computer-aided technology. Based on these analyses, AxSDR was rationally designed, leading to the identification of a triple-point variant, G94T/H145Y/Y188L (Mu3), which exhibited a 2-fold increase in catalytic efficiency. After condition optimization, Mu3 cells were able to convert 300 mM BOME, achieving a space-time yield of 15.1 g/L/h. The sustainability of the (2S,3R)-BHME biosynthesis method was further enhanced by immobilizing Mu3 on IPA-tolerant amino resin. The space-time yield of the immobilized enzyme Mu3-imm increased to 75.3 g/(Lh) and was maintained at 50.2 g/(Lh) after 100 uses. These results demonstrate the significant industrial application potential of Mu3-imm in reducing the costs and environmental risks associated with the preparation of (2S,3R)-BHME and its downstream products such as 4-AA, Penem, and Carbapenem antibiotics.
Keyword ：
asymmetrically reduction asymmetrically reduction carbonyl reductases carbonyl reductases immobilization immobilization methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate rational design rational design sustainability sustainability
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| GB/T 7714 | Meng, Fengwei , Su, Bingmei , Lin, Juan . Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase [J]. | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (2) : 767-777 . |
| MLA | Meng, Fengwei et al. "Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase" . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING 13 . 2 (2025) : 767-777 . |
| APA | Meng, Fengwei , Su, Bingmei , Lin, Juan . Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (2) , 767-777 . |
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5-Hydroxytryptophan (5-HTP) is widely used as a natural remedy for sleep disorders. In terms of biosafety, bio-derived 5-HTP is preferred over chemically synthesized 5-HTP. However, the low titer of 5-HTP in the reported microbiological methods (< 10 g/L) limits the industrialization of 5-HTP biosynthesis. In the present study, a Trp-accumulating E. coli strain TRP1 was constructed by blocking the degradation path (Delta tnaA), branching paths (Delta pheA, Delta tyrA) and repression system (Delta trpR, Delta trpL). Next, the hydroxylation module employing a phenylalanine hydroxylase mutant XcPAH(W179F) (XC2) coupled with an MH4 regenerating system (CvPCD-EcFolM system) was screened to convert L-Trp into 5-HTP. Protein engineering was performed on hydroxylase XC2 based on the molecular dynamics simulation of the enzyme-substrate complex, and the strain TRP1-XC4 harboring the triple-mutant XcPAH(L98I/A129K/W179F) (XC4) was able to produce 319.4 mg/L 5-HTP. Genome editing was carried out focused on accelerating product efflux (strengthening YddG) and increasing MH4 supply (strengthening FolM, FolE and FolX), resulting in a strain TRP5-XC4 to produce 13.9 g/L 5-HTP in 5 L fed-batch fermentation with a space-time yield of 0.29 g/L/h, which is the highest production and productivity record for 5-HTP biosynthesis. This study successfully provided an engineered strain and an efficient green method for the industrial synthesis of 5-HTP. [GRAPHICS] .
Keyword ：
5-Hydroxytryptophan 5-Hydroxytryptophan Cofactor engineering Cofactor engineering Genome editing Genome editing Phenylalanine hydroxylase Phenylalanine hydroxylase Protein engineering Protein engineering
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| GB/T 7714 | Ai, Yulin , Huang, Yusong , Zhao, Hongru et al. Engineered phenylalanine hydroxylase coupled with an effective cofactor synthesis and regeneration system for high-yield production of 5-hydroxytryptophan [J]. | BIORESOURCES AND BIOPROCESSING , 2025 , 12 (1) . |
| MLA | Ai, Yulin et al. "Engineered phenylalanine hydroxylase coupled with an effective cofactor synthesis and regeneration system for high-yield production of 5-hydroxytryptophan" . | BIORESOURCES AND BIOPROCESSING 12 . 1 (2025) . |
| APA | Ai, Yulin , Huang, Yusong , Zhao, Hongru , Su, Bingmei , Lin, Juan . Engineered phenylalanine hydroxylase coupled with an effective cofactor synthesis and regeneration system for high-yield production of 5-hydroxytryptophan . | BIORESOURCES AND BIOPROCESSING , 2025 , 12 (1) . |
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Ectoine, so-called tetrahydropyrimidine, is an important osmotic adjustment solute and widely applied in cosmetics and protein protectant. Some attempts have been made to improve the ectoine productivity. However, the strains with both high ectoine production capacity and high glucose conversion were still absent so far. Aim to construct a strain for efficiently producing ectoine, ectoine synthetic gene cluster ectABC from Pseudomonas stutzeri was overexpressed in E. coli BL21 (DE3). The ection production was improved by 382 % (ectoine titer increased from 1.73 g/L to 8.33 g/L) after the rational design of rate-limiting enzyme L-2,4-diaminobutyrate transaminase EctBps (protein engineering) combined with the metabolic engineering that focused on the enrichment and conversion of precursors. The final strain YW20 was applied to overproduce ectoine in fed-batch fermentation and yield 68.9 g/L of ectoine with 0.88 g/L/h of space-time yield and the highest glucose conversion reported [34 % (g/g)]. From the fermentation broth, ectoine was purified with 99.7 % purity and 79.8 % yield. This study successfully provided an engineered strain as well as an efficient method for the industrial biosynthesis and preparation of ectoine.
