Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 20255
Title Crosslinked xylan as an affinity adsorbent for endo-xylanases.
Author(s) Rozie, H.; Somers, W.; Bonte, A.; Rombouts, F.M.; Visser, J.
Source Carbohydrate Polymers 17 (1992). - ISSN 0144-8617 - p. 19 - 28.
DOI https://doi.org/10.1016/0144-8617(92)90019-M
Department(s) Laboratory of Genetics
Food Chemistry and Microbiology
Publication type Refereed Article in a scientific journal
Publication year 1992
Abstract In order to facilitate the purification of xylanases from Aspergillus niger, an affinity adsorbent has been developed from oat spelts xylan. A suitable adsorbent was only obtained by crosslinking oat spelts xylan with epichlorohydrin in water but not in ethanol or ethanol-water mixtures. After some initial degradation of the adsorbent (approximately 4%), no significant biodegradation was measured with a reused adsorbent. Up to 60% of the xylanase activity from an Aspergillus niger enzyme mixture (50 mU/ml) was adsorbed at pH 4 (50 mm sodium acetate buffer). The degree of adsorption to crosslinked xylan of four fractions of this preparation, previously separated by DEAE-Biogel A chromatography, varied between 40 and 90%.

Adsorption was strongly dependent on pH and ionic strength and desorption was easily accomplished by an increase in ionic strength. In addition to xylanases, polygalacturonases were also adsorbed to the matrix. No significant adsorption of β-d-xylosidase, α-l-arabinofuranosidase, β-d-galactosidase, β-(1,4)-galactanase,
β-(1-36)-d-galactanase
or cellulase activities was found.
Comments
There are no comments yet. You can post the first one!
Post a comment
 
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.