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Recent advances in the synthesis and applications of single-atom nanozymes in food safety monitoring

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dc.contributor.authorZhang, Daohong-
dc.contributor.authorKukkar, Deepak-
dc.contributor.authorKaur, Harsimran-
dc.contributor.authorKim, Ki-Hyun-
dc.date.accessioned2024-11-28T15:02:26Z-
dc.date.available2024-11-28T15:02:26Z-
dc.date.issued2023-09-
dc.identifier.issn0001-8686-
dc.identifier.issn1873-3727-
dc.identifier.urihttps://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/197215-
dc.description.abstractNanozymes are synthetic compounds with enzyme-like tunable catalytic properties. The success of nanozymes for catalytic applications can be attributed to their small dimensions, cost-effective synthesis, appreciable stability, and scalability to molecular dimensions. The emergence of single atom nanozymes (SANzymes) has opened up new possibilities in bioanalytical applications. In this regard, this review outlines enzyme-mimicking features of SANzymes for food safety applications in relation to the key variables controlling their catalytic performance. The discussion is extended further to cover the applications of SANzymes for the monitoring of various compounds/biomaterials of significance with respect to food safety (e.g., pesticides, veterinary drug residues, foodborne pathogenic bacteria, mycotoxins/bacterial endotoxin, antioxidant residues, hydrogen peroxide residues, and heavy metal ions). Furthermore, the performance of SANzymes is evaluated in terms of various performance metrics such as limit of detection (LOD), linear dynamic range, and figure of merit (FoM). The challenges and future road map for the applications of SANzymes are also addressed along with their upscaling in the area of food safety.-
dc.format.extent19-
dc.language영어-
dc.language.isoENG-
dc.publisherElsevier BV-
dc.titleRecent advances in the synthesis and applications of single-atom nanozymes in food safety monitoring-
dc.typeArticle-
dc.publisher.location네델란드-
dc.identifier.doi10.1016/j.cis.2023.102968-
dc.identifier.scopusid2-s2.0-85167829263-
dc.identifier.wosid001147913300001-
dc.identifier.bibliographicCitationAdvances in Colloid and Interface Science, v.319, pp 1 - 19-
dc.citation.titleAdvances in Colloid and Interface Science-
dc.citation.volume319-
dc.citation.startPage1-
dc.citation.endPage19-
dc.type.docTypeReview-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalWebOfScienceCategoryChemistry, Physical-
dc.subject.keywordPlusPEROXIDASE-LIKE ACTIVITY-
dc.subject.keywordPlusOXYGEN REDUCTION-
dc.subject.keywordPlusHORSERADISH-PEROXIDASE-
dc.subject.keywordPlusPROPYL GALLATE-
dc.subject.keywordPlusHEAVY-METALS-
dc.subject.keywordPlusENZYME-
dc.subject.keywordPlusSITES-
dc.subject.keywordPlusBUTYRYLCHOLINESTERASE-
dc.subject.keywordPlusMYCOTOXINS-
dc.subject.keywordPlusCATALYSTS-
dc.subject.keywordAuthorBiosensing-
dc.subject.keywordAuthorColloidal particles-
dc.subject.keywordAuthorEnzyme catalysis-
dc.subject.keywordAuthorFood safety-
dc.subject.keywordAuthorPerformance comparison-
dc.subject.keywordAuthorSANzymes-
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0001868623001355?via%3Dihub-
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