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Title: Purification and characterization of a XIP-type endoxylanase inhibitor from Rice (Oryza sativa)
Authors: Goesaert, Hans ×
Gebruers, Kurt
Courtin, Christophe
Delcour, Jan #
Issue Date: 2005
Publisher: Taylor & francis ltd
Series Title: Journal of enzyme inhibition and medicinal chemistry vol:20 issue:1 pages:95-101
Abstract: A rice XIP-type inhibitor was purified by affinity chromatography with an immobilized Aspergillus aculeatus family 10 endoxylanase. Rice XIP is a monomeric protein, with a molecular mass of ca. 32 kDa and a pI of ca. 5.6. Its N-terminal amino acid sequence was identical to that of a rice chitinase homologue, demonstrating the difficulty when using sequence information to differentiate between endoxylanase inhibitors and (putative) chitinases in rice. Rice XIP inhibited different endoxylanases to a varying degree. In particular, it most strongly inhibited family 10 endoxylanases from A. niger and A. oryzae, while several family 11 enzymes from Bacillus subtilis, A. niger and Trichoderma sp. were not sensitive to inhibition. The above mentioned A. aculeatus endoxylanase was not inhibited either, although gel permeation chromatography revealed that it complexed rice XIP in a 1: 1 molar stoichiometric ratio.
URI: 
ISSN: 1475-6366
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

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