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.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s12010-017-2585-2DOI Listing

Publication Analysis

Top Keywords

chitin oligosaccharides
8
stenotrophomonas maltophilia
8
whole-cell catalyst
8
glcnac
5
synthesis chitin
4
oligosaccharides dried
4
dried stenotrophomonas
4
maltophilia cells
4
cells transglycosylation
4
transglycosylation reaction-catalyzing
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!