학술논문

The GH26 β-mannanase RsMan26H from a symbiotic protist of the termite Reticulitermes speratus is an endo-processive mannobiohydrolase: Heterologous expression and characterization.
Document Type
Article
Source
Biochemical & Biophysical Research Communications. Sep2014, Vol. 452 Issue 3, p520-525. 6p.
Subject
*PROTISTA
*SYMBIOSIS
*TERMITES
*RETICULITERMES
*HYDROLASES
*LIGNOCELLULOSE
*BIODEGRADATION
Language
ISSN
0006-291X
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. [ABSTRACT FROM AUTHOR]