Protein-inorganic hybrid nanoflowers with enhanced laccase-like activity for optical analysis of urease.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Protein-inorganic hybrid nanoflowers with enhanced laccase-like activity for optical analysis of urease.
Συγγραφείς: Feng S; Changchun Veterinary Research Institude, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, 130122, China. Electronic address: 17839959954@163.com., Wang X; Changchun Veterinary Research Institude, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, 130122, China; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, School of Public Health, Jilin University, Changchun, 130012, China., Li Y; Changchun Veterinary Research Institude, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, 130122, China; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, School of Public Health, Jilin University, Changchun, 130012, China., Li J; Changchun Veterinary Research Institude, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, 130122, China; School of Chemistry and Environmental Engineering, Changchun University of Science and Technology, Changchun, 130022, China., An X; Changchun Veterinary Research Institude, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, 130122, China., Zhou B; Changchun Veterinary Research Institude, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, 130122, China. Electronic address: hottank3210@126.com., Sun J; College of Pharmacy, Xinjiang Key Laboratory of Biopharmaceuticals and Medical Devices, Xinjiang Medical University, Urumqi, 830017, China. Electronic address: sun@xjmu.edu.cn.
Πηγή: Analytica chimica acta [Anal Chim Acta] 2026 May 15; Vol. 1399, pp. 345315. Date of Electronic Publication: 2026 Feb 27.
Τύπος έκδοσης: Journal Article; Research Support, Non-U.S. Gov't
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 0370534 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-4324 (Electronic) Linking ISSN: 00032670 NLM ISO Abbreviation: Anal Chim Acta Subsets: MEDLINE
Imprint Name(s): Publication: Amsterdam : Elsevier
Original Publication: Amsterdam.
Ιατρικοί όροι (MeSH): Urease*/analysis , Urease*/metabolism , Copper*/chemistry , Serum Albumin, Bovine*/chemistry , Serum Albumin, Bovine*/metabolism , Laccase*/chemistry , Laccase*/metabolism , Nanostructures*/chemistry, Colorimetry/methods ; Animals ; Cattle ; Limit of Detection
Περίληψη: Background: Urease is a crucial enzyme involved in urea hydrolysis, playing essential roles in the environmental monitoring, agricultural management, and clinical diagnostics. In these fields, the accurate and timely detection of urease activity is essential. However, conventional assays for its activity are often limited by inadequate sensitivity, tedious procedures, or expensive instrumentation, which hinders their utility for rapid, on-site, or real-time monitoring. Given the important role of urease in environmental and biological analysis, constructing a facile identification sensor is of great interest.
Results: Herein, a specific and stable colorimetric sensor was presented for the urease determination based on the bovine serum albumin (BSA)-inorganic Cu2+ hybrid nanoflowers (Cu-BSA HNFs). We successfully synthesized Cu-BSA HNFs nanozyme with laccase-like activity under the ultrasound assistance at room temperature. Surprisingly, the NH3 produced by the urease hydrolysis of urea coordinates to the Cu2+ centers in the Cu-BSA HNFs, which modulates the electronic structure of the active sites, stabilizes the Cu+ state within the catalytic cycle, and accelerates the electron transfer rate. This specific enhancement the catalytic activity, ultimately resulting the change of colorimetric signal. Thus, the colorimetric strategy for sensitive urease analysis with LODs of 0.054 mU/mL was established by the proposed based on the facile signal-on response. It was worth mentioning that a portable paper-based Cu-BSA HNFs sensor was also prepared for in situ qualitative monitoring of urease with the aid of a smartphone-based autonomous signal readout.
Significance: This work employs Cu-BSA HNFs nanozyme to construct a robust colorimetric platform for simple and sensitive urease activity monitoring, which not only presents an effective approach for the facile analysis of urease in biological and environmental samples but also broadens the utilization scope of nanozymes in point-of-care testing applications.
(Copyright © 2026 Elsevier B.V. All rights reserved.)
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Laccase-like activity; Nanozyme; Optical biosensor; Paper-based analytical devices; Urease detection
Substance Nomenclature: EC 3.5.1.5 (Urease)
789U1901C5 (Copper)
27432CM55Q (Serum Albumin, Bovine)
EC 1.10.3.2 (Laccase)
Entry Date(s): Date Created: 20260311 Date Completed: 20260710 Latest Revision: 20260731
Update Code: 20260731
DOI: 10.1016/j.aca.2026.345315
PMID: 41813338
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:1873-4324
DOI:10.1016/j.aca.2026.345315