AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vera, J.
Right arrow Articles by Leon, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vera, J.
Right arrow Articles by Leon, O.
Agricola
Right arrow Articles by Vera, J.
Right arrow Articles by Leon, O.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 1998, p. 4378-4383, Vol. 64, No. 11
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of a Marine Agarolytic Pseudoalteromonas Isolate and Characterization of Its Extracellular Agarase

Jorge Vera,1 Raul Alvarez,1 Erminio Murano,2 Juan Carlos Slebe,1 and Oscar Leon1,*

Instituto de Bioquimica, Facultad de Ciencias, Universidad Austral de Chile, Valdivia, Chile,1 and POLYbios, Laboratorio Biopolimeri Tecnologici, Padriciano 99-I-34012, Trieste, Italy2

Received 6 February 1998/Accepted 23 July 1998

The phenotypic and agarolytic features of an unidentified marine bacteria that was isolated from the southern Pacific coast was investigated. The strain was gram negative, obligately aerobic, and polarly flagellated. On the basis of several phenotypic characters and a phylogenetic analysis of the genes coding for the 16S rRNA, this strain was identified as Pseudoalteromonas antarctica strain N-1. In solid agar, this isolate produced a diffusible agarase that caused agar softening around the colonies. An extracellular agarase was purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography on DEAE-cellulose. The purified protein was determined to be homogeneous on the basis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and it had a molecular mass of 33 kDa. The enzyme hydrolyzed the beta -1,4-glycosydic linkages of agar, yielding neoagarotetraose and neoagarohexaose as the main products, and exhibited maximal activity at pH 7. The enzyme was stable at temperatures up to 30°C, and its activity was not affected by salt concentrations up to 0.5 M NaCl.

* Corresponding author. Mailing address: Instituto de Bioquimica, Facultad de Ciencias, Universidad Austral de Chile, casilla 567, Valdivia, Chile. Phone: 56-63-221332. Fax: 56-63-229155. E-mail: Oleon{at}valdivia.uca.uach.cl.

Applied and Environmental Microbiology, November 1998, p. 4378-4383, Vol. 64, No. 11
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 1998 by the American Society for Microbiology. All rights reserved.