Keyword ：
Ectoine Ectoine L-2,4-diaminobutyrate transaminase L-2,4-diaminobutyrate transaminase Metabolic engineering Metabolic engineering
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| GB/T 7714 | Su, Bingmei , Yang, Wen , Zhou, Yi et al. Efficiently manufacturing ectoine via metabolic engineering and protein engineering of L-2,4-diaminobutyrate transaminase [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
| MLA | Su, Bingmei et al. "Efficiently manufacturing ectoine via metabolic engineering and protein engineering of L-2,4-diaminobutyrate transaminase" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 275 (2024) . |
| APA | Su, Bingmei , Yang, Wen , Zhou, Yi , Lin, Juan . Efficiently manufacturing ectoine via metabolic engineering and protein engineering of L-2,4-diaminobutyrate transaminase . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
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Hydroxytyrosol, a naturally occurring compound with antioxidant and antiviral activity, is widely applied in the cosmetic, food, and nutraceutical industries. The development of a biocatalytic approach for producing hydroxytyrosol from simple and readily accessible substrates remains a challenge. Here, we designed and implemented an effective biocatalytic cascade to obtain hydroxytyrosol from 3,4-dihydroxybenzaldehyde and l-threonine via a four-step enzymatic cascade composed of seven enzymes. To prevent cross-reactions and protein expression burden caused by multiple enzymes expressed in a single cell, the designed enzymatic cascade was divided into two modules and catalyzed in a stepwise manner. The first module (FM) assisted the assembly of 3,4-dihydroxybenzaldehyde and l-threonine into (2S,3R)-2-amino-3-(3,4-dihydroxyphenyl)-3-hydroxypropanoic acid, and the second module (SM) entailed converting (2S,3R)-2-amino-3-(3,4-dihydroxyphenyl)-3-hydroxypropanoic acid into hydroxytyrosol. Each module was cloned into Escherichia coli BL21 (DE3) and engineered in parallel by fine-tuning enzyme expression, resulting in two engineered whole-cell catalyst modules, BL21(FM01) and BL21(SM13), capable of converting 30 mM 3,4-dihydroxybenzaldehyde to 28.7 mM hydroxytyrosol with a high space-time yield (0.88 g/L/h). To summarize, the current study proposes a simple and effective approach for biosynthesizing hydroxytyrosol from low-cost substrates and thus has great potential for industrial applications.
