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 O'Connell Motherway, M.
Right arrow Articles by van Sinderen, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O'Connell Motherway, M.
Right arrow Articles by van Sinderen, D.
Agricola
Right arrow Articles by O'Connell Motherway, M.
Right arrow Articles by van Sinderen, D.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, October 2008, p. 6271-6279, Vol. 74, No. 20
0099-2240/08/$08.00+0     doi:10.1128/AEM.01169-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of ApuB, an Extracellular Type II Amylopullulanase from Bifidobacterium breve UCC2003{triangledown}

Mary O'Connell Motherway,1,2 Gerald F. Fitzgerald,1,2,3 Sabine Neirynck,1 Sinead Ryan,1,2 Lothar Steidler,1 and Douwe van Sinderen1,2*

Alimentary Pharmabiotic Centre,1 Departments of Microbiology,2 Food and Nutritional Sciences, National University of Ireland, Cork, Western Road, Cork, Ireland3

Received 26 May 2008/ Accepted 31 July 2008

The apuB gene of Bifidobacterium breve UCC2003 was shown to encode an extracellular amylopullulanase. ApuB is composed of a distinct N-terminally located {alpha}-amylase-containing domain which hydrolyzes {alpha}-1,4-glucosidic linkages in starch and related polysaccharides and a C-terminally located pullulanase-containing domain which hydrolyzes {alpha}-1,6 linkages in pullulan, allowing the classification of this enzyme as a bifunctional class II pullulanase. A knockout mutation of the apuB gene in B. breve UCC2003 rendered the resulting mutant incapable of growth in medium containing starch, amylopectin, glycogen, or pullulan as the sole carbon and energy source, confirming the crucial physiological role of this gene in starch metabolism.

* Corresponding author. Mailing address: Room 4.05, Department of Microbiology, National University of Ireland, Cork, Western Road, Cork, Ireland. Phone: 00 353 21 490 1365. Fax: 00 353 21 490 3101. E-mail: d.vansinderen{at}ucc.ie

{triangledown} Published ahead of print on 8 August 2008.

Applied and Environmental Microbiology, October 2008, p. 6271-6279, Vol. 74, No. 20
0099-2240/08/$08.00+0     doi:10.1128/AEM.01169-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Klaassens, E. S., Boesten, R. J., Haarman, M., Knol, J., Schuren, F. H., Vaughan, E. E., de Vos, W. M. (2009). Mixed-Species Genomic Microarray Analysis of Fecal Samples Reveals Differential Transcriptional Responses of Bifidobacteria in Breast- and Formula-Fed Infants. Appl. Environ. Microbiol. 75: 2668-2676 [Abstract] [Full Text]  
  • Pokusaeva, K., O'Connell-Motherway, M., Zomer, A., Fitzgerald, G. F., van Sinderen, D. (2009). Characterization of Two Novel {alpha}-Glucosidases from Bifidobacterium breve UCC2003. Appl. Environ. Microbiol. 75: 1135-1143 [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»