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学者姓名：许鑫琦
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Abstract ：
Chiral sulfinamides find broad applications in bioactive compounds, chiral auxiliaries, chiral ligands, and organocatalysts. However, biocatalytic approaches for their enantioselective synthesis have rarely been explored. Herein, an efficient biocatalytic strategy for the synthesis of chiral sulfinamides via polycyclic ketone monooxygenase (PockeMO) catalyzed asymmetric oxidation of sulfenamides was reported. A diverse array of chiral sulfinamides can be readily accessed with high yields (up to >99%) and enantioselectivities (>99:1 er). Additionally, this biocatalytic platform was scalable, and the resulting synthetic chiral sulfinamides could be easily derivatized to various chiral S-stereogenic compounds. Molecular dynamics simulation studies revealed that hydrogen bonding interactions between the sulfenamides and key residues were essential for enantioselectivity control. This work unlocks a biocatalytic avenue to access chiral sulfinamides for synthetic chemistry and drug discovery.
Keyword ：
asymmetric oxidation asymmetric oxidation biocatalysis biocatalysis chiralsulfinamides chiralsulfinamides polycyclic ketone monooxygenase (PockeMO) polycyclic ketone monooxygenase (PockeMO) sulfenamides sulfenamides
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| GB/T 7714 | Xue, Wanqing , Lin, Yuqi , Lin, Xiaomin et al. Synthesis of Chiral Sulfinamides Enabled by Polycyclic Ketone Monooxygenase Catalyzed Asymmetric Oxidation of Sulfenamides [J]. | ACS CATALYSIS , 2025 , 15 (18) : 16247-16253 . |
| MLA | Xue, Wanqing et al. "Synthesis of Chiral Sulfinamides Enabled by Polycyclic Ketone Monooxygenase Catalyzed Asymmetric Oxidation of Sulfenamides" . | ACS CATALYSIS 15 . 18 (2025) : 16247-16253 . |
| APA | Xue, Wanqing , Lin, Yuqi , Lin, Xiaomin , Xu, Xinqi , Chen, Jingjing , Lin, Juan et al. Synthesis of Chiral Sulfinamides Enabled by Polycyclic Ketone Monooxygenase Catalyzed Asymmetric Oxidation of Sulfenamides . | ACS CATALYSIS , 2025 , 15 (18) , 16247-16253 . |
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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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Abstract ：
Whole-cell redox-neutral cascade reactions are promising for the sustainable synthesis of bulky lactones. In this study, the cyclohexanone monooxygenase from Acinetobacter sp. NCIMB 9871 (CHMOAc) was rationally designed based on enhancing product release and consensus sequence design to enhance the activity and stability of the enzyme. A four-point mutant MU4 (G14A/A43G/M400L/F432I) showed improved activity and stability for the oxidation of cyclohexanone to epsilon-caprolactone at a high substrate loading. A newly NADPH-dependent alcohol dehydrogenase from Pseudomonas monteilii (PmADH) with high cyclohexanol oxidation activity was introduced for constructing the redox-neutral cascade for the synthesis of epsilon-caprolactone from cyclohexanol. To improve the intracellular environment for cascade synthesis of epsilon-caprolactone, CRISPR/Cas9-mediated strong promoter insertion to the endogenous catalase gene katE in the NADP self-sufficient Escherichia coli strain BK-1 (Ptrc-nadK/Ptrc-pncB) was done for mitigating the oxidative stress to obtain the strain E. coli BKE-3 harboring MU4 and PmADH. Finally, 776 mM cyclohexanol could be converted into epsilon-caprolactone by the BKE-3 whole-cell catalytic system with a >99% conversion rate without cyclohexanone accumulation, which was the highest record for the redox-neutral cascade synthesis of epsilon-caprolactone. The BKE-3 whole-cell catalytic system also showed high efficiency for the synthesis of various lactones. This work provides an efficient redox-neutral catalytic platform for the sustainable synthesis of lactones featuring high substrate loading and atomic economy.
Keyword ：
CRISPR/Cas9genome editing CRISPR/Cas9genome editing cyclohexanone monooxygenase cyclohexanone monooxygenase enzymatic cascade enzymatic cascade epsilon-caprolactone epsilon-caprolactone protein engineering protein engineering
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| GB/T 7714 | Xu, Xinqi , Wang, Shumin , Zhong, Yaqun et al. Rational Design of Cyclohexanone Monooxygenase and a Whole-Cell System for Biocatalytic Redox-Neutral Cascade Synthesis of Lactones [J]. | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (33) : 13340-13353 . |
| MLA | Xu, Xinqi et al. "Rational Design of Cyclohexanone Monooxygenase and a Whole-Cell System for Biocatalytic Redox-Neutral Cascade Synthesis of Lactones" . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING 13 . 33 (2025) : 13340-13353 . |
| APA | Xu, Xinqi , Wang, Shumin , Zhong, Yaqun , Yang, Juanjuan , Xu, Lian , Su, Bingmei et al. Rational Design of Cyclohexanone Monooxygenase and a Whole-Cell System for Biocatalytic Redox-Neutral Cascade Synthesis of Lactones . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (33) , 13340-13353 . |
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A large quantity of orange peel waste (OPW) is generated per year, yet effective biorefinery methods are lacking. In this study, Trichosporonoides oedocephalis ATCC 16958 was employed for hydrolyzing OPW to produce soluble sugars. Glycosyl hydrolases from Paenibacillussp.LLZ1 which can hydrolyze cellulose and hemicellulose were mined and characterized, with the highest beta-mannanase activity of 39.1 U/mg at pH 6.0 and 50 degree celsius. The enzyme was overexpressed in T. oedocephalis and the sugar production was enhanced by 16 %. The accumulated sugar contains 57 % value-added mannooligosaccharides by the hydrolysis of mannans. The process was intensified by a pretreatment combining H2O2 submergence and steam explosion to remove potential inhibitors. The mannooligosaccharides yield of 6.5 g/L was achieved in flask conversion and increased to 9.7 g/L in a 5-L fermenter. This study improved the effectiveness of orange peel waste processing, and provided a hydrolysis-based methodology for the utilization of fruit wastes.
Keyword ：
beta-mannanase beta-mannanase Mannooligosaccharides Mannooligosaccharides Orange peel waste Orange peel waste Pretreatment Pretreatment Trichosporonoides oedocephalis Trichosporonoides oedocephalis
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| GB/T 7714 | Zhou, Taotao , Ju, Xin , Yan, Lishi et al. Production of mannooligosaccharides from orange peel waste with β-mannanase expressed in Trichosporonoides oedocephalis [J]. | BIORESOURCE TECHNOLOGY , 2024 , 395 . |
| MLA | Zhou, Taotao et al. "Production of mannooligosaccharides from orange peel waste with β-mannanase expressed in Trichosporonoides oedocephalis" . | BIORESOURCE TECHNOLOGY 395 (2024) . |
| APA | Zhou, Taotao , Ju, Xin , Yan, Lishi , Fang, Ruiqi , Xu, Xinqi , Li, Liangzhi . Production of mannooligosaccharides from orange peel waste with β-mannanase expressed in Trichosporonoides oedocephalis . | BIORESOURCE TECHNOLOGY , 2024 , 395 . |
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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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Norepinephrine, a kind of beta-adrenergic receptor agonist, is commonly used for treating shocks and hypotension caused by a variety of symptoms. The development of a straightforward, efficient and environmentally friendly biocatalytic route for manufacturing norepinephrine remains a challenge. Here, we designed and realized an artificial biocatalytic cascade to access norepinephrine starting from 3, 4-dihydroxybenzaldehyde and L-threonine mediated by a tailored-made L-threonine transaldolase PsLTTA-Mu1 and a newly screened tyrosine decarboxylase ErTDC. To overcome the imbalance of multi-enzymes in a single cell, engineering of PsLTTA for improved activity and fine-tuning expression mode of multi-enzymes in single E.coli cells were combined, leading to a robust whole cell biocatalyst ES07 that could produce 100 mM norepinephrine with 99% conversion, delivering a highest time-space yield (3.38 g/L/h) ever reported. To summarized, the current study proposed an effective biocatalytic approach for the synthesis of norepinephrine from low-cost substrates, paving the way for industrial applications of enzymatic norepinephrine production.
Keyword ：
Biocatalytic cascade Biocatalytic cascade L-threonine transaldolase L-threonine transaldolase Tyrosine decarboxylase Tyrosine decarboxylase
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| GB/T 7714 | Xu, Lian , Shen, Jun-Jiang , Wu, Ming et al. An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 265 . |
| MLA | Xu, Lian et al. "An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 265 (2024) . |
| APA | Xu, Lian , Shen, Jun-Jiang , Wu, Ming , Su, Bing-Mei , Xu, Xin-Qi , Lin, Juan . An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 265 . |
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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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S-omeprazole and R-rabeprazole are important proton pump inhibitors (PPIs) used for treating peptic disorders. They can be biosynthesized from the corresponding sulfide catalyzed by Baeyer-Villiger monooxygenases (BVMOs). During the development of BVMOs for target sulfoxide preparation, stereoselectivity and over- oxidation degree are important factors considered most. In the present study, LnPAMO-Mu15 designed previously and TtPAMO from Thermothelomyces thermophilus showed high (S)- and (R)-configuration stereoselectivity respectively towards thioethers. TtPAMO was found to be capable of oxidating omeprazole sulfide (OPS) and rabeprazole sulfide (RPS) into R-omeprazole and R-rabeprazole respectively. However, the overoxidation issue existed and limited the application of TtPAMO in the biosynthesis of sulfoxides. The structural mechanisms for adverse stereoselectivity between LnPAMO-Mu15 and TtPAMO towards OPS and the overoxidation of OPS by TtPAMO were revealed, based on which, TtPAMO was rationally designed focused on the flexibility of loops near catalytic sites. The variant TtPAMO-S482Y was screened out with lowest overoxidation degree towards OPS and RPS due to the decreased flexibility of catalytic center than TtPAMO. The success in this study not only proved the rationality of the overoxidation mechanism proposed in this study but also provided hints for the development of BVMOs towards thioether substrate for corresponding sulfoxide preparation.
