15961-60-1Relevant articles and documents
Sialic acid and N-acyl sialic acid analog production by fermentation of metabolically and genetically engineered Escherichia coli
Lundgren, Benjamin R.,Boddy, Christopher N.
, p. 1903 - 1909 (2007)
Sialic acid is the terminal sugar found on most glycoproteins and is crucial in determining serum half-life and immunogenicity of glycoproteins. Sialic acid analogs are antiviral therapeutics as well as crucial tools in bacterial pathogenesis research, immunobiology and development of cancer diagnostic imaging. The scarce supply of sialic acid hinders production of these materials. We have developed an efficient, rapid and cost effective fermentation route to access sialic acid. Our approach uses low cost feedstock, produces an industrially relevant amount of sialic acid and is scalable to manufacturing levels. We have also shown that precursor directed biosynthesis can be used to produce a N-acyl sialic acid analog. This work demonstrates the feasibility of engineering manufacturing-friendly bacteria to produce complex, unavailable small molecules. The Royal Society of Chemistry.
Highly efficient and selective biocatalytic production of glucosamine from chitin
Lv,Laborda,Huang,Cai,Wang,Lu,Doherty,Liu,Flitsch,Voglmeir
supporting information, p. 527 - 535 (2017/08/15)
N-Acetyl glucosamine (GlcNAc) is one of the most abundant biomolecules on Earth and is cheaply available from chitin, a major component of crustaceans. The key step in the conversion of GlcNAc to high-value products is the de-N-acetylation to glucosamine, in itself a valuable dietary supplement that is produced at over 29:000 tons scale per annum by chemical hydrolysis, a process that requires harsh reaction conditions and leads to side products requiring separation. Here, we report for the first time the isolation and characterisation of an enzyme, a deacetylase from Cyclobacterium marinum that is able to catalyse the highly selective quantitative hydrolysis of GlcNAc to glucosamine under mild reaction conditions. This enzyme is small (38 kDa), is easily obtainable by heterologous expression in E. coli, has high turnover rates (kcat=61 s-1), tolerates high substrate concentrations (over 100 g L-1) and can be repeatedly re-used as an immobilised catalyst. When coupled with chitinase, the high selectivity of the enzyme for GlcNAc over other biomolecules allowed one-pot extraction of glucosamine from crude solid mushroom fractions containing chitin, thus allowing for alternative production of glucosamine from non-animal sources, of benefit to consumers with crustacean allergies and vegan diets. We suggest that the deacetylase fills an important gap in the sustainable exploitation of GlcNAc and chitin.
A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: Substrate specificity investigations of N-acetylhexosamine 1-kinase
Cai, Li,Guan, Wanyi,Kitaoka, Motomitsu,Shen, Jie,Xia, Chengfeng,Chen, Wenlan,Wang, Peng George
supporting information; experimental part, p. 2944 - 2946 (2009/12/01)
Reports an efficient chemoenzymatic production of an N-acetylhexosamine 1-phophate analogues library by N-acetylhexosamine 1-kinase (NahK) and describes the respective substrate specificity on this enzyme.
