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Molecules 2016, 21(11), 1485; doi:10.3390/molecules21111485

Aroma Release in Wine Using Co-Immobilized Enzyme Aggregates

1
School of Biochemical Engineering, Pontificia Universidad Católica de Valparaíso, Valparaíso 2362803, Chile
2
Technological Center for Grapevine and Wine, Faculty of Agricultural Sciences, Universidad de Talca, Talca 824000, Chile
*
Author to whom correspondence should be addressed.
Academic Editor: Roberto Fernandez-Lafuente
Received: 31 August 2016 / Revised: 18 October 2016 / Accepted: 19 October 2016 / Published: 8 November 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
View Full-Text   |   Download PDF [1464 KB, uploaded 8 November 2016]   |  

Abstract

Aroma is a remarkable factor of quality and consumer preference in wine, representing a distinctive feature of the product. Most aromatic compounds in varietals are in the form of glycosidic precursors, which are constituted by a volatile aglycone moiety linked to a glucose residue by an O-glycosidic bond; glucose is often linked to another sugar (arabinose, rhamnose or apiose). The use of soluble β-glycosidases for aroma liberation implies the addition of a precipitating agent to remove it from the product and precludes its reuse after one batch. An attractive option from a technological perspective that will aid in removing such constraints is the use of immobilized glycosidases. Immobilization by aggregation and crosslinking is a simple strategy producing enzyme catalysts of very high specific activity, being an attractive option to conventional immobilization to solid inert supports. The purpose of this work was the evaluation of co-immobilized β-glycosidases crosslinked aggregates produced from the commercial preparation AR2000, which contains the enzymes involved in the release of aromatic terpenes in Muscat wine (α-l-arabinofuranosidase and β-d-glucopyranosidase). To do so, experiments were conducted with co-immobilized crosslinked enzyme aggregates (combi-CLEAs), and with the soluble enzymes, using an experiment without enzyme addition as control. Stability of the enzymes at the conditions of winemaking was assessed and the volatiles composition of wine was determined by SPE-GC-MS. Stability of enzymes in combi-CLEAs was much higher than in soluble form, 80% of the initial activity remaining after 60 days in contact with the wine; at the same conditions, the soluble enzymes had lost 80% of their initial activities after 20 days. Such higher stabilities will allow prolonged use of the enzyme catalyst reducing its impact in the cost of winemaking. Wine treated with combi-CLEAs was the one exhibiting the highest concentration of total terpenes (18% higher than the control) and the highest concentrations of linalool (20% higher), nerol (20% higher) and geraniol (100% higher), which are the most important terpenes in determining Muscat typicity. Co-immobilized enzymes were highly stable at winemaking conditions, so their reutilization is possible and technologically attractive by reducing the impact of enzyme cost on winemaking cost. View Full-Text
Keywords: glycosidases; wine; aroma; combi-CLEAs glycosidases; wine; aroma; combi-CLEAs
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MDPI and ACS Style

Ahumada, K.; Martínez-Gil, A.; Moreno-Simunovic, Y.; Illanes, A.; Wilson, L. Aroma Release in Wine Using Co-Immobilized Enzyme Aggregates. Molecules 2016, 21, 1485.

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