Enzymatic preparation of an immunostimulant, the disaccharide‐dipeptide, N‐acetyl‐β‐D‐glucosaminyl‐(1→4)‐N‐acetylmuramyl‐L‐alanyl‐D‐isoglutamine, from a bacterial peptidoglycan

Abstract
The disaccharide-dipeptide N-acetyl-.beta.-D-glucosaminyl-(1 .fwdarw. 4)-N-acetylmuramyl-L-alanyl-D-isoglutamine was obtained by an enzymatic degradation of the peptidoglycan of Actinomadura R39. The peptidoglycan was hydrolyzed successively by the 3 following enzymes: lysozyme, DD-carboxypeptidase from Streptomyces albus G and .gamma.-D-glutamyl-meso-diaminopimelate endopeptidase I from Bacillus sphaericus 9602. The by-products of the last reaction were eliminated by successive ion-exchange and gel-permeation chromatographies. Both chemical analysis and mass spectrometry show that the resulting disaccharide-dipeptide is a pure compound.

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