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学者姓名：苏冰梅
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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
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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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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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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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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/Δ1-dehydrogenation from inexpensive androstenedione using an engineered polycyclic ketone monooxygenase (PockeMO) and an appropriate 3-ketosteroid-Δ1-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. © 2024
Keyword ：
Biosynthesis Biosynthesis Cell engineering Cell engineering Cytology Cytology Escherichia coli Escherichia coli Gene expression Gene expression Ketones Ketones Molecular dynamics Molecular dynamics Molecular orientation Molecular orientation
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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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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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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
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| 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 . |
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Dehydroepiandrosterone (DHEA) is an important neurosteroid hormone to keep human hormonal balance and reproductive health. However, DHEA was always produced with impurities either by chemical or biological method and required high-cost purification before the medical use. To address this issue, a novel chemo-enzymatic process was proposed and implemented to produce DHEA. An acetoxylated derivate of 4-androstene-3,17-dione (4-AD) was generated by chemical reaction and converted into DHEA by an enzyme cascade reaction combining a hydrolysis reaction with a reduction reaction. The hydrolysis reaction was catalyzed by a com-mercial esterase Z03 while the reduction reaction was catalyzed by E. coli cells co-expressing a 3 beta-hydroxysteroid dehydrogenase SfSDR and a glucose dehydrogenase BtGDH. After the condition optimization, DHEA was syn-thesized at a 100 mL scale under 100 mM of substrate loading and purified as white powder with the highest space-time yield (4.80 g/L/h) and purity (99 %) in the biosynthesis of DHEA. The successful attempt in this study provides a new approach for green synthesis of highly purified DHEA in the pharmaceutical industry.
Keyword ：
3?-hydroxysteroid dehydrogenase 3?-hydroxysteroid dehydrogenase Chemoenzymatic process Chemoenzymatic process Dehydroepiandrosterone Dehydroepiandrosterone Enzyme cascade Enzyme cascade Hydrolysis Hydrolysis
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| GB/T 7714 | Su, Bing-Mei , Shi, Yi-Bing , Lin, Wei et al. A chemoenzymatic process for preparation of highly purified dehydroepiandrosterone in high space-time yield [J]. | BIOORGANIC CHEMISTRY , 2023 , 133 . |
| MLA | Su, Bing-Mei et al. "A chemoenzymatic process for preparation of highly purified dehydroepiandrosterone in high space-time yield" . | BIOORGANIC CHEMISTRY 133 (2023) . |
| APA | Su, Bing-Mei , Shi, Yi-Bing , Lin, Wei , Xu, Lian , Xu, Xin-Qi , Lin, Juan . A chemoenzymatic process for preparation of highly purified dehydroepiandrosterone in high space-time yield . | BIOORGANIC CHEMISTRY , 2023 , 133 . |
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Tetrahydrofuran-3-one (3TF) was regarded as a difficult-to-reduce ketone for carbonyl reductases due to its high stereosymmetry, result of which, the biosynthesis of chiral 3-hydroxytetrahydrofuran (3HTF), a key precursor of pharmaceuticals for treatment of HIV or diabetes, has been limited. Present study mined a robust carbonyl reductase CmCR from Candida metapsilosis with high activity towards 3TF using isopropanol as co-substrate (500 mM, 22 g/L/h space-time yield, 67% ee). Based on the orientation of substrate's etheryl oxygen in the substrate binding pocket, CmCR was rationally designed and two mutants MuR and MuS were screened out to completely reduce 3TF into (R)-HTF and (S)-HTF respectively with the highest 3TF loading and productivity (200 mM, 4.4 g/ L/h space-time yield, 99% ee for MuR while 500 mM, 11 g/L/h space-time yield, 99% ee for MuS). The structural mechanism for the enhanced stereoselectivity was revealed that the mutagenesis changed the electrostatic potential surrounding the substrate entrance and promoted 3TF to approach, bind and form prereaction state with MuR or MuS in one certain direction, by which 3TF was converted into 3HTF with excellent optical purity. The success in this study provides a viable approach for rational design of carbonyl reductases with high enantioselectivity towards target substrates of high symmetry.
