Enzymes-Encapsulated Defective Metal–Organic Framework Hydrogel Coupling with a Smartphone for a Portable Glucose Biosensor DOI

Ningyi Zhong,

Rui Gao, Yujian Shen

et al.

Analytical Chemistry, Journal Year: 2022, Volume and Issue: 94(41), P. 14385 - 14393

Published: Oct. 7, 2022

Enzymes featuring high catalytic efficiency and selectivity have been widely used as the sensing element in analytical chemistry. However, structural fragility poor machinability of an enzyme significantly limit its practicability biosensors. Herein, we develop a robust sensitive hybrid biosensor by means co-encapsulating enzymes into defective metal–organic framework (MOF), followed double-crosslinked alginate gelatinization. The MOF encapsulation can enhance stability enzymes, yet well preserve their biocatalytic function, while gelatinization allows biohybrid stretchability mechanical strength, which facilitates integration bead-, fiber-, sheet-like portable biosensor. In this work, consisting glucose oxidase peroxidase are co-encapsulated hydrogel, it efficiently convert blue-violet product through cascade encapsulated enabling colorimetric biosensing on miniaturized hydrogel when coupling with smartphone. Interestingly, outputs stronger signal than free powders, attributed to product-accumulated effect highly hydrophilic microenvironment hydrogel. As result, sensitively selectively sense linear range from 0.05 4 mM. Importantly, both "armor" endow durability, activity was well-maintained even after placing at room temperature for 30 d. We believe that has huge potential engineering next-generation

Language: Английский

Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization DOI Creative Commons
Juan M. Bolívar, John M. Woodley, Roberto Fernandéz‐Lafuente

et al.

Chemical Society Reviews, Journal Year: 2022, Volume and Issue: 51(15), P. 6251 - 6290

Published: Jan. 1, 2022

Enzyme immobilization has been developing since the 1960s and although many industrial biocatalytic processes use technology to improve enzyme performance, still today we are far from full exploitation of field. One clear reason is that evaluate based on only a few experiments not always well-designed. In contrast other reviews subject, here highlight pitfalls using incorrectly designed protocols explain why in cases sub-optimal results obtained. We also describe solutions overcome these challenges come conclusion recent developments material science, bioprocess engineering protein science continue open new opportunities for future. this way, immobilization, being mature discipline, remains as subject high interest where intense research necessary take advantage possibilities.

Language: Английский

Citations

355

Enzyme entrapment, biocatalyst immobilization without covalent attachment DOI Creative Commons
Hasan T. Imam, Patricia C. Marr, Andrew C. Marr

et al.

Green Chemistry, Journal Year: 2021, Volume and Issue: 23(14), P. 4980 - 5005

Published: Jan. 1, 2021

The entrapment of enzymes in organic, inorganic or biomaterials can yield active immobilized biocatalysts for chemical transformations without the need to form covalent bonds with protein.

Language: Английский

Citations

219

Confining enzymes in porous organic frameworks: from synthetic strategy and characterization to healthcare applications DOI
Siming Huang, Guosheng Chen, Gangfeng Ouyang

et al.

Chemical Society Reviews, Journal Year: 2022, Volume and Issue: 51(15), P. 6824 - 6863

Published: Jan. 1, 2022

This review comprehensively presents the cutting-edge advances of enzyme confinement using different porous organic frameworks.

Language: Английский

Citations

187

Shortening Synthetic Routes to Small Molecule Active Pharmaceutical Ingredients Employing Biocatalytic Methods DOI Creative Commons
Stefan Simić,

Erna Zukić,

Luca Schmermund

et al.

Chemical Reviews, Journal Year: 2021, Volume and Issue: 122(1), P. 1052 - 1126

Published: Nov. 30, 2021

Biocatalysis, using enzymes for organic synthesis, has emerged as powerful tool the synthesis of active pharmaceutical ingredients (APIs). The first industrial biocatalytic processes launched in half last century exploited whole-cell microorganisms where specific enzyme at work was not known. In meantime, novel molecular biology methods, such efficient gene sequencing and triggered breakthroughs directed evolution rapid development process-stable with broad substrate scope good selectivities tailored substrates. To date, are employed to enable shorter, more efficient, sustainable alternative routes toward (established) small molecule APIs, additionally used perform standard reactions API efficiently. Herein, large-scale synthetic containing key steps >130 APIs approved drugs drug candidates compared corresponding chemical protocols (if available) regarding steps, reaction conditions, scale. review is structured according functional group formed reaction.

