Reaction mechanism of β-apiosidase from Aspergillus aculeatus

Vladimír Mastihuba; Elena Karnišová Potocká; Iveta Uhliariková; Peter Kis; Stanislav Kozmon; Mária Mastihubová

doi:10.1016/j.foodchem.2018.09.003

Reaction mechanism of β-apiosidase from Aspergillus aculeatus

Food Chem. 2019 Feb 15:274:543-546. doi: 10.1016/j.foodchem.2018.09.003. Epub 2018 Sep 1.

Authors

Vladimír Mastihuba¹, Elena Karnišová Potocká², Iveta Uhliariková², Peter Kis², Stanislav Kozmon², Mária Mastihubová²

Affiliations

¹ Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-845 38 Bratislava, Slovakia. Electronic address: vladimir.mastihuba@savba.sk.
² Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-845 38 Bratislava, Slovakia.

PMID: 30372976
DOI: 10.1016/j.foodchem.2018.09.003

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.

Keywords: Apiosidase; Inverting glycosidase; NMR; Reaction mechanism; Viscozyme L.

MeSH terms

Aspergillus / enzymology*
Fermentation
Glucosidases / metabolism*
Glycosides / metabolism
Hydrolysis

Substances

Glycosides
Glucosidases
beta-apiosidase