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Reaction mechanism of β-apiosidase from Aspergillus aculeatus
Vladimír Mastihuba1, Elena Karnišová Potocká1, Iveta Uhliariková1
1Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-845 38 Bratislava, Slovakia.
Abstract:
Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from Aspergillus aculeatus in commercial glycanase Viscozyme L was studied by 1H NMR technique. Study of hydrolysis of 4-nitrophenyl β-D-apiofuranoside revealed that this reaction proceeds with inversion of hydroxyl group in the anomeric center, which confirms inverting mechanism of the enzyme and its inability to catalyze transapiosylation in syntheses of apiosides.
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