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 Waché, Y.
Right arrow Articles by Belin, J.-M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Waché, Y.
Right arrow Articles by Belin, J.-M.
Agricola
Right arrow Articles by Waché, Y.
Right arrow Articles by Belin, J.-M.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, March 2000, p. 1233-1236, Vol. 66, No. 3
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Involvement of Acyl Coenzyme A Oxidase Isozymes in Biotransformation of Methyl Ricinoleate into gamma -Decalactone by Yarrowia lipolytica

Yves Waché,1,* Céline Laroche,1 Karin Bergmark,1 Charlotte Møller-Andersen,1 Mario Aguedo,1 Marie-Thérèse Le Dall,2 Huijie Wang,2 Jean-Marc Nicaud,2 and Jean-Marc Belin1

Laboratoire de Biotechnologie, Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation, Université de Bourgogne, 21000 Dijon,1 and Laboratoire de Génétique des Micro-organismes, INRA-CNRS, URA1925, 78850 Thiverval-Grignon,2 France

Received 25 October 1999/Accepted 22 November 1999

We reported previously on the function of acyl coenzyme A (acyl-CoA) oxidase isozymes in the yeast Yarrowia lipolytica by investigating strains disrupted in one or several acyl-CoA oxidase-encoding genes (POX1 through POX5) (H. Wang et al., J. Bacteriol. 181:5140-5148, 1999). Here, these mutants were studied for lactone production. Monodisrupted strains produced similar levels of lactone as the wild-type strain (50 mg/liter) except for Delta pox3, which produced 220 mg of gamma -decalactone per liter after 24 h. The Delta pox2 Delta pox3 double-disrupted strain, although slightly affected in growth, produced about 150 mg of lactone per liter, indicating that Aox2p was not essential for the biotransformation. The Delta pox2 Delta pox3 Delta pox5 triple-disrupted strain produced and consumed lactone very slowly. On the contrary, the Delta pox2 Delta pox3 Delta pox4 Delta pox5 multidisrupted strain did not grow or biotransform methyl ricinoleate into gamma -decalactone, demonstrating that Aox4p is essential for the biotransformation.

* Corresponding author. Mailing address: Laboratoire de Biotechnologie, Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation, Université de Bourgogne, 1, esplanade Erasme, 21000 Dijon, France. Phone: 33 3 80 39 66 80. Fax: 33 3 80 39 66 41. E-mail: ywache{at}u-bourgogne.fr.

Applied and Environmental Microbiology, March 2000, p. 1233-1236, Vol. 66, No. 3
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Wache, Y., Aguedo, M., Choquet, A., Gatfield, I. L., Nicaud, J.-M., Belin, J.-M. (2001). Role of beta -Oxidation Enzymes in gamma -Decalactone Production by the Yeast Yarrowia lipolytica. Appl. Environ. Microbiol. 67: 5700-5704 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»