8 results match your criteria Catalysts[Journal]

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Activated Carbon as a Cathode for Water Disinfection through the Electro-Fenton Process.

Catalysts 2019 Jul 12;9(7). Epub 2019 Jul 12.

Department of Civil and Environmental Engineering, Northeastern University, Boston, MA 02115, USA.

Unlike many other water disinfection methods, hydroxyl radicals (HO) produced by the Fenton reaction (Fe/HO) can inactivate pathogens regardless of taxonomic identity of genetic potential and do not generate halogenated disinfection by-products. Hydrogen peroxide (HO) required for the process is typically electrogenerated using various carbonaceous materials as cathodes. However, high costs and necessary modifications to the cathodes still present a challenge to large-scale implementation. Read More

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http://dx.doi.org/10.3390/catal9070601DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7062377PMC

Immobilization of β-Galactosidases on the Cell Surface Using the Peptidoglycan-Binding Motif LysM.

Catalysts 2019 May;9(5):443

Food Biotechnology Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, A-1190 Vienna, Austria.

Lysin motif (LysM) domains are found in many bacterial peptidoglycan hydrolases. They can bind non-covalently to peptidoglycan and have been employed to display heterologous proteins on the bacterial cell surface. In this study, we aimed to use a single LysM domain derived from a putative extracellular transglycosylase Lp_3014 of WCFS1 to display two different lactobacillal β-galactosidases, the heterodimeric LacLM-type from and the homodimeric LacZ-type from subsp. Read More

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http://dx.doi.org/10.3390/catal9050443DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6783300PMC

Immobilization of an Endo-β--acetylglucosaminidase for the Release of Bioactive glycans.

Catalysts 2018 Jul 10;8(7). Epub 2018 Jul 10.

Department of Food Science and Technology, University of California, One Shields Avenue, Davis, CA 95616, USA; (J.L.C.); (D.B.).

As more is learned about glycoproteins' roles in human health and disease, the biological functionalities of -linked glycans are becoming more relevant. Protein deglycosylation allows for the selective release of -glycans and facilitates glycoproteomic investigation into their roles as prebiotics or anti-pathogenic factors. To increase throughput and enzyme reusability, this work evaluated several immobilization methods for an endo-β--acetylglucosaminidase recently discovered from the commensal . Read More

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http://dx.doi.org/10.3390/catal8070278DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6419974PMC
July 2018
4 Reads

Alkanethiolate-Capped Palladium Nanoparticles for Regio- and Stereoselective Hydrogenation of Allenes.

Catalysts 2018 Oct 29;8(10). Epub 2018 Sep 29.

Department of Chemistry and Biochemistry, California State University Long Beach, 1250 Bellflower Blvd., Long Beach, CA 90840, USA.

Colloidal Pd nanoparticles capped with octanethiolate ligands have previously shown an excellent selectivity toward the mono-hydrogenation of both isolated and conjugated dienes to internal alkenes. This paper reports an efficient stereoselective mono-hydrogenation of cumulated dienes (allenes) to either Z or E olefinic isomers, depending on the substitution pattern around C=C bonds. Kinetic studies indicate that the reaction progresses through the hydrogenation of less hindered C=C bonds to produce internal Z olefinic isomers. Read More

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http://dx.doi.org/10.3390/catal8100428DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6363366PMC
October 2018
1 Read

An MM and QM Study of Biomimetic Catalysis of Diels-Alder Reactions Using Cyclodextrins.

Catalysts 2018 Feb 29;8(2). Epub 2018 Jan 29.

Department of Chemistry, University of California, Riverside, CA 92521, USA.

We performed a computational investigation of the mechanism by which cyclodextrins (CDs) catalyze Diels-Alder reactions between 9-anthracenemethanol and -cyclohexylmaleimide. Hydrogen bonds (Hbonds) between -cyclohexylmaleimide and the hydroxyl groups of cyclodextrins were suggested to play an important role in this catalytic process. However, our free energy calculations and molecular dynamics simulations showed that these Hbonds are not stable, and quantum mechanical calculations suggested that the reaction is not promoted by these Hbonds. Read More

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http://dx.doi.org/10.3390/catal8020051DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6011829PMC
February 2018
53 Reads

Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies.

Catalysts 2016 Jun 27;6(6). Epub 2016 May 27.

INRS-Institut Armand-Frappier, Université du Québec, 531 Boul. des Prairies, Laval, QC H7V 1B7, Canada (C.N.); PROTEO, the Québec Network for Research on Protein Function, Engineering, and Applications, 1045 Avenue de la Médecine, Université Laval, Québec, QC G1V 0A6, Canada; GRASP, the Groupe de Recherche Axé sur la Structure des Protéines, 3649 Promenade Sir William Osler, McGill University, Montréal, QC H3G 0B1, Canada.

It is now common knowledge that enzymes are mobile entities relying on complex atomic-scale dynamics and coordinated conformational events for proper ligand recognition and catalysis. However, the exact role of protein dynamics in enzyme function remains either poorly understood or difficult to interpret. This mini-review intends to reconcile biophysical observations and biological significance by first describing a number of common experimental and computational methodologies employed to characterize atomic-scale residue motions on various timescales in enzymes, and second by illustrating how the knowledge of these motions can be used to describe the functional behavior of enzymes and even act upon it. Read More

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http://dx.doi.org/10.3390/catal6060081DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5375114PMC
June 2016
2 Reads

Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function.

Catalysts 2017 14;7(7). Epub 2017 Jul 14.

Department of Chemistry, McKinley Hall, Wichita State University, 1845 Fairmount, Wichita, KS 67260-0051, USA.

Small molecules, such as solvent, substrate, and cofactor molecules, are key players in enzyme catalysis. Computational methods are powerful tools for exploring the dynamics and thermodynamics of these small molecules as they participate in or contribute to enzymatic processes. In-depth knowledge of how small molecule interactions and dynamics influence protein conformational dynamics and function is critical for progress in the field of enzyme catalysis. Read More

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http://dx.doi.org/10.3390/catal7070212DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6241538PMC
July 2017
22 Reads

Investigation of Structural Dynamics of Enzymes and Protonation States of Substrates Using Computational Tools.

Catalysts 2016 Jun 31;6(6). Epub 2016 May 31.

Department of Chemistry, University of California, Riverside, CA 92521, USA.

This review discusses the use of molecular modeling tools, together with existing experimental findings, to provide a complete atomic-level description of enzyme dynamics and function. We focus on functionally relevant conformational dynamics of enzymes and the protonation states of substrates. The conformational fluctuations of enzymes usually play a crucial role in substrate recognition and catalysis. Read More

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http://dx.doi.org/10.3390/catal6060082DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5119520PMC
June 2016
7 Reads
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