Effect of glycosylation and additional domains on the thermostability of a family 10 xylanase produced by Thermopolyspora flexuosa

Appl Environ Microbiol. 2010 Jan;76(1):356-60. doi: 10.1128/AEM.00357-09. Epub 2009 Oct 23.

Abstract

The effects of different structural features on the thermostability of Thermopolyspora flexuosa xylanase XYN10A were investigated. A C-terminal carbohydrate binding module had only a slight effect, whereas a polyhistidine tag increased the thermostability of XYN10A xylanase. In contrast, glycosylation at Asn26, located in an exposed loop, decreased the thermostability of the xylanase. The presence of a substrate increased stability mainly at low pH.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / enzymology*
  • Endo-1,4-beta Xylanases / chemistry*
  • Endo-1,4-beta Xylanases / genetics
  • Endo-1,4-beta Xylanases / metabolism
  • Enzyme Stability
  • Glycosylation
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Protein Structure, Tertiary / genetics

Substances

  • Endo-1,4-beta Xylanases