The GH26 β-mannanase RsMan26H from a symbiotic protist of the termite Reticulitermes speratus is an endo-processive mannobiohydrolase: heterologous expression and characterization

Biochem Biophys Res Commun. 2014 Sep 26;452(3):520-5. doi: 10.1016/j.bbrc.2014.08.103. Epub 2014 Aug 27.

Abstract

Symbiotic protists in the gut of termites are prominent natural resources for enzymes involved in lignocellulose degradation. Here we report expression, purification, and biochemical characterization of a glycoside hydrolase family 26 mannanase RsMan26H from the symbiotic protist of the lower termite, Reticulitermes speratus. Biochemical analysis of RsMan26H demonstrates that this enzyme is an endo-processive mannobiohydrolase producing mannobiose from oligo- and polysaccharides, followed by a minor accumulation of oligosaccharides larger than mannobiose. To our knowledge, this is the first report describing the unique mannobiohydrolase enzyme from the eukaryotic origin.

Keywords: Glycoside hydrolase family 26; Mannanase; Pichia pastoris expression; Processivity; Symbiotic protist; Termite.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Gene Expression
  • Isoptera / physiology
  • Kinetics
  • Mannans / chemistry*
  • Mannans / metabolism
  • Oligosaccharides / chemistry*
  • Oligosaccharides / metabolism
  • Parabasalidea / chemistry*
  • Parabasalidea / enzymology
  • Pichia / genetics
  • Pichia / metabolism
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism
  • Symbiosis
  • beta-Mannosidase / chemistry*
  • beta-Mannosidase / genetics
  • beta-Mannosidase / metabolism

Substances

  • Mannans
  • Oligosaccharides
  • Polysaccharides
  • Protozoan Proteins
  • mannobiose
  • beta-Mannosidase