Prebleaching of kraft pulp with full-length and truncated forms of a thermostable modular xylanase from Rhodothermus marinus

N Pfabigan, Eva Nordberg Karlsson, G Ditzelmueller, Olle Holst

Research output: Contribution to journalArticlepeer-review

5 Citations (SciVal)

Abstract

Full-length and truncated forms of a modular thermostable xylanase (EC 3.2.1.8., glycoside hydrolase family 10) were used in bleaching sequences of hardwood and softwood kraft pulps. Enzymatic treatment led to brightness gains of all pulps but the result depended on the pulp source. The presence of the additional domains in the full-length enzyme (including carbohydrate-binding modules) did not improve the bleaching process. No significant change in viscosity was seen after enzyme treatments indicating an unaffected pulp fibre length.
Original languageEnglish
Pages (from-to)1191-1197
JournalBiotechnology Letters
Volume24
Issue number14
DOIs
Publication statusPublished - 2002

Subject classification (UKÄ)

  • Industrial Biotechnology

Keywords

  • carbohydrate binding module
  • CBM
  • GH10
  • glycoside hydrolase family 10

Fingerprint

Dive into the research topics of 'Prebleaching of kraft pulp with full-length and truncated forms of a thermostable modular xylanase from Rhodothermus marinus'. Together they form a unique fingerprint.

Cite this