The aim of this study was to evaluate
the potential application
of cell-surface-displayed β-glucosidase (BGL) in wine aroma
enhancement. Gene cassettes for the surface display of Aspergillus
niger BGL were constructed using different promoters (GPD and SED1) and glycosylphosphatidylinositol
(GPI) anchoring regions (Sag1, Sed1, and Cwp2). The differences in
surface-display cassettes, the tolerance of the displayed BGL to typical
winemaking conditions, and the hydrolysis capacity for the liberation
of grape aroma glycosides were analyzed. Results revealed that simultaneous
utilization of GPD promoter and Sed1 anchoring domain
achieved the highest BGL activity. The displayed BGL exhibited relatively
high activity at pH 3.0 and at glucose concentration below 2.5% (w/v),
compared to commercial enzyme (AR 2000), but exhibited no significant
difference under varying ethanol concentrations. Furthermore, the
surface-displayed BGL presented better ability to release free terpenols
compared to AR 2000. Therefore, a surface-display system could provide
a new viable solution for enhancing wine aroma.