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GrainGenes Reference Report: JCS-38-317

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Reference
JCS-38-317
Title
XIP-type endoxylanase inhibitors in different cereals
Journal
Journal of Cereal Science
Year
2003
Volume
38
Pages
317-324
Author
Goesaert H
Gebruers K
Brijs K
Courtin CM
Delcour JA
Abstract
Summary: Highly pure XIP-type (for Xylanase Inhibiting Protein) endoxylanase inhibitor fractions were selectively obtained with a high yield from rye, durum wheat, barley, and maize extracts by affinity chromatography with immobilised Aspergillus niger endoxylanase Xyn1 following removal of the TAXI-type (for Triticum aestivum xylanase inhibitor) endoxylanase inhibitors by affinity chromatography with immobilised Bacillus subtilis endoxylanase XynA. No inhibitors belonging to the XIP family occur in rice, oats, and buckwheat. N-terminal amino acid sequences of the non-wheat XIP-type inhibitors were very similar or identical to those of wheat XIP-1, a chitinase homologue. The isolated inhibitors are basic, monomeric proteins of ca. 30 kDa with pI values of at least 8.5 (rye, durum wheat, and barley XIP) and ca. 7.0 (maize XIP). They are, in general, active against fungal endoxylanases and do not hydrolyse chitin. SDS-PAGE analysis and high-resolution cation exchange chromatography suggest the presence of multiple XIP-type isoinhibitors in the different cereals
Keyword
[ Hide all but 1 of 28 ]
affinity chromatography
amino
amino acid sequence
arabinoxylans
barley
chitin
chitinase
durum
endoxylanase inhibitor
family
food
inhibitor
maize
niger
oat
purification
rice
rye
sds page
sequence
solubilization
taxi-type
triticum
triticum aestivum
values
xylanase inhibiting protein
xylanases
yield

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