Oligosaccharide oxidase for the enzymatic synthesis of glucosaminic acids

Background D-Glucosaminic acid is a valuable amino acid useful in food and medical applications. It is a highly sought after enantiopure molecule important in synthesis of drugs and glycopeptides. Current enzymatic synthesis pathways to D-glucosaminic acid carry disadvantages such as low product yield, long reaction times, and high cost due to increase in enzyme usage. Results Herein, the Auxiliary Activity 7 chito-oligosaccharide oxidase from Lentinus brumalis , LbChi7A, was shown as a potent biocatalyst capable of efficiently converting D-glucosamine (GlcN) and N -acetyl-D-glucosamine (GlcNAc) to their respective C ₁ -acids. Due to a unique substrate specificity towards GlcN and GlcNAc, LbChi7A converts at least 90% GlcN to D-glucosaminic acid within 60 min and 100% GlcNAc to N -acetyl-D-glucosaminic acid within the same time frame. Furthermore, LbChi7A inhibition by the hydrogen peroxide co-product was not detected, even at 860 mM. This single enzymatic conversion offers an efficient process for the production of glucosaminic acids including D-glucosaminic acid or N -acetyl-D-glucosaminic acid. Conclusions The biotechnological potential of LbChi7A is demonstrated, particularly in the production of rare sugars and pharmaceutical intermediates. The ability of the enzyme to perform selective oxidation without the need for hazardous chemicals presents a cleaner and efficient alternative to traditional chemical methods.