Insights from Enzymatic Catalysis: A Path towards Bioinspired High‐Performance Electrocatalysts

Sedenho, Graziela C.; Colombo, Rafael N. P.; Crespilho, Frank N.

doi:10.1002/cctc.202300491

Cited by 5 publications

(2 citation statements)

References 144 publications

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“…The notable enhancement of enzyme activity observed with the incorporation of Ca 2+ , Cu 2+ , Mg 2+ , and Mn 2+ ions as co-enzymes can be attributed to several mechanisms. Firstly, these metal ions play a crucial role in stabilizing the enzyme structure by interacting with specific amino acid residues in the enzyme's active site [51], thereby promoting optimal enzymesubstrate interactions. Secondly, they act as cofactors that bind to the enzyme-substrate complex, facilitating substrate binding and catalysis [52].…”

Section: Testing Of Immobilized Lipase For Hydrolysis Reactionmentioning

confidence: 99%

Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production

Moentamaria,

Irfin,

Chumaidi

et al. 2024

Bull. Chem. React. Eng. Catal.

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The low cost and excellent catalytic properties of lipase for industrial processes are highly desirable. A promising new approach involves the support modification of lipase and spacer arm, which enables the enhancement of lipase properties. This study investigates the immobilization of crude lipase from Mucor miehei onto a Polyurethane Foam (PUF) surface using various coating techniques. The PUF matrix was obtained through isocyanate and polyol reactions. Subsequently, the PUF was coated by adsorbing lipase and adding edible support material. The immobilized lipase was then utilized in the hydrolysis of coconut oil to produce fatty acids. Furthermore, the immobilized enzyme was employed in the esterification of fatty acids to produce bio-flavors. The results demonstrate that the attachment reaction using support material, namely lecithin, gelatin, MgCl2, and Polyethylene glycol 6000 (PEG), all of which are simple and edible, was able to enhance the stability and reusability of lipase. This immobilization technique increased triglyceride hydrolysis into FFA by 422%. The successful edible support modification of immobilized lipase from M. miehei on PUF, coupled with significantly enhanced enzyme stability and catalytic activity, offers a promising, environmentally friendly solution for diverse applications in the food industry. Copyright © 2024 by Authors, Published by BCREC Publishing Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).

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Section: Testing Of Immobilized Lipase For Hydrolysis Reactionmentioning

confidence: 99%

Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production

Moentamaria,

Irfin,

Chumaidi

et al. 2024

Bull. Chem. React. Eng. Catal.

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“…Because of these challenges with native systems, significant effort has been devoted to the development of bio‐inspired materials that recapitulate the activity of enzymes in materials that are more stable and scalable. [ 10 ] However, especially for polymeric systems, bio‐inspired materials remain limited in their control over the geometry of chelated metals serving as active sites and often have even less control over mimicking the secondary sphere influences that occur in proteins. Thus, the development of bio‐inspired materials that afford the specificity and selectivity of enzymes while maintaining the stability and scalability of polymers is essential to reach yields relevant for work beyond the laboratory.…”

Section: Introductionmentioning

confidence: 99%

Secondary Structure in Enzyme‐Inspired Polymer Catalysts Impacts Water Oxidation Efficiency

Sedenho,

Nascimento,

Zamani

et al. 2024

Advanced Science

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Protein structure plays an essential role on their stability, functionality, and catalytic activity. In this work, the interplay between the β‐sheet structure and its catalytic implications to the design of enzyme‐inspired materials is investigated. Here, inspiration is drawn from the active sites and β‐sheet rich structure of the highly efficient multicopper oxidase (MCO) to engineer a bio‐inspired electrocatalyst for water oxidation utilizing the abundant metal, copper. Copper ions are coordinated to poly‐histidine (polyCuHis), as they are in MCO active sites. The resultant polyCuHis material effectively promotes water oxidation with low overpotentials (0.15 V) in alkaline systems. This activity is due to the 3D structure of the poly‐histidine backbone. By increasing the prevalence of β‐sheet structure and decreasing the random coil nature of the polyCuHis secondary structures, this study is able to modulates the electrocatalytic activity of this material is modulated, shifting it toward water oxidation. These results highlight the crucial role of the local environment at catalytic sites for efficient, energy‐relevant transformations. Moreover, this work highlights the importance of conformational structure in the design of scaffolds for high‐performance electrocatalysts.

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Effect of Bipyridines on Catalytic Oxygen Reduction by Oxamidato‐Bridged Dicopper(II) Complexes

Liu,

Li,

Liu

et al. 2024

Applied Organom Chemis

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The oxygen reduction reaction (ORR) has a crucial impact on the energy conversion efficiency and the performance of fuel cells, it is urgent to deliver low‐cost efficient ORR catalysts for the aim to scale up the utilization of fuel cells. In this study, three oxamidate copper(II) complexes [Cu2(trans‐L)(H2O)2(ClO4)2]·2H2O (Cuox), [Cu2(cis‐L)(bpy)(ClO4)2]·CH3OH (Cuoxbpy), and [Cu2(cis‐L)(mebpy)(ClO4)](ClO4) (Cuoxmebpy) (L = N,N–bis(2–pyridylmethyl)oxamide, bpy = 2,2′–bipyridine, and mebpy = 4,4′–dimethyl–2,2′–bipyridine) were prepared and characterized. The configuration of L varied from the trans form to the cis form as the bipyridines were introduced to the dicopper complex. The redox properties of three oxamidate copper(II) complexes and their catalytic activities for the ORR were studied in neutral aqueous solutions. The ORR onset potentials by Cuox, Cuoxbpy, and Cuoxmebpy were 0.417, 0.502, and 0.481 versus RHE, respectively. Three complexes homogeneously catalyzed the ORR to predominantly generate H2O2. A bimolecular catalytic pathway was proposed for the ORR mediated by Cuox, whereas a single‐molecular pathway was by Cuoxbpy and Cuoxmebpy. This work demonstrated that oxamidate metal complexes are promising ORR catalyst candidates provided that their electronic structures are appropriately tuned by altering the substituent on the organic ligands.

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Insights from Enzymatic Catalysis: A Path towards Bioinspired High‐Performance Electrocatalysts

Cited by 5 publications

References 144 publications

Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production

Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production

Secondary Structure in Enzyme‐Inspired Polymer Catalysts Impacts Water Oxidation Efficiency

Effect of Bipyridines on Catalytic Oxygen Reduction by Oxamidato‐Bridged Dicopper(II) Complexes

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