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dc.creatorGarcía, José Luis-
dc.creatorHormigo, Daniel-
dc.creatorStuart, Maribel-
dc.creatorArroyo, Miguel-
dc.creatorTorres, Pedro-
dc.creatorTorres-Bacete, Jesús-
dc.creatorCastillón, María Pilar-
dc.creatorAcebal, Carmen-
dc.creatorMata, Isabel de la-
dc.date2008-02-06T12:15:35Z-
dc.date2008-02-06T12:15:35Z-
dc.date2007-06-22-
dc.date.accessioned2017-01-31T00:59:58Z-
dc.date.available2017-01-31T00:59:58Z-
dc.identifierAppl Environ Microbiol. 2007 August; 73(16): 5378–5381-
dc.identifierPMCID: 1950969-
dc.identifierhttp://hdl.handle.net/10261/2874-
dc.identifier10.1128/AEM.00452-07-
dc.identifier.urihttp://dspace.mediu.edu.my:8181/xmlui/handle/10261/2874-
dc.descriptionWe express our gratitude to J. A. Salas from the University of Oviedo for providing the pEM4 expression vector.-
dc.descriptionAculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM−1 s−1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C.-
dc.descriptionThis work was supported by grant BIO 2003-04832 from the Spanish Ministry of Education and Science.-
dc.descriptionPeer reviewed-
dc.format429459 bytes-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherAmerican Society for Microbiology-
dc.rightsopenAccess-
dc.titleNewly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis-
dc.typeArtículo-
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