Title: Purification and characterization of strongly chitin-binding chitinases from salicylic acid-treated leek (Allium porrum)
Authors: Vergauwen, Rudolf ×
Van Leuven, Freddy
Van Laere, André #
Issue Date: Oct-1998
Publisher: Munksgaard int publ ltd
Series Title: Physiologia plantarum vol:104 issue:2 pages:175-182
Abstract: Six chitinases (EC were purified from salicylate-treated leek (Allium porrum L.). They all strongly bind to chitin and can roughly be divided into two groups. One group has blocked W-termini, is completely inhibited by 1 mM AgNO3, has a relatively narrow pH optimum, a temperature optimum of 40 degrees C and cannot degrade the tetramer of chitin. The other group has unblocked N-termini showing homology to the chitin-binding lectin WGA and is therefore considered as class I chitinases. This group is only moderately inhibited by 1 mM AgNO3 (30%), has a relatively broad pH optimum, has a higher temperature optimum (50 to 60 degrees C) and can degrade the tetramer of chitin to dimers. Furthermore, all isoforms have molecular masses around 34 kDa as estimated by SDS-PAGE. They have isoelectric points ranging From 4 to 8 and no detectable lysozyme activity. Two isoforms investigated in more detail differ in their antifungal potential.
ISSN: 0031-9317
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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