A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3'-Sialyllactose, 6'-Sialyllactose, and Sialyllacto-N-tetraose-b.

ABSTRACT: Sialidases catalyze the removal of terminal sialic acids from sialylated biomolecules, and their substrate preference is frequently indicated in terms of the glycosidic linkages cleaved (α2-3, α2-6, and α2-8) without mention of the remaining sub-terminal reducing-end saccharide moieties. Many human gut commensal and pathogenic bacteria secrete sialidases to forage for sialic acids, which are then utilized as an energy source or assimilated into membrane/capsular structural components. Infant gut commensals similarly utilize sialylated human milk oligosaccharides containing different glycosidic linkages. Here, we have studied the preference of the bacterial sialidases, BbSia2 from Bifidobacterium bifidum, CpNanI from Clostridium perfringens, and HpNanH from Glaesserella par

SUBMITTER: Lata M 

PROVIDER: S-EPMC11326918 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature