Algerian pearl millet ( Pennisetum glaucum L.) contains XIP but not TAXI and TLXI type xylanase inhibitors.
An XIP (xylanase inhibiting protein) type xylanase inhibitor was purified from Algerian pearl millet ( Pennisetum glaucum L.) grains and characterized for the first time. Cation exchange and affinity chromatography with immobilized Trichoderma longibrachiatum glycoside hydrolase (GH) family 11 xylanase resulted in electrophoretically pure protein with a molecular mass of 27-29 kDa and a pI value of 6.7. The experimentally determined N-terminal amino acid sequence of the purified XIP protein is 87.5%, identical to that of sorghum ( Sorghum bicolor L.) XIP and 79.2% identical to that of wheat ( Triticum aestivum L.) XIP-I. The biochemical properties of pearl millet XIP are comparable to those described earlier for sorghum XIP, except for the higher specific activity toward a T. longibrachiatum GH family 11 xylanase. On the basis of immunoblot neither TAXI nor TLXI type xylanase inhibitors were detected in pearl millet grains.
Mokrane
Hind
H
Laboratoire des Produits Bioactifs et de la Valorisation de la Biomasse, Ecole Normale Superieure, Vieux-Kouba, Alger, Algeria.
Gebruers
Kurt
K
Beaugrand
Johnny
J
Proost
Paul
P
Nadjemi
Boubekeur
B
Belhanèche-Bensemra
Naima
N
Courtin
Christophe M
CM
Delcour
Jan A
JA
D000595:Amino Acid Sequence; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D031782:Pennisetum / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D014995:Xylosidases / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D010940:Plant Proteins; D014995:Xylosidases