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Appl Biochem Biotechnol ; 184(2): 673-684, 2018 Feb.
Article in English | MEDLINE | ID: mdl-28840460

ABSTRACT

Bacterial strain NYT501, which we previously isolated from soil, was identified as Stenotrophomonas maltophilia, and it was confirmed that this strain produces an intracellular ß-N-acetylhexosaminidase exhibiting transglycosylation activity. Several properties of this enzyme were characterized using a partially purified enzyme preparation. Using N,N'-diacetylchitobiose (GlcNAc)2 and N,N',N″-triacetylchitotriose (GlcNAc)3 as substrates and dried cells of this bacterium as a whole-cell catalyst, chitin oligosaccharides of higher degrees of polymerization were synthesized. (GlcNAc)3 was generated from (GlcNAc)2 as the major transglycosylation product, and a certain amount of purified sample of the trisaccharide was obtained. By contrast, in the case of the reaction using (GlcNAc)3 as a substrate, the yield of higher-degree polymerization oligosaccharides was comparatively low.


Subject(s)
Bacterial Proteins/chemistry , Chitin/chemical synthesis , Oligosaccharides/chemical synthesis , Stenotrophomonas maltophilia/enzymology , beta-N-Acetylhexosaminidases/chemistry , Chitin/chemistry , Oligosaccharides/chemistry
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