Abstract
The substrate specificity was studied for the metabolic degradation of N-acetyl-D-glucosamine (GlcNAc) derivatives by Rhodococcus rhodochrous IFO 15564 which possesses N-acetyl-D-glucosamine deacetylase as a key-step enzyme. This microorganism degraded a wide range of substrates with modified N-acyl groups. The metabolizing activity of this strain became low to the substrates substituted at 1,3,4,6-positions of GlcNAc, and GlcNAc itself was suggested to be metabolized via an open-chain aldehyde form. Based on these results, a simplified procedure for the isolation of allyl α-N-acetyl-D-glucosaminide from an α, β-anomeric mixture was developed by selectively hydrolyzing the β-anomer with Jackbean β-N-acetyl-D-glucosaminidase and subsequently degrading the resulting N-acetyl-D-glucosamine in the reaction mixture with this microorganism.
Original language | English |
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Pages (from-to) | 1581-1585 |
Number of pages | 5 |
Journal | Bioscience, Biotechnology and Biochemistry |
Volume | 62 |
Issue number | 8 |
DOIs | |
Publication status | Published - 1998 |
Keywords
- Allyl α-N-acetyl-D-glucosaminide
- N-acetyl-D-glucosamine
- N-acetyl-D-glucosamine deacetylase
- Rhodococcus rhodochrous IFO 15564
- β-N-acetyl-D-glucosaminidase
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry