Purification of TAXI-like endoxylanase inhibitors from wheat (Triticum aestivum L.) whole meal reveals a family of iso-forms.
An affinity chromatography method has been developed for purification of endoxylanase inhibitors concentrated by cation exchange chromatography from wheat whole meal and is based on immobilisation of a Bacillus subtilis family 11 endoxylanase on N-hydroxysuccinimide activated Sepharose 4 Fast Flow. When followed by high-resolution cation exchange chromatography, the purification of seven TAXIs, Triticum aestivum L. endoxylanase inhibitors was achieved so extending the number of such proteins known to date (TAXI I and II). Based on their inhibition activities against a B. subtilis family 11 and an Aspergillus niger family 11 endoxylanase, six TAXI I- and only one TAXI II-like inhibitor could be distinguished. The first type of endoxylanase inhibitor is active against both endoxylanases and the second type only has significant activity against the B. subtilis endoxylanase.
D001412:Bacillus subtilis / Q000201:enzymology; D002846:Chromatography, Affinity; D043364:Endo-1,4-beta Xylanases; D004791:Enzyme Inhibitors / Q000302:isolation & purification / Q000494:pharmacology; D007525:Isoelectric Focusing; D010940:Plant Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D020033:Protein Isoforms / Q000302:isolation & purification / Q000494:pharmacology; D014908:Triticum / Q000737:chemistry*; D014995:Xylosidases / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D010940:Plant Proteins; D020033:Protein Isoforms; C422246:TAXI I protein, Triticum aestivum; C422247:TAXI II protein, Triticum aestivum; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases