In:
Bioscience, Biotechnology, and Biochemistry, Informa UK Limited, Vol. 84, No. 12 ( 2020-12-01), p. 2499-2507
Abstract:
Di-N-acetylchitobiase (Ctbs) degrades β-1,4 glycoside bonds of the chitobiose core of free asparagine-linked glycan. This study examined whether Ctbs degrades chitin-oligosaccharides to GlcNAc in mammals. We analyzed Ctbs mRNA and protein expression in mouse tissues and characterized enzymatic activity using recombinant mouse Ctbs expressed in Escherichia coli. Ctbs mRNA and protein were expressed in various tissues of mouse, including the stomach. Optimal conditions for recombinant Ctbs were pH 3.0 and 45°C, and the recombinant enzyme was retained more than 94% activity after incubation at pH 3.0–7.0 and below 37°C. The recombinant Ctbs hydrolyzed (GlcNAc)3 and (GlcNAc)6 at pH 3.0 and produced GlcNAc. The Km of Ctbs was lowest with (GlcNAc)3 as a substrate. kcat/Km was fourfold as high with (GlcNAc)3 and (GlcNAc)4 as substrates than with (GlcNAc)2. These results suggest that Ctbs digests chitin-oligosaccharides or (GlcNAc)2 of reducing-end residues of oligosaccharides and produces GlcNAc in mouse tissues.
Type of Medium:
Online Resource
ISSN:
1347-6947
,
0916-8451
DOI:
10.1080/09168451.2020.1805584
Language:
English
Publisher:
Informa UK Limited
Publication Date:
2020
detail.hit.zdb_id:
2110940-0
detail.hit.zdb_id:
1106450-X
SSG:
12
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