A Rational Design for Enhanced Catalytic Activity and Durability: Strongly Coupled N-Doped CrOx/Ce0.2Zr0.8O2 Nanoparticle Composites

2018 ◽  
Vol 1 (3) ◽  
pp. 1150-1163 ◽  
Author(s):  
Wei Cai ◽  
Qin Zhong ◽  
Dongyu Wang ◽  
Yunxia Zhao ◽  
Mindong Chen ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Rational Design ◽  
Strongly Coupled ◽  
Nanoparticle Composites

scholarly journals Rational Design of Bioinspired Nanocomposites with Tunable Catalytic Activity

2021 ◽  
Author(s):  
Hans C. Hendrikse ◽  
Alejo Aguirre ◽  
Arno van der Weijden ◽  
Anne S. Meeussen ◽  
Fernanda Neira D’Angelo ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Rational Design

Engineering of serine protease for improved thermostability and catalytic activity using rational design

2019 ◽  
Vol 126 ◽  
pp. 229-237 ◽  
Author(s):  
Naeem Mahmood Ashraf ◽  
Akshaya Krishnagopal ◽  
Aadil Hussain ◽  
David Kastner ◽  
Ahmed Mahmoud Mohammed Sayed ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Rational Design

A Finite Element Framework for Magneto-Actuated Large Deformation and Instability of Slender Magneto-Active Elastomers

2020 ◽  
Vol 12 (01) ◽  
pp. 2050013 ◽  
Author(s):  
Yin Liu ◽  
Shoue Chen ◽  
Xiaobo Tan ◽  
Changyong Cao
Keyword(s):  
Magnetic Field ◽  
Finite Element ◽  
Magnetic Fields ◽  
Large Deformation ◽  
Rational Design ◽  
Mesh Distortion ◽  
Strongly Coupled ◽  
Background Space ◽  
Spatial Coordinates ◽  
The Magnetic Field

In this paper, we present an efficient finite element framework for modeling the finite deformations of slender magneto-active elastomers (MAE) under applied magnetic fields or currents. For the convenience of numerical modeling, magnetic field is defined at fixed spatial coordinates in the background space rather than in the elastic MAEs using material coordinates. The magnetic field will vary with free or localized currents while the spatial distribution of the magnetic field will evolve with the motion or deformation of the MAE materials, which is actuated by the surface or body forces induced by external magnetic fields or equivalent currents. A staggered strategy and a Riks method are introduced to solve the strongly coupled governing equations of the magnetic field and displacement field using finite element method. The mesh distortion along the interfaces between MAE domain and free-space domain is resolved by considering concurrent deformation of the mesh in these two domains. A few 2D numerical examples demonstrate the validity and efficiency of the developed model for simulating large deformation of MAE with non-uniform spatial magnetic field under different actuation sources such as free currents, magnetization or external magnetic field. This framework offers a new solution strategy for modeling mechano-magneto problems of MAEs and will help rational design and analysis of MAE-based actuators and soft robotics in the future.

Towards rational design of core–shell catalytic nanoreactor with high performance catalytic hydrogenation of levulinic acid

2016 ◽  
Vol 6 (13) ◽  
pp. 5102-5115 ◽  
Author(s):  
Biplab Banerjee ◽  
Ramana Singuru ◽  
Sudipta K. Kundu ◽  
Karnekanti Dhanalaxmi ◽  
Linyi Bai ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Catalytic Hydrogenation ◽  
Levulinic Acid ◽  
High Performance ◽  
Rational Design ◽  
Core Shell ◽  
High Catalytic Activity

Core–shell catalytic nanoreactor was designed, exhibiting high catalytic activity for levulinic acid hydrogenation.

The Rational Design and Synthesis of Water-Soluble Thiourea Ligands for Recoverable Pd-Catalyzed Aerobic Aqueous Suzuki–Miyaura Reactions at Room Temperature

Synthesis ◽  
2018 ◽  
Vol 50 (07) ◽  
pp. 1499-1510 ◽  
Author(s):  
Wei Chen ◽  
Xiao-Yan Lu ◽  
Bei-Hua Xu ◽  
Wei-guo Yu ◽  
Zi-niu Zhou ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Rational Design ◽  
Pd Nanoparticles ◽  
Water Soluble ◽  
Tem Analysis ◽  
Arylboronic Acids ◽  
Design And Synthesis ◽  
Black Precipitate ◽  
Aryl Bromides ◽  
Carboxylic Groups

Eight precatalysts containing carboxylic-functionalized thiourea ligands are prepared and their activities and recyclability are evaluated in aerobic aqueous Suzuki–Miyaura reactions. A bulky monothiourea–Pd complex, functionalized with four carboxylic groups, shows the best activity and recyclability in the coupling of aryl bromides with arylboronic acids. The catalyst can be reused at least five times without any significant reduction in its catalytic activity. TEM analysis and the confirmed catalytic activity of the observed black precipitate reveal that Pd nanoparticles are formed during the reactions and are stabilized by the carboxylic-functionalized thiourea ligands.

scholarly journals Engineering of the Recombinant Expression and PEGylation Efficiency of the Therapeutic Enzyme Human Thymidine Phosphorylase

2021 ◽  
Vol 9 ◽  
Author(s):  
Christos S. Karamitros ◽  
Catrina M. Somody ◽  
Giulia Agnello ◽  
Scott Rowlinson
Keyword(s):  
Catalytic Activity ◽  
Thymidine Phosphorylase ◽  
Rational Design ◽  
Metabolic Diseases ◽  
Recombinant Expression ◽  
Bacterial Enzymes ◽  
Gastrointestinal Complications ◽  
E Coli ◽  
Enzyme Replacement ◽  
Arginine Residues

Human thymidine phosphorylase (HsTP) is an enzyme with important implications in the field of rare metabolic diseases. Defective mutations of HsTP lead to mitochondrial neurogastrointestinal encephalomyopathy (MNGIE), a disease with a high unmet medical need that is associated with severe neurological and gastrointestinal complications. Current efforts focus on the development of an enzyme replacement therapy (ERT) using the Escherichia coli ortholog (EcTP). However, bacterial enzymes are counter-indicated for human therapeutic applications because they are recognized as foreign by the human immune system, thereby eliciting adverse immune responses and raising significant safety and efficacy risks. Thus, it is critical to utilize the HsTP enzyme as starting scaffold for pre-clinical drug development, thus de-risking the safety concerns associated with the use of bacterial enzymes. However, HsTP expresses very poorly in E. coli, whereas its PEGylation, a crucial chemical modification for achieving long serum persistence of therapeutic enzymes, is highly inefficient and negatively affects its catalytic activity. Here we focused on the engineering of the recombinant expression profile of HsTP in E. coli cells, as well as on the optimization of its PEGylation efficiency aiming at the development of an alternative therapeutic approach for MNGIE. We show that phylogenetic and structural analysis of proteins can provide important insights for the rational design of N’-terminus-truncation constructs which exhibit significantly improved recombinant expression levels. In addition, we developed and implemented a criteria-driven rational surface engineering strategy for the substitution of arginine-to-lysine and lysine-to-arginine residues to achieve more efficient, homogeneous and reproducible PEGylation without negatively affecting the enzymatic catalytic activity upon PEGylation. Collectively, our proposed strategies provide an effective way to optimize enzyme PEGylation and E. coli recombinant expression and are likely applicable for other proteins and enzymes.

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