Abstract
An enzyme preparation from almond emulsin cleaved the peptide-carbohydrate linkage of stem bromelain glycopeptide, Asn-Asn (oligosaccharide)-Glu-Ser-Ser. The resulting products were determined to be an intact peptide, Asn- Asp -Glu-Ser-Ser, and an intact oligosaccharide unit with two moles of N-acetylglucosamine. So far as tested the enzyme hydrolyzed glycopeptides with 3 to 10 amino acids, while both asparagine-oligosaccharide from ovalbumin and Asn-GlcNAc were not. Thus, the enzyme is a new amidase capable of hydrolyzing aspartylglycosylamine linkage in glycopeptides with multiple amino acid residues.
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