Query：
学者姓名：许鑫琦
Refining：
Year
Type
Indexed by
Source
Complex
Former Name
Co-
Language
Clean All
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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. © The Author(s), under exclusive licence to Springer Nature B.V. 2024.
Keyword ：
Ethyl ferulate cross-coupling Ethyl ferulate cross-coupling Laccase immobilization Laccase immobilization Metal–organic frameworks Metal–organic frameworks
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Xu, X. , Shen, F. , Lv, G. et al. Immobilization of laccase on mesoporous metal organic frameworks for efficient cross-coupling of ethyl ferulate [J]. | World Journal of Microbiology and Biotechnology , 2024 , 40 (10) . |
| MLA | Xu, X. et al. "Immobilization of laccase on mesoporous metal organic frameworks for efficient cross-coupling of ethyl ferulate" . | World Journal of Microbiology and Biotechnology 40 . 10 (2024) . |
| APA | Xu, X. , Shen, F. , Lv, G. , Lin, J. . Immobilization of laccase on mesoporous metal organic frameworks for efficient cross-coupling of ethyl ferulate . | World Journal of Microbiology and Biotechnology , 2024 , 40 (10) . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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 Ptrc 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. © 2024
Keyword ：
Asymmetric sulfoxidation Asymmetric sulfoxidation Cofactor engineering Cofactor engineering CRISPR/Cas9 CRISPR/Cas9 Esomeprazole Esomeprazole Whole-cell catalysis Whole-cell catalysis
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Xu, X. , Meng, Y. , Su, B. 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, X. 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, X. , Meng, Y. , Su, B. , Lin, J. . Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway . | Enzyme and Microbial Technology , 2024 , 179 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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) . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
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
Cite：
Copy from the list or Export to your reference management。
| 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 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Export
| Results： |
Selected to |
| Format： |
