LARGE-SCALE PRODUCTION OF RECOMBINANT ALPHA-1,2-MANNOSYLTRANSFERASE FROM ESCHERICHIA-COLI FOR THE STUDY OF ACCEPTOR SPECIFICITY AND USE OF THE RECOMBINANT WHOLE CELLS IN SYNTHESIS
Gf. Herrmann et al., LARGE-SCALE PRODUCTION OF RECOMBINANT ALPHA-1,2-MANNOSYLTRANSFERASE FROM ESCHERICHIA-COLI FOR THE STUDY OF ACCEPTOR SPECIFICITY AND USE OF THE RECOMBINANT WHOLE CELLS IN SYNTHESIS, Journal of organic chemistry, 59(21), 1994, pp. 6356-6362
We report the first large scale heterologous expression of a recombina
nt yeast alpha-1,2-mannosyltransferase in E. coli. The enzyme was isol
ated from 10-L and 50-L fermentations, purified and used for mannosyla
tion reactions. The specificity of the recombinant enzyme was extensiv
ely studied by using mannose derivatives, oligosaccharides, and analog
s as accepters, and the results show that the enzyme exhibits high act
ivities toward ManOMe and disaccharides connected by an alpha-1,2-mann
osidic linkage. The recombinant E. coli cells were also used as a cata
lyst for glycosylation reaction, and mannosylation of saccharides and
glycopeptides proceeded in moderate to good yields.