Free and Immobilised β-Glucosidases in Oenology: Biotechnological Characterisation and Its Effect on Enhancement of Wine Aroma

Abstract

In grapes, monoterpenes and norisoprenoids are in the form of non-volatile compounds, flavourless glycosides which could enhance the aroma of wines after its hydrolysis using β- glucosidases enzymes. It is known that the use of immobilised enzymes offers advantages such as reusability and easy recuperation. In this study, a commercial β-glucosidase was immobilised by absorption in sodium alginate. Biotechnological characteristics and terpen hydrolysis (hydrolysis aroma precursors) in muscat wines were studied after treatment with both free and immobilised commercial β- glucosidase with two different concentrations. It was revealed that both forms shared an optimal pH (4.5) and a maximum temperature (64°C), even an increment on the activity between 40and 60°C. A similar Km value has been determined while Vmax from the immobilised enzyme was higher than the free (3.35 and 2.52 μmol min–1 mg–1, respectively). Additionally, the immobilised enzyme showed a better hydrolytic activity during 24 h, and its reusability has been proven. Regarding enzymatic hydrolysis in grape must, the best results were observed for the highest concentration of free β-glucosidase although glucose release was also determined for the immobilised enzyme along the days. In contrast, maximum activity was reached by the immobilised β-glucosidase in less time but in no case equalled the free ones. Finally, volatile compound liberation in wines treated with free or immobilised enzymes was analysed using HRGC-MS. Liberation for both enzymes and the greatest concentrations of some volatiles were detected when a double dose of the free β-glucosidase was used. Nevertheless, the wines treated with the immobilised β-glucosidase showed a high concentration of some volatile compounds such as nerol or geraniol.

Encapsulation of Amyloglucosidase in Chitosan-SDS Coacervates as a Means to Control Starch Hydrolysis in Plant-Based Beverages

“…The heightened enzyme collision rate could also lead to undesirable intermolecular interactions and steric hindrance, potentially inhibiting enzymatic activity and reducing reaction rate [43]. These findings align with previous literature that also observed a reduction in V max and an increase in K M after entrapping different types of enzymes, which might be caused by substrate mass transfer resistance and increased relative concentration of enzymes within the beads [44][45][46][47].…”

Effect of deep eutectic solvents on the biocatalytic properties of β-glucosidase@ZnOFe nano-biocatalyst

“…The exploitation of BGLs on biotechnological processes has been proved an advantageous strategy regarding the production of biofuels, flavour enhancement, edible extracts' clarification, and pharmaceuticals synthesis (Singh et al, 2016). More specifically, by using hydrolytic enzymes as βglycosidases, food industries can improve the organoleptic properties of their products (juice, wine) or enrich them with nutritional aglycones (o-diphenols, coumarins, flavonoids, isoflavones), which mostly demonstrate enhanced bioactivities and aroma (Fernández-Pacheco et al, 2021;Monteiro et al, 2019); Several aglycone derivatives are of high pharmaceutical interest too (Cheng and Zhang, 2017;Ma et al, 2020). BGLs can also catalyze transglycosylation reactions (Ahmed et al, 2017;Xia et al, 2022); Especially immobilized β-glucosidases are ideal candidates for targeted enzymatic glycosylation of natural compounds due to the decreased enzyme inhibition by the substrates (Geronimo et al, 2019).…”

Polymer/Enzyme Composite Materials—Versatile Catalysts with Multiple Applications

“…Fernandez-Pacheco and collaborators immobilized a commercially available β-glucosidase on ALGCa beads in order to improve white wine aroma by the depletion of flavorless glycosides. The immobilized enzyme displays a superior hydrolytic activity, their activity maintained at 96.5% after reutilization for seven times [142].…”