Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays

Abstract As a typical superwettability behavior, superhydrophobicity can provide an appropriate strategy to enhance the mass transport in multiphase chemical reactions. In the oxidase‐based enzymatic reactions, the elaborately regulating of reactant oxygen are critical to the development of an oxida...

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Main Authors: Dandan Wang, Liping Chen, Xinjian Feng
Format: Article
Language:English
Published: Wiley 2023-04-01
Series:Droplet
Online Access:https://doi.org/10.1002/dro2.51
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author Dandan Wang
Liping Chen
Xinjian Feng
author_facet Dandan Wang
Liping Chen
Xinjian Feng
author_sort Dandan Wang
collection DOAJ
description Abstract As a typical superwettability behavior, superhydrophobicity can provide an appropriate strategy to enhance the mass transport in multiphase chemical reactions. In the oxidase‐based enzymatic reactions, the elaborately regulating of reactant oxygen are critical to the development of an oxidase‐based high‐performance biosensor. In solid–liquid diphase condition, however, the kinetics of oxidase‐catalyzed reactions is inhibited by delayed mass transport and poor solubility of oxygen. To address this limitation, the design of the solid–liquid–air triphase interface is proposed according to the binary cooperation of superhydrophobicity and hydrophilicity. On the triphase joint interface, oxygen required for the oxidase‐catalyzed reactions can diffuse directly to the reaction center from the air phase through the micro/nanostructured superhydrophobic substrate, thus improving the kinetics of the oxidase‐catalyzed reactions. In this minireview, we summarize recent advances in the fabrication of triphase reaction system based on different superhydrophobic substrate for oxidase‐based biosensors. Common substrates including fibrous network, nanowire arrays, 3D porous framework, and hollow sphere structures are outlined in categories.
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spelling doaj.art-de2fa8414e7d407b9685a9d3841f6f012023-11-22T16:25:30ZengWileyDroplet2731-43752023-04-0122n/an/a10.1002/dro2.51Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassaysDandan Wang0Liping Chen1Xinjian Feng2College of Chemistry, Chemical Engineering and Materials Science Soochow University Suzhou ChinaCollege of Chemistry, Chemical Engineering and Materials Science Soochow University Suzhou ChinaCollege of Chemistry, Chemical Engineering and Materials Science Soochow University Suzhou ChinaAbstract As a typical superwettability behavior, superhydrophobicity can provide an appropriate strategy to enhance the mass transport in multiphase chemical reactions. In the oxidase‐based enzymatic reactions, the elaborately regulating of reactant oxygen are critical to the development of an oxidase‐based high‐performance biosensor. In solid–liquid diphase condition, however, the kinetics of oxidase‐catalyzed reactions is inhibited by delayed mass transport and poor solubility of oxygen. To address this limitation, the design of the solid–liquid–air triphase interface is proposed according to the binary cooperation of superhydrophobicity and hydrophilicity. On the triphase joint interface, oxygen required for the oxidase‐catalyzed reactions can diffuse directly to the reaction center from the air phase through the micro/nanostructured superhydrophobic substrate, thus improving the kinetics of the oxidase‐catalyzed reactions. In this minireview, we summarize recent advances in the fabrication of triphase reaction system based on different superhydrophobic substrate for oxidase‐based biosensors. Common substrates including fibrous network, nanowire arrays, 3D porous framework, and hollow sphere structures are outlined in categories.https://doi.org/10.1002/dro2.51
spellingShingle Dandan Wang
Liping Chen
Xinjian Feng
Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays
Droplet
title Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays
title_full Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays
title_fullStr Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays
title_full_unstemmed Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays
title_short Superhydrophobicity‐mediated enhanced enzymatic kinetics and high‐performance bioassays
title_sort superhydrophobicity mediated enhanced enzymatic kinetics and high performance bioassays
url https://doi.org/10.1002/dro2.51
work_keys_str_mv AT dandanwang superhydrophobicitymediatedenhancedenzymatickineticsandhighperformancebioassays
AT lipingchen superhydrophobicitymediatedenhancedenzymatickineticsandhighperformancebioassays
AT xinjianfeng superhydrophobicitymediatedenhancedenzymatickineticsandhighperformancebioassays