Keyword ：
Baeyer-Villiger monooxygenase Baeyer-Villiger monooxygenase Flexibility Flexibility Overoxidation Overoxidation R-rabeprazole R-rabeprazole S-omeprazole S-omeprazole Stereoselectivity Stereoselectivity
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| GB/T 7714 | Su, Bingmei , Xu, Fahui , Zhong, Jinchang et al. Rational design on loop regions for precisely regulating flexibility of catalytic center to mitigate overoxidation of prazole sulfides by Baeyer-Villiger monooxygenase [J]. | BIOORGANIC CHEMISTRY , 2024 , 151 . |
| MLA | Su, Bingmei et al. "Rational design on loop regions for precisely regulating flexibility of catalytic center to mitigate overoxidation of prazole sulfides by Baeyer-Villiger monooxygenase" . | BIOORGANIC CHEMISTRY 151 (2024) . |
| APA | Su, Bingmei , Xu, Fahui , Zhong, Jinchang , Xu, Xinqi , Lin, Juan . Rational design on loop regions for precisely regulating flexibility of catalytic center to mitigate overoxidation of prazole sulfides by Baeyer-Villiger monooxygenase . | BIOORGANIC CHEMISTRY , 2024 , 151 . |
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Enantiopure 1,2-diols are widely used in the production of pharmaceuticals, cosmetics, and functional materials as essential building blocks or bioactive compounds. Nevertheless, developing a mild, efficient and environmentally friendly biocatalytic route for manufacturing enantiopure 1,2-diols from simple substrate remains a challenge. Here, we designed and realized a step-wise biocatalytic cascade to access chiral 1,2-diols starting from aromatic aldehyde and formaldehyde enabled by a newly mined benzaldehyde lyase from Sphingobium sp. combined with a pair of tailored-made short-chain dehydrogenase/reductase from Pseudomonas monteilii (PmSDR-MuR and PmSDR-MuS) capable of producing (R)- and (S)-1-phenylethane-1,2-diol with 99% ee. The planned biocatalytic cascade could synthesize a series of enantiopure 1,2-diols with a broad scope (16 samples), excellent conversions (94%-99%), and outstanding enantioselectivity (up to 99% ee), making it an effective technique for producing chiral 1,2-diols in a more environmentally friendly and sustainable manner. A step-wise biocatalytic cascade to access chiral 1,2-diols starting from aromatic aldehyde and formaldehyde enabled by a newly mined ThDP-dependent benzaldehyde lyase from Sphingobium sp. combined with a pair of tailored-made short-chain dehydrogenase/reductase from Pseudomonas monteilii (PmSDR-MuR and PmSDR-MuS). image
Keyword ：
benzaldehyde lyase benzaldehyde lyase chiral 1,2-diols chiral 1,2-diols rational design rational design short-chain dehydrogenase/reductase short-chain dehydrogenase/reductase
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| GB/T 7714 | Ren, Xiu-Xin , Su, Bing-Mei , Xu, Xin-Qi et al. Rational design of short-chain dehydrogenase/reductase for enantio-complementary synthesis of chiral 1,2-diols by successive hydroxymethylation and reduction of aldehydes [J]. | BIOTECHNOLOGY AND BIOENGINEERING , 2024 , 121 (12) : 3796-3807 . |
| MLA | Ren, Xiu-Xin et al. "Rational design of short-chain dehydrogenase/reductase for enantio-complementary synthesis of chiral 1,2-diols by successive hydroxymethylation and reduction of aldehydes" . | BIOTECHNOLOGY AND BIOENGINEERING 121 . 12 (2024) : 3796-3807 . |
| APA | Ren, Xiu-Xin , Su, Bing-Mei , Xu, Xin-Qi , Xu, Lian , Lin, Juan . Rational design of short-chain dehydrogenase/reductase for enantio-complementary synthesis of chiral 1,2-diols by successive hydroxymethylation and reduction of aldehydes . | BIOTECHNOLOGY AND BIOENGINEERING , 2024 , 121 (12) , 3796-3807 . |
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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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