View in EDS

Construction of extracellular peptide laccase-mimic nanozyme for the detection and degradation of phenols pollutants.

Saved in:
Bibliographic Details
Title: Construction of extracellular peptide laccase-mimic nanozyme for the detection and degradation of phenols pollutants.
Authors: Wang, Qinyu1,2 (AUTHOR), Hou, Yunhua1,2 (AUTHOR), Lin, Mingzhen2 (AUTHOR), Yang, Qinzheng1,2 (AUTHOR) yqz@qlu.edu.cn
Source: Colloids & Surfaces A: Physicochemical & Engineering Aspects. Oct2024, Vol. 699, pN.PAG-N.PAG. 1p.
Subjects: Peptides, Charge exchange, Pollutants, Waste recycling, Structural stability
Abstract: The search for efficient peptide ligands to boost the electron transfer from the metal center and enhance the activity of nano mimetic laccase has become a hot research topic. This study presents, an electrochemically active extracellular peptide ligand for the copper-based nanozyme (EP-Cu) with laccase-like activity. The surface-attached extracellular peptide enables EP-Cu to form a sphere with a porous structure, which shows better acid-base resistances, stability, and recyclability. The electron transfer pathway between the electrochemically active extracellular peptide and Cu provides EP-Cu a similar K m to that of laccase, but a higher V max and endows it excellent catalytic activity and substrate versatility. Therefore, the EP-Cu nanozyme prepared with the extracellular peptide have a broad applications prospect in the detection and degradation of phenols. [Display omitted] • Electrochemical active extracellular peptides can be used as ligands to construct EP-Cu nanozyme with laccase-like activity. • EP-Cu nanozyme have excellent structural thermodynamic stability due to the large number of peptides attached to the surface. • Extracellular peptides enhance the catalytic activity and stability of EP-Cu under extreme conditions. • EP-Cu catalyzes a wide range of phenols compounds due to hydrophobic residues in the extracellular peptide. [ABSTRACT FROM AUTHOR]
Copyright of Colloids & Surfaces A: Physicochemical & Engineering Aspects is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
Description
Abstract:The search for efficient peptide ligands to boost the electron transfer from the metal center and enhance the activity of nano mimetic laccase has become a hot research topic. This study presents, an electrochemically active extracellular peptide ligand for the copper-based nanozyme (EP-Cu) with laccase-like activity. The surface-attached extracellular peptide enables EP-Cu to form a sphere with a porous structure, which shows better acid-base resistances, stability, and recyclability. The electron transfer pathway between the electrochemically active extracellular peptide and Cu provides EP-Cu a similar K m to that of laccase, but a higher V max and endows it excellent catalytic activity and substrate versatility. Therefore, the EP-Cu nanozyme prepared with the extracellular peptide have a broad applications prospect in the detection and degradation of phenols. [Display omitted] • Electrochemical active extracellular peptides can be used as ligands to construct EP-Cu nanozyme with laccase-like activity. • EP-Cu nanozyme have excellent structural thermodynamic stability due to the large number of peptides attached to the surface. • Extracellular peptides enhance the catalytic activity and stability of EP-Cu under extreme conditions. • EP-Cu catalyzes a wide range of phenols compounds due to hydrophobic residues in the extracellular peptide. [ABSTRACT FROM AUTHOR]
ISSN:09277757
DOI:10.1016/j.colsurfa.2024.134687