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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2874| Title: | Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis |
| Publisher: | American Society for Microbiology |
| Description: | We express our gratitude to J. A. Salas from the University of Oviedo for providing the pEM4 expression vector. Aculeacin 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. This work was supported by grant BIO 2003-04832 from the Spanish Ministry of Education and Science. Peer reviewed |
| URI: | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2874 |
| Other Identifiers: | Appl Environ Microbiol. 2007 August; 73(16): 5378–5381 PMCID: 1950969 http://hdl.handle.net/10261/2874 10.1128/AEM.00452-07 |
| Appears in Collections: | Digital Csic |
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