JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Scolari, G.
Right arrow Articles by Vescovi, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Scolari, G.
Right arrow Articles by Vescovi, F.
J. Dairy Sci. 89:3800-3809
© American Dairy Science Association, 2006.

Extraction and Partial Characterization of Proteolytic Activities from the Cell Surface of Lactobacillus helveticus Zuc2

G. Scolari1, M. Vescovo, C. Zacconi and F. Vescovi

Istituto Microbiologia, Università Cattolica del Sacro Cuore (UCSC), via Emilia parmense, 84, 29100 Piacenza, Italy

1 Corresponding author: gianluigi.scolari{at}unicatt.it

Proteolytic activities were extracted from a dairy Lactobacillus helveticus strain and partially characterized. A first cell envelope proteinase (CEP) was extracted using a high ionic strength buffer, both in the presence and in the absence of Ca2+. Moreover, cell treatment by 5 M LiCl allowed for the selective removal of the S-layer protein and CEP, suggesting an enzyme ionic linkage to the cell envelope similar to that observed for the Slayer structure. The enzyme specificity against {alpha}s1-CN (f1–23) showed unusual activity on the Lys3-His4 bond compared with other proteinases of the same species. A second proteinase appeared to be linked to the cell membrane because it was extractable only after membrane disgregation by detergents. Its specificity against CN fractions and {alpha}s1-CN (f1–23) was different from that of the first CEP; moreover, the measured activity was lower than that of CEP.

Key Words: Lactobacillus helveticus • cell envelope • proteinase • specificity




This article has been cited by other articles:


Home page
 Appl. Environ. Microbiol.Home page
E. M. Hebert, G. Mamone, G. Picariello, R. R. Raya, G. Savoy, P. Ferranti, and F. Addeo
Characterization of the Pattern of {alpha}s1- and {beta}-Casein Breakdown and Release of a Bioactive Peptide by a Cell Envelope Proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
Appl. Envir. Microbiol., June 15, 2008; 74(12): 3682 - 3689.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by the American Dairy Science Association ®.