Modification of cellulose fiber surfaces by use of a lipase and a xyloglucan endotransglycosylase
2005 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 6, no 1, 196-203 p.Article in journal (Refereed) Published
A strategy for the modification of cellulose fiber surfaces was developed that used the ability of Candida antarctica lipase B (CALB) to acylate carbohydrates with high regioselectivity, combined with the transglycosylating activity of the Populus tremula x P. tremuloides xyloglucan endotransglycosylase 16A (PttXET16A). Xyloglucan oligosaccharides (XGOs) prepared from tamarind xyloglucan were acylated with CALB as a catalyst and vinyl stearate or gamma-thiobutyrolactone as acyl donors to produce carbohydrate molecules with hydrophobic alkyl chains or reactive sulfhydryl groups, respectively. The modified XGOs were shown to act as glycosyl acceptors in the transglycosylation reaction catalyzed by PttXET16A and could therefore be incorporated into high M-r xyloglucan chains. The resulting xyloglucan molecules exhibited a high affinity for cellulose surfaces, which enabled the essentially irreversible introduction of fatty acid esters or thiol groups to cellulose fibers.
Place, publisher, year, edition, pages
2005. Vol. 6, no 1, 196-203 p.
ring-opening polymerization, fatty-acid esters, plant-cell walls, organic media, enzymatic acylation, catalyzed synthesis, pichia-pastoris, fusion protein, oligosaccharides, optimization
IdentifiersURN: urn:nbn:se:kth:diva-14465DOI: 10.1021/bm049588iISI: 000226344300027ScopusID: 2-s2.0-14044277441OAI: oai:DiVA.org:kth-14465DiVA: diva2:332506
QC 201005252010-08-052010-08-05Bibliographically approved