Yuhong Ren

East China University of Science and Technology

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Dongzhi Wei

East China University of Science and Technology

Feng‐Qing Wang

Shanghai Jiao Tong University

Xinyi Tao

Third Affiliated Hospital of Southern Medical University

Kefeng Ni

DuPont (China)

Yong Wang

Center for Excellence in Molecular Plant Sciences

Hualei Wang

East China University of Science and Technology

Xin Gao

Jiangsu Province Hospital

Ming Zhao

Anhui Polytechnic University

Wei Dong-zhi

East China University of Science and Technology

Chengcheng Zhao

Wuhan Botanical Garden

Cooperative Institutions

East China University of Science and Technology

Chinese Academy of Sciences

University of Chinese Academy of Sciences

Sun Yat-sen University

Zhejiang University

Jilin University

Peking University

Shanxi Agricultural University

Shanghai Jiao Tong University

Center for Excellence in Molecular Plant Sciences

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Photocontrolled reversible self-assembly of dodecamer nitrilase

Bioresources and Bioprocessing (2017)

Qiao Yu Yong Wang Sheng-Yun Zhao Yuhong Ren

Naturally photoswitchable proteins act as a powerful tool for the spatial and temporal control of biological processes by inducing the formation of a photodimerizer. In this study, a method for the precise and reversible inducible self-assembly of dodecamer nitrilase in vivo (in Escherichia coli) and in vitro (in a cell-free solution) was developed by means of the photoswitch-improved light-inducible dimer (iLID) system which could induce protein–protein dimerization. Nitrilase was fused with the photoswitch protein AsLOV2-SsrA to achieve the photocontrolled self-assembly of dodecamer nitrilase. The fusion protein self-assembled into a supramolecular assembly when illuminated at 470 nm. Scanning electron microscopy showed that the assembly formed a circular sheet structure. Self-assembly was also induced by light in E. coli. Dynamic light scattering and turbidity assay experiments showed that the assemblies formed within a few seconds under 470-nm light and completely disassembled within 5 min in the dark. Assembly and disassembly could be maintained for at least five cycles. Both in vitro and in vivo, the assemblies retained 90% of the initial activity of nitrilase and could be reused at least four times in vitro with 90% activity. An efficient method was developed for the photocontrolled assembly and disassembly of dodecamer nitrilase and for scaffold-free reversible self-assembly of multiple oligomeric enzymes in vivo and in vitro, providing new ideas and methods for immobilization of enzyme without carrier.

Photoswitch

Dodecameric protein

Nitrilase

Supramolecular assembly

10.1186/s40643-017-0167-3

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Citations (7)

Cadmium sulfide net framework nanoparticles for photo-catalyzed cell redox

RSC Advances (2020)

Zhaoyu Chang Jian Zhang Wanyuan Dong Xiangqi Meng Hualei Wang

A strategy for synthesizing cadmium sulfide net framework (CdS-NF) nanoparticles was developed in a water-based system under mild reaction conditions. The CdS-NFs have not only the excellent photocatalytic properties of CdS, but also the large surface area and diverse porous structures of a metal-organic framework. An Escherichia coli-CdS-NF hybrid system was constructed using NADH regeneration to promote the conversion of trimethylpyruvate acid to l-tert-leucine. The E. coli-CdS-NF system showed higher NAD+ recycling efficiency and substrate conversion rate than CdS QDs under visible light illumination. This work demonstrates a novel method for developing a brilliant coenzyme recycling photocatalyst in bio-redox reactions.

Cadmium sulfide

Zinc sulfide

Visible spectrum

10.1039/d0ra08235j

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Citations (4)

Photocontrol of Itaconic Acid Synthesis in Escherichia coli

ACS Synthetic Biology (2022)

Yuting Li Ming Zhao Dongzhi Wei Jian Zhang Yuhong Ren

Metabolic engineering aims to control cellular metabolic flow and maximize the production of a product of interest. Photocontrol of the activities of proteins is an effective method for accurately regulating metabolic pathways. In this study, we inserted the photosensor light-oxygen-voltage-sensing domain 2 of Avena sativa (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH), the key enzyme in the competitive pathway of itaconic acid (ITA) synthesis, to construct photoswitchable IDH-AsLOV2 (ILOVs). These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in Escherichia coli to improve ITA production. The engineered fusion proteins ILOV2, ILOV3, ILOV6, and ILOV7 exhibited effective reversibility under the oscillation of darkness and blue light illumination in vitro. The efficacies of the intracellular photoswitches were evaluated, and an optimal photocontrol strategy was established in vivo. The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the icd gene. The photocontrol strategy developed here can be extended for process optimization and titer improvement of other high-value bioengineering chemicals.

Itaconic acid

Metabolic Engineering

Tricarboxylic acid

Metabolic pathway

10.1021/acssynbio.2c00014

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Characterization of a nitrilase from Arthrobacter aurescens CYC705 for synthesis of iminodiacetic acid

The Journal of General and Applied Microbiology (2014)

Wenwen Cai Erzheng Su Shujing Zhu Yuhong Ren Dongzhi Wei

A nitrilase gene cyc705 from Arthrobacter aurescens CYC705 for synthesis of iminodiacetic acid (IDA) was cloned. This gene contained a 930 bp ORF, which encoded a polypeptide of 310 amino acids. A recombinant Escherichia coli BL21(DE3)/pET28a-cyc705 was constructed to achieve the heterologous expression of cyc705. This recombinant nitrilase was purified to homogeneity with a molecular weight of 36.7 kDa on SDS-PAGE and mass spectrometry, and characterized to be an oligomer of 14 subunits by gel permeation chromatography. Using iminodiacetonitrile (IDAN) as the substrate, the Vmax, Km, kcat and kcat/Km were 9.05 U mg−1, 43.17 mM−1, 94.1 min−1 and 2.18×103 min−1 M−1, respectively. The optimum temperature and pH were 25°C and 5.8. The suitable substrates for the purified nitrilase were short-chain aliphatic dinitriles. High concentration of IDAN could be hydrolyzed to IDA in a shorter time.

