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.
Keywords: Saccharomyces cerevisiae; aroma glycosides; cell-surface display; stabilization; β-glucosidase.