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dc.contributor.authorJang, E.
dc.contributor.authorSon, Y.
dc.contributor.authorPark, S.
dc.contributor.authorYoo, J.
dc.contributor.authorCho, Y.
dc.contributor.authorJeong, S.
dc.contributor.authorLiu, Shaomin
dc.contributor.authorSon, H.
dc.date.accessioned2018-04-30T02:40:26Z
dc.date.available2018-04-30T02:40:26Z
dc.date.created2018-04-16T07:41:29Z
dc.date.issued2017
dc.identifier.citationJang, E. and Son, Y. and Park, S. and Yoo, J. and Cho, Y. and Jeong, S. and Liu, S. et al. 2017. Improved biosynthesis of silver nanoparticles using keratinase from Stenotrophomonas maltophilia R13: reaction optimization, structural characterization, and biomedical activity. Bioprocess and Biosystems Engineering: pp. 1-13.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/66369
dc.identifier.doi10.1007/s00449-017-1873-0
dc.description.abstract

© 2017 Springer-Verlag GmbH Germany, part of Springer Nature In the present study, keratinase from Stenotrophomonas maltophilia R13 was used for the first time as a reducing agent for the eco-friendly synthesis of AgNPs. The keratinase produced by strain R13 was responsible for the reduction of silver ions and the subsequent formation of AgNPs. Maximum AgNP synthesis was achieved using 2 mM AgNO 3 at pH 9 and 40 °C. Electron microscopy and dynamic light scattering analysis showed AgNPs were spherical and of average diameter ~ 8.4 nm. X-ray diffraction revealed that AgNPs were crystalline. FTIR indicated AgNPs were stabilized by proteins present in the crude enzyme solution of strain R13. AgNPs exhibited a broad antimicrobial spectrum against several pathogenic microorganisms, and the antimicrobial mechanism appeared to involve structural deformation of cells resulting in membrane leakage and subsequent lysis. AgNPs also displayed 1,1-diphenyl-2-picrylhydrazyl (IC 50 = 0.0112 mg/ml), 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonate radical scavenging (IC 50 = 0.0243 mg/ml), and anti-collagenase (IC 50 = 23.5 mg/ml) activities.

dc.titleImproved biosynthesis of silver nanoparticles using keratinase from Stenotrophomonas maltophilia R13: reaction optimization, structural characterization, and biomedical activity
dc.typeJournal Article
dcterms.source.startPage1
dcterms.source.endPage13
dcterms.source.issn1615-7591
dcterms.source.titleBioprocess and Biosystems Engineering
curtin.departmentWASM: Minerals, Energy and Chemical Engineering (WASM-MECE)
curtin.accessStatusFulltext not available


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