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 Google Scholar
Google Scholar
Right arrow Articles by Sakamoto, K.
Right arrow Articles by Konings, W. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sakamoto, K.
Right arrow Articles by Konings, W. N.
Agricola
Right arrow Articles by Sakamoto, K.
Right arrow Articles by Konings, W. N.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 2002, p. 5374-5378, Vol. 68, No. 11
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.11.5374-5378.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Membrane-Bound ATPase Contributes to Hop Resistance of Lactobacillus brevis

Kanta Sakamoto,1* H. W. van Veen,2,{dagger} Hiromi Saito,3 Hiroshi Kobayashi,3 and Wil N. Konings2

Fundamental Research Laboratory, Asahi Breweries, Ltd., Moriya-shi, Ibaraki 302-0106,1 Faculty of Pharmaceutical Science, Chiba University, Inage-ku, Chiba 263-8522, Japan,3 Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751NN Haren, The Netherlands2

Received 20 February 2002/ Accepted 2 August 2002

The activity of the membrane-bound H+-ATPase of the beer spoilage bacterium Lactobacillus brevis ABBC45 increased upon adaptation to bacteriostatic hop compounds. The ATPase activity was optimal around pH 5.6 and increased up to fourfold when L. brevis was exposed to 666 µM hop compounds. The extent of activation depended on the concentration of hop compounds and was maximal at the highest concentration tested. The ATPase activity was strongly inhibited by N,N'-dicyclohexylcarbodiimide, a known inhibitor of FoF1-ATPase. Western blots of membrane proteins of L. brevis with antisera raised against the {alpha}- and ß-subunits of FoF1-ATPase from Enterococcus hirae showed that there was increased expression of the ATPase after hop adaptation. The expression levels, as well as the ATPase activity, decreased to the initial nonadapted levels when the hop-adapted cells were cultured further without hop compounds. These observations strongly indicate that proton pumping by the membrane-bound ATPase contributes considerably to the resistance of L. brevis to hop compounds.

* Corresponding author. Mailing address: Fundamental Research Laboratory, Asahi Breweries, Ltd., 1-21, Midori 1-chome, Moriya-shi, Ibaraki 302-0106, Japan. Phone: 81 297 461504. Fax: 81 297 461506. E-mail: kanta.sakamoto{at}asahibeer.co.jp.

{dagger} Present address: Department of Pharmacology, University of Cambridge, CB2 1QJ Cambridge, United Kingdom.

Applied and Environmental Microbiology, November 2002, p. 5374-5378, Vol. 68, No. 11
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.11.5374-5378.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.





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