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Applied and Environmental Microbiology, August 2007, p. 5378-5381, Vol. 73, No. 16
0099-2240/07/$08.00+0     doi:10.1128/AEM.00452-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis{triangledown}

Jesús Torres-Bacete,1 Daniel Hormigo,1 Maribel Stuart,1 Miguel Arroyo,1 Pedro Torres,1 María P. Castillón,1 Carmen Acebal,1 José L. García,2 and Isabel de la Mata1*

Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, C/ José Antonio Nováis 2, 28040 Madrid, Spain,1 Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas, CSIC, C/ Ramiro de Maeztu 9, 28040 Madrid, Spain2

Received 27 February 2007/ Accepted 9 June 2007

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.

* Corresponding author. Mailing address: Departamento de Bioquímica y Biología Molecular I Facultad de Biología, Universidad Complutense, C/ José Antonio Nováis 2, 28040 Madrid, Spain. Phone: 34-91-3945120. Fax: 34-91-3944672. E-mail: isabel{at}bbm1.ucm.es

{triangledown} Published ahead of print on 22 June 2007.

Applied and Environmental Microbiology, August 2007, p. 5378-5381, Vol. 73, No. 16
0099-2240/07/$08.00+0     doi:10.1128/AEM.00452-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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