Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal

Nanozymes hold huge potential in various fields, but their much lower catalytic activities than natural enzymes greatly limit their extensive applications. Recent studies indicated that an enhanced enzyme-like activity could be obtained by decreasing the particle size through rational design because...

Full description

Bibliographic Details
Main Authors: Phouphien Keoingthong, Shengkai Li, Zhaotian Zhu, Liang Zhang, Jieqiong Xu, Long Chen, Weihong Tan, Zhuo Chen
Format: Article
Language:English
Published: AIP Publishing LLC 2021-05-01
Series:APL Materials
Online Access:http://dx.doi.org/10.1063/5.0048777
id doaj-c2bb307513484118aa99ae2e5b5999d0
record_format Article
collection DOAJ
language English
format Article
sources DOAJ
author Phouphien Keoingthong
Shengkai Li
Zhaotian Zhu
Liang Zhang
Jieqiong Xu
Long Chen
Weihong Tan
Zhuo Chen
spellingShingle Phouphien Keoingthong
Shengkai Li
Zhaotian Zhu
Liang Zhang
Jieqiong Xu
Long Chen
Weihong Tan
Zhuo Chen
Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal
APL Materials
author_facet Phouphien Keoingthong
Shengkai Li
Zhaotian Zhu
Liang Zhang
Jieqiong Xu
Long Chen
Weihong Tan
Zhuo Chen
author_sort Phouphien Keoingthong
title Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal
title_short Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal
title_full Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal
title_fullStr Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal
title_full_unstemmed Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystal
title_sort enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled coru nanocrystal
publisher AIP Publishing LLC
series APL Materials
issn 2166-532X
publishDate 2021-05-01
description Nanozymes hold huge potential in various fields, but their much lower catalytic activities than natural enzymes greatly limit their extensive applications. Recent studies indicated that an enhanced enzyme-like activity could be obtained by decreasing the particle size through rational design because smaller nanoparticles (NPs) have larger surface-area-to-volume ratios and more unsaturated sites, which are beneficial to the adsorption of reactant species. However, ultrasmall NPs have low adsorption energy and poor stability, which makes the synthesis of superstable and ultrasmall nanozymes extremely difficult. Several interesting works reported that the encapsulation of ultrasmall NPs with few-layer carbon shells could effectively protect them from dissolution and agglomeration, and meanwhile, their catalytic activities were not greatly affected. Herein, we report a superstable and ultrasmall graphene encapsuled CoRu nanocrystal (CoRu@G) with the CoRu alloy confined in the nanospace of few-layer graphene via the chemical vapor deposition method. It shows excellent corrosion resistance in aqua regia due to the protection of the chemically inert graphitic shell. The intrinsic peroxidase-, oxidase-, and catalase-like activities of the CoRu@G are systematically explored, including the influence of the concentration, pH, and temperature on the enzyme-like activity, steady-state kinetic analysis, and catalytic oxidation mechanism study. Significantly, the CoRu@G shows an excellent and ultrastable enzyme-like activity with the treatment of high temperatures, buffered solutions, or NaCl solutions probably because the graphene layer protects it from dissolution and agglomeration efficiently. We believe that the proposed graphene confinement strategy could highlight the direction of highly active, superstable, and ultrasmall-sized nanozyme preparation.
url http://dx.doi.org/10.1063/5.0048777
work_keys_str_mv AT phouphienkeoingthong enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT shengkaili enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT zhaotianzhu enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT liangzhang enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT jieqiongxu enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT longchen enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT weihongtan enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
AT zhuochen enzymemimicactivitystudyofsuperstableandultrasmallgrapheneencapsuledcorunanocrystal
_version_ 1721410372825513984
spelling doaj-c2bb307513484118aa99ae2e5b5999d02021-06-01T18:30:19ZengAIP Publishing LLCAPL Materials2166-532X2021-05-0195051110051110-710.1063/5.0048777Enzyme-mimic activity study of superstable and ultrasmall graphene encapsuled CoRu nanocrystalPhouphien Keoingthong0Shengkai Li1Zhaotian Zhu2Liang Zhang3Jieqiong Xu4Long Chen5Weihong Tan6Zhuo Chen7Molecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaMolecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaMolecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaMolecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaMolecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaFaculty of Science and Technology, University of Macau, Taipa 999078, Macau, ChinaMolecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaMolecular Science and Biomedicine Laboratory (MBL), State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, College of Biology, Aptamer Engineering Center of Hunan Province, Hunan University, Changsha, Hunan 410082, ChinaNanozymes hold huge potential in various fields, but their much lower catalytic activities than natural enzymes greatly limit their extensive applications. Recent studies indicated that an enhanced enzyme-like activity could be obtained by decreasing the particle size through rational design because smaller nanoparticles (NPs) have larger surface-area-to-volume ratios and more unsaturated sites, which are beneficial to the adsorption of reactant species. However, ultrasmall NPs have low adsorption energy and poor stability, which makes the synthesis of superstable and ultrasmall nanozymes extremely difficult. Several interesting works reported that the encapsulation of ultrasmall NPs with few-layer carbon shells could effectively protect them from dissolution and agglomeration, and meanwhile, their catalytic activities were not greatly affected. Herein, we report a superstable and ultrasmall graphene encapsuled CoRu nanocrystal (CoRu@G) with the CoRu alloy confined in the nanospace of few-layer graphene via the chemical vapor deposition method. It shows excellent corrosion resistance in aqua regia due to the protection of the chemically inert graphitic shell. The intrinsic peroxidase-, oxidase-, and catalase-like activities of the CoRu@G are systematically explored, including the influence of the concentration, pH, and temperature on the enzyme-like activity, steady-state kinetic analysis, and catalytic oxidation mechanism study. Significantly, the CoRu@G shows an excellent and ultrastable enzyme-like activity with the treatment of high temperatures, buffered solutions, or NaCl solutions probably because the graphene layer protects it from dissolution and agglomeration efficiently. We believe that the proposed graphene confinement strategy could highlight the direction of highly active, superstable, and ultrasmall-sized nanozyme preparation.http://dx.doi.org/10.1063/5.0048777