Nitrilase

Arthrobacter

Enzyme Kinetics

Iminodiacetic acid

Heterologous expression

10.2323/jgam.60.207

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Synthesis and Evaluation of Transdermal Permeation, Pharmacological Activity of Bornyl NSAID Esters

Letters in Drug Design & Discovery (2014)

Jiufeng Lin Kefeng Ni Yang Zhang Dongzhi Wei Yuhong Ren

The bornyl ester derivatives of non-steroidal anti-inflammatory drugs (NSAIDs) including naproxen, ketoprofen and flufenamic acid, were synthesized and their transdermal permeation efficiency and pharmacological activity were determined. The bornyl NSAID esters exhibited more than 10-fold increase of permeation efficiency across mice skin than parent NSAIDs. The preliminary biological and pharmacological evaluations suggested that the bornyl NSAID esters retain most of their inhibition activity toward cyclooxygenase (COX) enzymes and show significant analgesic effect against acetic acid-induced writhing in mice. Keywords: Anti-nociceptive, borneol, cyclooxygenase, esters, non-steroidal anti-inflammatory drugs, transdermal permeation.

10.2174/1570180811666140627004820

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The protective effect of ascorbic acid derivative on PC12 cells: Involvement of its ROS scavenging ability

Life Sciences (2003)

Changbin Du Jianwen Liu Wu Su Yuhong Ren Dongzhi Wei

Scavenging

10.1016/j.lfs.2003.07.014

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Study on the heredity stability of a recombinant plasmid pMal--2X in {\sl Escherichia coli}

Baosheng Ge Yuhong Ren Zhihong Tang Yang Yu Qin Song

The strain of TB1 from the original stock which harboring a recombinant plasmid pMal-2X including apc gene from cyanophyceae had been subcultured serialyto 100~(th) generation in Amp~(+) plate. The growth characteristics and the morphology of the cultures did not show differences among the generations. The chromatogram of the plasmids in different generations digested by EcoRⅠ restriction enzymes were same, as well as DNA sequences showed no difference among generations. In addition to that, origin strain and 10~(th), 20~(th), 50~(th) and 100~(th) generation strain had a similar rAPC expression level. The immunology activity of the rAPC and SDS-PAGE of the proteins expressed in different generations were also same. From the above results, it is indicated that recombinant stain P1 has a high hereditable stability.

Strain (injury)

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A novel technique for in situ aggregation of Gluconobacter oxydans using bio‐adhesive magnetic nanoparticles

Biotechnology and Bioengineering (2012)

Kefeng Ni Huimin Lu Cunxun Wang Kvar C. L. Black Dongzhi Wei

Abstract Here, we present a novel technique to immobilize magnetic particles onto whole Gluconobacter oxydans in situ via a synthetic adhesive biomimetic material inspired by the protein glues of marine mussels. Our approach involves simple coating of a cell adherent polydopamine film onto magnetic nanoparticles, followed by conjugation of the polydopamine‐coated nanoparticles to G. oxydans which resulted in cell aggregation. After optimization, 21.3 mg (wet cell weight) G. oxydans per milligram of nanoparticle was aggregated and separated with a magnet. Importantly, the G. oxydan aggregates showed high specific activity and good reusability. The facile approach offers the potential advantages of low cost, easy cell separation, low diffusion resistance, and high efficiency. Furthermore, the approach is a convenient platform technique for magnetization of cells in situ by direct mixing of nanoparticles with a cell suspension. Biotechnol. Bioeng. 2012; 109: 2970–2977. © 2012 Wiley Periodicals, Inc.

10.1002/bit.24582

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Citations (28)

Quantification intracellular levels of oligodeoxynucleotide-doxorubicin conjugate in human carcinoma cells in situ

Journal of Pharmaceutical and Biomedical Analysis (2004)

Yuhong Ren Dongzhi Wei

Conjugate

10.1016/j.jpba.2004.06.012

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Citations (10)

Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase

PLoS ONE (2012)

Kefeng Ni Xu Zhou Li Zhao Hualei Wang Yuhong Ren

The magnetic chitosan nanocomposites have been studied intensively and been used practically in various biomedical and biological applications including enzyme immobilization. However, the loading capacity and the remained activity of immobilized enzyme based on existing approaches are not satisfied. Simpler and more effective immobilization strategies are needed. Here we report a simple catechol modified protocol for preparing a novel catechol-chitosan (CCS) - iron oxide nanoparticles (IONPs) composites carrying adhesive moieties with strong surface affinity. The ω-transaminase (ω-TA) was immobilized onto this magnetic composite via nucleophilic reactions between catechol and ω-TA. Under optimal conditions, 87.5% of the available ω-TA was immobilized on the composite, yielding an enzyme loading capacity as high as 681.7 mg/g. Furthermore, the valuation of enzyme activity showed that ω-TA immobilized on CCS-IONPs displayed enhanced pH and thermal stability compared to free enzyme. Importantly, the immobilized ω-TA retained more than 50% of its initial activity after 15 repeated reaction cycles using magnetic separation and 61.5% of its initial activity after storage at 4°C in phosphate buffered saline (PBS) for 15 days. The results suggested that such adhesive magnetic composites may provide an improved platform technology for bio-macromolecules immobilized.

Catechol

Thermal Stability

10.1371/journal.pone.0041101

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Citations (33)