Bacterial strain NYT501, which we previously isolated from soil, was identified as Stenotrophomonas maltophilia, and it was confirmed that this strain produces an intracellular β-N-acetylhexosaminidase exhibiting transglycosylation activity. Several properties of this enzyme were characterized using a partially purified enzyme preparation. Using N,N'-diacetylchitobiose (GlcNAc) and N,N',N″-triacetylchitotriose (GlcNAc) as substrates and dried cells of this bacterium as a whole-cell catalyst, chitin oligosaccharides of higher degrees of polymerization were synthesized. (GlcNAc) was generated from (GlcNAc) 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) as a substrate, the yield of higher-degree polymerization oligosaccharides was comparatively low.
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http://dx.doi.org/10.1007/s12010-017-2585-2 | DOI Listing |
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