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Article: Entrapment of a Trigonopsis variabilis D-amino acid oxidase variant F54Y for oxidative deamination of cephalosporin C

TitleEntrapment of a Trigonopsis variabilis D-amino acid oxidase variant F54Y for oxidative deamination of cephalosporin C
Authors
KeywordsAlginate
D-Amino acid oxidase
Entrapment
Issue Date2011
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jabout/85007410/2129_info.html
Citation
Engineering In Life Sciences, 2011, v. 11 n. 5, p. 491-495 How to Cite?
AbstractTrigonopsis variabilis D-amino acid oxidase (TvDAAO) is an enzyme used in the industrial bioconversion of cephalosporin C (CPC) into 7-aminocephalosporanic acid, a crucial biosynthetic nucleus for a wide spectrum of semi-synthetic cephem antibiotics. Using homology modeling and site-directed mutagenesis, we have previously shown that the TvDAAO variant F54Y possesses improved catalytic activity and thermostability. To further explore its industrial application, the conditions for immobilization of the enzyme were examined in the present investigation. The results showed that entrapment in a calcium alginate (Ca-alginate) matrix using 2% alginate, 500mM CaCl 2, and 15min stabilization appeared to be optimal for the immobilization of F54Y. The entrapped enzyme allowed complete CPC conversion. The entrapped enzyme also showed good operational stability and retained at least 90% of its original activity after 20 reaction cycles. To conclude, the entrapment of F54Y in Ca-alginate appeared to be a simple and efficient biocatalysis system with potential application in the antibiotics industry. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Persistent Identifierhttp://hdl.handle.net/10722/134977
ISSN
2015 Impact Factor: 2.119
2015 SCImago Journal Rankings: 0.726
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants Council of the Hong Kong Special Administrative Region, ChinaHKU 475007M
Funding Information:

The work described in this paper was fully supported by a grant from the Research Grants Council of the Hong Kong Special Administrative Region, China (Project no. HKU 475007M).

References
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DC FieldValueLanguage
dc.contributor.authorWong, KSen_HK
dc.contributor.authorFong, WPen_HK
dc.contributor.authorTsang, PWKen_HK
dc.date.accessioned2011-07-27T01:25:17Z-
dc.date.available2011-07-27T01:25:17Z-
dc.date.issued2011en_HK
dc.identifier.citationEngineering In Life Sciences, 2011, v. 11 n. 5, p. 491-495en_HK
dc.identifier.issn1618-0240en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134977-
dc.description.abstractTrigonopsis variabilis D-amino acid oxidase (TvDAAO) is an enzyme used in the industrial bioconversion of cephalosporin C (CPC) into 7-aminocephalosporanic acid, a crucial biosynthetic nucleus for a wide spectrum of semi-synthetic cephem antibiotics. Using homology modeling and site-directed mutagenesis, we have previously shown that the TvDAAO variant F54Y possesses improved catalytic activity and thermostability. To further explore its industrial application, the conditions for immobilization of the enzyme were examined in the present investigation. The results showed that entrapment in a calcium alginate (Ca-alginate) matrix using 2% alginate, 500mM CaCl 2, and 15min stabilization appeared to be optimal for the immobilization of F54Y. The entrapped enzyme allowed complete CPC conversion. The entrapped enzyme also showed good operational stability and retained at least 90% of its original activity after 20 reaction cycles. To conclude, the entrapment of F54Y in Ca-alginate appeared to be a simple and efficient biocatalysis system with potential application in the antibiotics industry. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_HK
dc.languageengen_US
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jabout/85007410/2129_info.htmlen_HK
dc.relation.ispartofEngineering in Life Sciencesen_HK
dc.subjectAlginateen_HK
dc.subjectD-Amino acid oxidaseen_HK
dc.subjectEntrapmenten_HK
dc.titleEntrapment of a Trigonopsis variabilis D-amino acid oxidase variant F54Y for oxidative deamination of cephalosporin Cen_HK
dc.typeArticleen_HK
dc.identifier.emailTsang, PWK:pwktsang@hku.hken_HK
dc.identifier.authorityTsang, PWK=rp01388en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/elsc.201000135en_HK
dc.identifier.scopuseid_2-s2.0-80054104827en_HK
dc.identifier.hkuros187280en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-80054104827&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume11en_HK
dc.identifier.issue5en_HK
dc.identifier.spage491en_HK
dc.identifier.epage495en_HK
dc.identifier.eissn1618-2863-
dc.identifier.isiWOS:000300111800006-
dc.publisher.placeGermanyen_HK
dc.relation.projectCharacterization of highly active, thermostable mutants of Trigonopsis variabilis D-Amino acid oxidase for antibiotics production: Kinetic measurements, structural studies and beyond-
dc.identifier.scopusauthoridWong, KS=35191126000en_HK
dc.identifier.scopusauthoridFong, WP=7102816006en_HK
dc.identifier.scopusauthoridTsang, PWK=8334953500en_HK

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