Keyword ：
Biocatalytic cascade Biocatalytic cascade hydroxytyrosol hydroxytyrosol stepwisecatalysis stepwisecatalysis
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| GB/T 7714 | Liu, Wen-Kai , Su, Bing-Mei , Xu, Xin-Qi et al. Multienzymatic Cascade for Synthesis of Hydroxytyrosol via Two-Stage Biocatalysis [J]. | JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY , 2024 , 72 (27) : 15293-15300 . |
| MLA | Liu, Wen-Kai et al. "Multienzymatic Cascade for Synthesis of Hydroxytyrosol via Two-Stage Biocatalysis" . | JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 72 . 27 (2024) : 15293-15300 . |
| APA | Liu, Wen-Kai , Su, Bing-Mei , Xu, Xin-Qi , Xu, Lian , Lin, Juan . Multienzymatic Cascade for Synthesis of Hydroxytyrosol via Two-Stage Biocatalysis . | JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY , 2024 , 72 (27) , 15293-15300 . |
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Esomeprazole is the most popular proton pump inhibitor for treating gastroesophageal reflux disease. Previously, a phenylacetone monooxygenase mutant LnPAMOmu15 (LM15) was obtained by protein engineering for asymmetric synthesis of esomeprazole using pyrmetazole as substrate. To scale up the whole cell asymmetric synthesis of esomeprazole and reduce the cost, in this work, an Escherichia coli whole-cell catalyst harboring LM15 and formate dehydrogenase from Burkholderia stabilis 15516 (BstFDH) were constructed through optimized gene assembly patterns. CRISPR/Cas9 mediated insertion of P-trc promoter in genome was done to enhance the expression of key genes to increase the cellular NADP supply in the whole cell catalyst, by which the amount of externally added NADP(+) for the asymmetric synthesis of esomeprazole decreased to 0.05 mM from 0.3 mM for reducing the cost. After the optimization of reaction conditions in the reactor, the scalable synthesis of esomeprazole was performed using the efficient LM15-BstFDH whole-cell as catalyst, which showed the highest reported space-time yield of 3.28 g/L/h with 50 mM of pyrmetazole loading. Isolation procedure was conducted to obtain esomeprazole sodium of 99.55 % purity and > 99.9 % ee with 90.1 % isolation yield. This work provides the basis for production of enantio-pure esomeprazole via cost-effective whole cell biocatalysis.
Keyword ：
Asymmetric sulfoxidation Asymmetric sulfoxidation Cofactor engineering Cofactor engineering CRISPR/Cas9 CRISPR/Cas9 Esomeprazole Esomeprazole Whole-cell catalysis Whole-cell catalysis
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| GB/T 7714 | Xu, Xinqi , Meng, Yaping , Su, Bingmei et al. Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway [J]. | ENZYME AND MICROBIAL TECHNOLOGY , 2024 , 179 . |
| MLA | Xu, Xinqi et al. "Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway" . | ENZYME AND MICROBIAL TECHNOLOGY 179 (2024) . |
| APA | Xu, Xinqi , Meng, Yaping , Su, Bingmei , Lin, Juan . Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway . | ENZYME AND MICROBIAL TECHNOLOGY , 2024 , 179 . |
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Laccases act as green catalysts for oxidative cross-coupling of phenolic antioxidnt compounds, but low stability and non-recyclability limit its application. To address that, metal-organic frameworks Cu-BTC and Cr-MOF were synthesized as supports to immobilize the efficient laccase from Cerrena sp. HYB07. The Brunauer-Emmett-Teller surface area of Cu-BTC and Cr-MOF were 1213.2 and 907.1 m2/g, respectively. The two carriers respectively presented pore diameters of 1.2-10 nm and 1.4-12 nm as octahedron, indicating nano-scale mesoporosity. These Cu-BTC and Cr-MOF carriers could adsorb laccase with enzyme loading of 1933.2 and 1564.4 U/g carrier, respectively. The stability and organic solvent tolerance of Cu-BTC-laccase and Cr-MOF-laccase were both obviously improved compared to free laccase. Thermal inactivation kinetics showed that both the two immobilized laccases displayed lower thermal inactivation rate constants. Importantly, the Cu-BTC-laccase and Cr-MOF-laccase both showed much higher activity for cross-coupling of ethyl ferulate than free laccase, which had 2.5-fold higher cross-coupling efficiency than that by free laccase. The ethyl ferulate coupling product was also analyzed by mass spectroscopy and the synthesis pathway of ethyl ferulate dimer was proposed. The cross coupling of ethyl ferulate required the formation of radical intermediates of ethyl ferulate generated by laccase mediated oxidation. This work paved the way for MOFs immobilized laccase for cross coupling of antioxidant phenols.