Language: Английский

Citations

177

Multivalent Ce-MOFs as biomimetic laccase nanozyme for environmental remediation DOI
Shan Liang,

Xiaoling Wu,

Jun Xiong

et al.

Chemical Engineering Journal, Journal Year: 2022, Volume and Issue: 450, P. 138220 - 138220

Published: July 21, 2022

Language: Английский

Citations

149

Green Chemistry, Biocatalysis, and the Chemical Industry of the Future DOI
Roger A. Sheldon, Dean Brady

ChemSusChem, Journal Year: 2022, Volume and Issue: 15(9)

Published: Jan. 13, 2022

In the movement to decarbonize our economy and move away from fossil fuels we will need harness waste products of activities, such as lignocellulose, methane, carbon dioxide. Our wastes be integrated into a circular where used are recycled manufacturing cycle. Key this recycling plastics at resin monomer levels. Biotechnology is well suited future chemical industry that must adapt widely distributed diverse biological feedstocks. increasing mastery biotechnology allowing us develop enzymes organisms can synthesize widening selection desirable bulk chemicals, including plastics, commercially viable productivities. Integration bioreactors with electrochemical systems permit new production opportunities enhanced productivities advantage using low-carbon electricity renewable sustainable sources.

Language: Английский

Citations

127

Applications of immobilized lipases in enzymatic reactors: A review DOI
Daniela Remonatto, Rodney H. Miotti,

Rubens Monti

et al.

Process Biochemistry, Journal Year: 2022, Volume and Issue: 114, P. 1 - 20

Published: Jan. 5, 2022

Language: Английский

Citations

122

Biocatalysis as Key to Sustainable Industrial Chemistry DOI
Andrés R. Alcántara, Pablo Domı́nguez de Marı́a, Jennifer A. Littlechild

et al.

ChemSusChem, Journal Year: 2022, Volume and Issue: 15(9)

Published: March 3, 2022

The role and power of biocatalysis in sustainable chemistry has been continuously brought forward step by to its present outstanding position. problem-solving capabilities have realized numerous substantial achievements biology, engineering. Advances breakthroughs the life sciences interdisciplinary cooperation with clearly accelerated implementation biocatalytic synthesis modern chemistry. Resource-efficient manufacturing processes already provided benefits as well customer-centric value creation pharmaceutical, food, flavor, fragrance, vitamin, agrochemical, polymer, specialty, fine chemical industries. Biocatalysis can make significant contributions not only processes, but also design completely new value-creation chains. now be considered a key enabling technology implement

Language: Английский

Citations

102

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications DOI Open Access

Joaquim Bié,

Bruno Sepodes, Pedro Fernandes

et al.

Processes, Journal Year: 2022, Volume and Issue: 10(3), P. 494 - 494

Published: March 1, 2022

Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up several orders magnitude but also for the high degree substrate specificity, regiospecificity and stereospecificity. The use development enzymes as robust biocatalysts is one main challenges in biotechnology. However, despite specificities turnover enzymes, there drawbacks. At industrial level, these drawbacks typically overcome resorting immobilized enhance stability. Immobilization allows reuse, increases stability, facilitates process control, eases product recovery, enhances yield quality. This especially important expensive those obtained low fermentation with relatively activity. review provides an integrated perspective (multi)enzyme immobilization that abridges a critical evaluation methods carriers, biocatalyst metrics, impact key carrier features performance, trends towards miniaturization detailed illustrative examples representative biocatalytic applications promoting sustainability.

Language: Английский

Citations

100

Combining a Genetically Engineered Oxidase with Hydrogen‐Bonded Organic Frameworks (HOFs) for Highly Efficient Biocomposites DOI
Peter Wied, Francesco Carraro, Juan M. Bolívar

et al.

Angewandte Chemie International Edition, Journal Year: 2022, Volume and Issue: 61(16)

Published: Jan. 17, 2022

Enzymes incorporated into hydrogen-bonded organic frameworks (HOFs) via bottom-up synthesis are promising biocomposites for applications in catalysis and sensing. Here, we explored synthetic incorporation of d-amino acid oxidase (DAAO) with the metal-free tetraamidine/tetracarboxylate-based BioHOF-1 water. N-terminal enzyme fusion positively charged module Z

Language: Английский

Citations

75