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

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

Author information

1
Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan.
2
Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan.
3
Biomass Engineering Program Cooperation Division, RIKEN, Yokohama, Kanagawa 230-0045, Japan.
4
Laboratory of Environmental Molecular Biology, Graduate School of Yokohama City University, Yokohama, Kanagawa 230-0045, Japan; Molecular and Informative Life Science Unit, RIKEN Advanced Science Institute, Yokohama, Kanagawa 230-0045, Japan.
5
Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan. Electronic address: arioka@mail.ecc.u-tokyo.ac.jp.

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

PMID:
25173929
DOI:
10.1016/j.bbrc.2014.08.103
[Indexed for MEDLINE]

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