Keyword ：
Ethyl ferulate cross-coupling Ethyl ferulate cross-coupling Laccase immobilization Laccase immobilization Metal-organic frameworks Metal-organic frameworks
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| GB/T 7714 | Xu, Xinqi , Shen, Feng , Lv, Gan et al. Immobilization of laccase on mesoporous metal organic frameworks for efficient cross-coupling of ethyl ferulate [J]. | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY , 2024 , 40 (10) . |
| MLA | Xu, Xinqi et al. "Immobilization of laccase on mesoporous metal organic frameworks for efficient cross-coupling of ethyl ferulate" . | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY 40 . 10 (2024) . |
| APA | Xu, Xinqi , Shen, Feng , Lv, Gan , Lin, Juan . Immobilization of laccase on mesoporous metal organic frameworks for efficient cross-coupling of ethyl ferulate . | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY , 2024 , 40 (10) . |
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Organofluorine compounds find extensive application in the fields of agrochemicals, pharmaceuticals, materials science, and molecular imaging. Introducing fluorine atoms can provide organic compounds with unique physicochemical properties or improve their biological activity. Although significant progress has been made in the chemical synthesis of fluorine-containing compounds, achieving selective fluorination under mild conditions remains extremely challenging. Introducing biocatalytic approaches in organofluorine chemistry is an important strategy given their high efficiency, selectivity, and environmental friendliness. In this review, we present the discovery of fluorinated natural products and fluorinases, the crystal structure and the directed evolution of fluorinases, with a focus on recent advances in the enzymatic synthesis of fluorine-containing compounds in recent years. It is hoped that this review will help to promote the field of biocatalytic organofluorine compound synthesis. Organofluorine compounds play a crucial role in agrochemicals, pharmaceuticals, and materials science. Biocatalysis has emerged as an essential strategy in the synthesis of fluorinated molecules under mild conditions. This review mainly focused on recent advances in the enzymatic synthesis of fluorine-containing compounds. Furthermore, the identification of fluorinated natural products and fluorinases, the crystal structure and the directed evolution of fluorinases were discussed. image
Keyword ：
C-F bond C-F bond enzyme enzyme fluorinase fluorinase fluorinated compounds fluorinated compounds fluorination fluorination
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| GB/T 7714 | Lin, Yuqi , Xue, Wanqing , Li, Hechen et al. Advances in Enzymatic Incorporation of Small Fluorine Modules [J]. | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY , 2024 , 27 (17) . |
| MLA | Lin, Yuqi et al. "Advances in Enzymatic Incorporation of Small Fluorine Modules" . | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY 27 . 17 (2024) . |
| APA | Lin, Yuqi , Xue, Wanqing , Li, Hechen , Su, Bingmei , Lin, Juan , Ye, Ke-Yin . Advances in Enzymatic Incorporation of Small Fluorine Modules . | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY , 2024 , 27 (17) . |
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The synthesis of steroids is challenging through multistep steroidal core modifications with high site-selectivity and productivity. In this work, a novel enzymatic cascade system was constructed for synthesis of testolactone by specific C17 lactonization/A1-dehydrogenation from inexpensive androstenedione using an engineered polycyclic ketone monooxygenase (PockeMO) and an appropriate 3-ketosteroid-A1-dehydrogenase (ReKstD). The focused saturation mutagenesis in the substrate binding pocket was implemented for evolution of PockeMO to eliminate the bottleneck effect. A best mutant MU3 (I225L/L226V/L532Y) was obtained with 20-fold higher specific activity compared to PockeMO. The catalytic efficiency (kcat/Km) of MU3 was 171-fold higher and the substrate scope shifted to polycyclic ketones. Molecular dynamic simulations suggested that the activity was improved by stabilization of the pre-lactonization state and generation of productive orientation of 4-AD mediated by distal L532Y mutation. Based on that, the three genes, MU3, ReKstD and a ketoreductase for NADPH regeneration, were rationally integrated in one cell via expression fine-tuning to form the efficient single cell catalyst E. coli S9. The single whole-cell biocatalytic process was scaled up and could generate 9.0 g/L testolactone with the high space time yield of 1 g/L/h without steroidal by-product, indicating the potential for site-specific and one-pot synthesis of steroid.
Keyword ：
Enzymatic cascade Enzymatic cascade Gene co-expression tuning Gene co-expression tuning Polycyclic ketone monooxygenase Polycyclic ketone monooxygenase Protein engineering Protein engineering Testolactone Testolactone
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| GB/T 7714 | Xu, Xinqi , Zhong, Jinchang , Su, Bingmei et al. Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
| MLA | Xu, Xinqi et al. "Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 275 (2024) . |
| APA | Xu, Xinqi , Zhong, Jinchang , Su, Bingmei , Xu, Lian , Hong, Xiaokun , Lin, Juan . Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
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