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 Laurent, P.
Right arrow Articles by Orange, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Laurent, P.
Right arrow Articles by Orange, N.
Agricola
Right arrow Articles by Laurent, P.
Right arrow Articles by Orange, N.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, April 2000, p. 1538-1543, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Production of Pectate Lyases and Cellulases by Chryseomonas luteola Strain MFCL0 Depends on the Growth Temperature and the Nature of the Culture Medium: Evidence for Two Critical Temperatures

P. Laurent, L. Buchon, J. F. Guespin-Michel, and N. Orange*

Laboratoire de Microbiologie du Froid, UPRES 2123, IFR CNRS 61, Université de Rouen, 27000 Evreux, France

Received 17 August 1999/Accepted 17 December 1999

Several extracellular enzymes that are responsible for plant tissue maceration were detected in culture supernatant of the psychrotrophic bacterium Chryseomonas luteola MFCL0. Isoelectrofocusing experiments showed that pectate lyase (PL) activity resulted from the cumulative action of three major isoenzymes, designated PLI, PLII, and PLIII. Cellulolytic activity was also detected in culture supernatants. These enzymes exhibited different behaviors with respect to growth temperature. PLII was not regulated by temperature, whereas PLI and PLIII were regulated similarly by growth temperature. Maximal levels of PLI and PLIII were produced at 14°C when cells were grown in polygalacturonate-containing synthetic medium and at around 20 to 24°C in nutrient broth. In contrast, thermoregulation of cellulolytic activity production differed from thermoregulation of PL. The level of cellulolytic activity was low in all media at temperatures up to 20°C, and then it increased dramatically until the temperature was 28°C, which is the optimal temperature for growth of C. luteola. Previously, we defined the critical temperature by using the modified Arrhenius equation to characterize bacterial behavior. This approach consists of monitoring changes in the maximal specific growth rate as a function of temperature. Our most striking result was the finding that the temperature at which maximum levels of PLI and PLIII were produced in two different media was the same as the critical temperature for growth observed in these two media.


* Corresponding author. Mailing address: Laboratoire de Microbiologie du Froid, 55 rue Saint-Germain, 27000 Evreux, France. Phone and fax: (33) 02 32 29 15 66. E-mail: nicole.orange{at}univ-rouen.fr.


Applied and Environmental Microbiology, April 2000, p. 1538-1543, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Moreau, M., Feuilloley, M. G. J., Veron, W., Meylheuc, T., Chevalier, S., Brisset, J.-L., Orange, N. (2007). Gliding Arc Discharge in the Potato Pathogen Erwinia carotovora subsp. atroseptica: Mechanism of Lethal Action and Effect on Membrane-Associated Molecules. Appl. Environ. Microbiol. 73: 5904-5910 [Abstract] [Full Text]  
  • Chihab, W., Alaoui, A. S., Amar, M. (2004). Chryseomonas luteola Identified as the Source of Serious Infections in a Moroccan University Hospital. J. Clin. Microbiol. 42: 1837-1839 [Abstract] [Full Text]  
  • Park, S.-Y., Lee, S. J., Oh, T.-K., Oh, J.-W., Koo, B.-T., Yum, D.-Y., Lee, J.-K. (2003). AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria. Microbiology 149: 1541-1550 [Abstract] [Full Text]