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 Dean, M.
Right arrow Articles by Bergamini, C. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dean, M.
Right arrow Articles by Bergamini, C. M.
Agricola
Right arrow Articles by Dean, M.
Right arrow Articles by Bergamini, C. M.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, June 2002, p. 3126-3128, Vol. 68, No. 6
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.6.3126-3128.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Characterization of Cholylglycine Hydrolase from a Bile-Adapted Strain of Xanthomonas maltophilia and Its Application for Quantitative Hydrolysis of Conjugated Bile Salts{dagger}

Mariangela Dean,1 Carlo Cervellati,1 Elena Casanova,2 Monica Squerzanti,1 Vincenzo Lanzara,1 Alessandro Medici,2 Patrizia Polverino de Laureto,3 and Carlo M. Bergamini1,4*

Department of Biochemistry and Molecular Biology,1 Department of Chemistry,2 ICSI, Centre for the Study of Inflammatory Diseases, University of Ferrara, 44100 Ferrara,4 CRIBI, Biotechnology Centre, University of Padua, Padua, Italy3

Received 26 October 2001/ Accepted 1 March 2002

Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60°C for up to 60 min, in agreement with calorimetric data.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Ferrara, Via Borsari 46, 44100 Ferrara, Italy. Phone: 0039-0532-291425. Fax: 0039-0532-202723. E-mail: bgc{at}dns.unife.it.

{dagger} This report is dedicated to the memory of our teacher, Mario Rippa, who suddenly died on 27 March 2001.

Applied and Environmental Microbiology, June 2002, p. 3126-3128, Vol. 68, No. 6
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.6.3126-3128.2002
Copyright © 2002, 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 © 2002 by the American Society for Microbiology. All rights reserved.