Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
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 Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
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 CrossRef
Right arrow Citing Articles via Web of Science (48)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mutter, M.
Right arrow Articles by Voragen, AGJ.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mutter, M.
Right arrow Articles by Voragen, AGJ.
Agricola
Right arrow Articles by Mutter, M.
Right arrow Articles by Voragen, AGJ.

PLANT PHYSIOLOGY , Vol 106, Issue 1 241-250, Copyright © 1994 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Rhamnogalacturonan [alpha]-L-Rhamnopyranohydrolase (A Novel Enzyme Specific for the Terminal Nonreducing Rhamnosyl Unit in Rhamnogalacturonan Regions of Pectin)

M. Mutter, G. Beldman, H. A. Schols and AGJ. Voragen
Wageningen Agricultural University, Department of Food Chemistry, Bomenweg 2, 6703 HD Wageningen, The Netherlands

Two [alpha]-L-rhamnohydrolases with different substrate specificities were isolated from a commercial preparation produced by Aspergillus aculeatus. The first rhamnohydrolase was active toward p-nitrophenyl-[alpha]-L-rhamnopyranoside, naringin, and hesperidin and was termed p-nitrophenyl-[alpha]-L-rhamnopyranohydrolase (pnp-rhamnohydrolase). From the data collected, the enzyme seemed specific for the [alpha]-1,2- or [alpha]-1,6-linkage to [beta]-D-glucose. The pnp-rhamnohydrolase had a molecular mass of 87 kD (sodium dodecyl sulfate-polyacrylamide gel electrophoresis), a pH optimum of 5.5 to 6, a temperature optimum of 60[deg]C, and a specific activity toward pnp-[alpha]-L-rhamnopyranoside (pnp-Rha) of 13 units mg-1 protein. The second rhamnohydrolase, on the contrary, was active toward rhamnogalacturonan (RG) fragments, releasing Rha, and was therefore termed RG-rhamnohydrolase. The RG-rhamnohydrolase had a molecular mass of 84 kD, a pH optimum of 4, a temperature optimum of 60[deg]C, and a specific activity toward RG oligomers of 60 units mg-1 protein. The RG-rhamnohydrolase liberated Rha from the nonreducing end of the RG chain and appeared specific for the [alpha]-1,4-linkage to [alpha]-D-galacturonic acid. The enzyme was hindered when this terminal Rha residue was substituted at the 4-position by a [beta]-D-galactose. The results so far obtained did not indicate particular preference of the enzyme for low or high molecular mass RG fragments. From the results it can be concluded that a new enzyme, an RG [beta]-L-rhamnopyranohydrolase, has been isolated with high specificity toward RG regions of pectin.


This article has been cited by other articles:


Home page
 Appl. Environ. Microbiol.Home page
A. Ochiai, T. Itoh, A. Kawamata, W. Hashimoto, and K. Murata
Plant Cell Wall Degradation by Saprophytic Bacillus subtilis Strains: Gene Clusters Responsible for Rhamnogalacturonan Depolymerization
Appl. Envir. Microbiol., June 15, 2007; 73(12): 3803 - 3813.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
M. Laatu and G. Condemine
Rhamnogalacturonate Lyase RhiE Is Secreted by the Out System in Erwinia chrysanthemi
J. Bacteriol., March 1, 2003; 185(5): 1642 - 1649.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
R. P. de Vries and J. Visser
Aspergillus Enzymes Involved in Degradation of Plant Cell Wall Polysaccharides
Microbiol. Mol. Biol. Rev., December 1, 2001; 65(4): 497 - 522.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
P. Manzanares, H. C. van den Broeck, L. H. de Graaff, and J. Visser
Purification and Characterization of Two Different {alpha}-L-Rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus
Appl. Envir. Microbiol., May 1, 2001; 67(5): 2230 - 2234.
[Abstract] [Full Text]

Home page
 Appl. Environ. Microbiol.Home page
C. J. B. van der Vlugt-Bergmans, P. J. A. Meeuwsen, A. G. J. Voragen, and A. J. J. van Ooyen
Endo-Xylogalacturonan Hydrolase, a Novel Pectinolytic Enzyme
Appl. Envir. Microbiol., January 1, 2000; 66(1): 36 - 41.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
M. Mutter, I. J. Colquhoun, G. Beldman, H. A. Schols, E. J. Bakx, and A. G.J. Voragen
Characterization of Recombinant Rhamnogalacturonan alpha -l-Rhamnopyranosyl-(1,4)-alpha -d-Galactopyranosyluronide Lyase from Aspergillus aculeatus . An Enzyme That Fragments Rhamnogalacturonan I Regions of Pectin
Plant Physiology, May 1, 1998; 117(1): 141 - 152.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
M. Mutter, G. Beldman, S. M. Pitson, H. A. Schols, and A. G.J. Voragen
Rhamnogalacturonan alpha -d-Galactopyranosyluronohydrolase . An Enzyme That Specifically Removes the Terminal Nonreducing Galacturonosyl Residue in Rhamnogalacturonan Regions of Pectin
Plant Physiology, May 1, 1998; 117(1): 153 - 163.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
S. Kauppinen, S. Christgau, L. V. Kofod, T. Halkier, K. Dörreich, and H. Dalbřge
Molecular Cloning and Characterization of a Rhamnogalacturonan Acetylesterase from Aspergillus aculeatus
J. Biol. Chem., November 10, 1995; 270(45): 27172 - 27178.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1994 by the American Society of Plant Biologists