Keyword ：
Carbonyl reductase Carbonyl reductase Chiral 3-hydroxytetrahydrofuran Chiral 3-hydroxytetrahydrofuran Highest productivity Highest productivity Rational design Rational design Stereoselectivity Stereoselectivity
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| GB/T 7714 | Lin, Ya-Ping , Su, Bing-Mei , Lin, Juan . Engineering of carbonyl reductase for asymmetric reduction of difficult-to-reduce ketone tetrahydrofuran-3-one [J]. | MOLECULAR CATALYSIS , 2023 , 548 . |
| MLA | Lin, Ya-Ping et al. "Engineering of carbonyl reductase for asymmetric reduction of difficult-to-reduce ketone tetrahydrofuran-3-one" . | MOLECULAR CATALYSIS 548 (2023) . |
| APA | Lin, Ya-Ping , Su, Bing-Mei , Lin, Juan . Engineering of carbonyl reductase for asymmetric reduction of difficult-to-reduce ketone tetrahydrofuran-3-one . | MOLECULAR CATALYSIS , 2023 , 548 . |
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Bovine lactoferrin peptide (LFcinB), as an antimicrobial peptide, is expected to be an alternative of antibiotics owing to its broad-spectrum antimicrobial activity and specific mechanism. However, the weak antimicrobial activity, high hemolysis, and poor stability of LFcinB limited its applications in the field of biomedicine, food and agriculture. In order to improve the antimicrobial activity of LFcinB, five mutants were designed rationally, of which mutant LF4 (M10W/P16R/A24L) showed highest antimicrobial activity. The bioinformatics analysis indicated that the improved antimicrobial activity of LF4 was related to its increased cations, higher amphiphilicity and the extension of the & beta;-sheet in the structure. These studies will highlight the important role of bioinformatic tools in designing ideal biopeptides and lay a foundation for further development of antimicrobial peptides.
Keyword ：
Actimicrobial activity Actimicrobial activity Bioinformatics analysis Bioinformatics analysis Bovine lactoferrin peptide Bovine lactoferrin peptide Rational design Rational design
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| GB/T 7714 | Hong, Xiaokun , Liu, Xueqian , Su, Bingmei et al. Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design [J]. | PROTEIN JOURNAL , 2023 , 42 (6) : 633-644 . |
| MLA | Hong, Xiaokun et al. "Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design" . | PROTEIN JOURNAL 42 . 6 (2023) : 633-644 . |
| APA | Hong, Xiaokun , Liu, Xueqian , Su, Bingmei , Lin, Juan . Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design . | PROTEIN JOURNAL , 2023 , 42 (6) , 633-644 . |
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本发明属于生物工程技术领域，具体涉及一种3β‑羟基甾体脱氢酶SfSDR及其在制备去氢表雄酮中的应用。本发明将3β‑羟基甾体脱氢酶SfSDR与葡萄糖脱氢酶BtGDH在大肠埃希氏菌中共表达，并以共表达工程菌的静息细胞作为生物催化剂协同酯酶Z03共同催化3‑乙酰氧基‑△3, 5‑雄甾二烯‑17‑酮合成去氢表雄酮。该生物催化剂具有较高的催化活性、区域选择性和立体选择性，可以在6 h以内完全转化32.8 g/L的3‑乙酰氧基‑△3, 5‑雄甾二烯‑17‑酮生成目标产物去氢表雄酮，无需添加有机溶剂且无副产物产生，经过分离纯化，产物回收率高达95%以上，说明该生物催化剂是去氢表雄酮绿色合成的高效催化剂。
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| GB/T 7714 | 林娟 , 苏冰梅 , 师艺冰 et al. 一种3β-羟基甾体脱氢酶及其在制备去氢表雄酮中的应用 : CN202211028698.9[P]. | 2022-08-25 00:00:00 . |
| MLA | 林娟 et al. "一种3β-羟基甾体脱氢酶及其在制备去氢表雄酮中的应用" : CN202211028698.9. | 2022-08-25 00:00:00 . |
| APA | 林娟 , 苏冰梅 , 师艺冰 , 许炼 , 许鑫琦 . 一种3β-羟基甾体脱氢酶及其在制备去氢表雄酮中的应用 : CN202211028698.9. | 2022-08-25 00:00:00 . |
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