Biotransformation of the lipoglycopeptide antibiotic A40926 by Actinoplanes teichomyceticus cells

Compound A40926, produced by Actinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria and Neisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells of Actinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L-1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished with tert-butoxycarbonyl (tert-BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an endoenzyme whose preliminary characterization is presented. © 1995 Society for Industrial Microbiology.