Reaction mechanism of β-apiosidase from Aspergillus aculeatus

Reaction mechanism of β-apiosidase from Aspergillus aculeatus

•Reaction mechanism of apiosidase was studied by 1H NMR.•Apiosidase in Viscozyme L is inverting glycosidase.•Viscozyme L does not catalyze transapiosylations. Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Food chemistry 2019-02, Vol.274, p.543-546
Hauptverfasser: Mastihuba, Vladimír, Karnišová Potocká, Elena, Uhliariková, Iveta, Kis, Peter, Kozmon, Stanislav, Mastihubová, Mária
Format: Artikel
Sprache:eng
Schlagworte:
Apiosidase
Aspergillus - enzymology
Fermentation
Glucosidases - metabolism
Glycosides - metabolism
Hydrolysis
Inverting glycosidase
NMR
Reaction mechanism
Viscozyme L
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:•Reaction mechanism of apiosidase was studied by 1H NMR.•Apiosidase in Viscozyme L is inverting glycosidase.•Viscozyme L does not catalyze transapiosylations. 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.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2018.09.003