Next Article in Journal
Synthesis and In Vitro Anti Leishmania amazonensis Biological Screening of Morita-Baylis-Hillman Adducts Prepared from Eugenol, Thymol and Carvacrol
Next Article in Special Issue
Agarose and Its Derivatives as Supports for Enzyme Immobilization
Previous Article in Journal
Inflammasomes and Natural Ingredients towards New Anti-Inflammatory Agents
Previous Article in Special Issue
Enzyme Engineering for In Situ Immobilization
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessArticle
Molecules 2016, 21(11), 1485;

Aroma Release in Wine Using Co-Immobilized Enzyme Aggregates

School of Biochemical Engineering, Pontificia Universidad Católica de Valparaíso, Valparaíso 2362803, Chile
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)
Full-Text   |   PDF [1464 KB, uploaded 8 November 2016]   |  


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

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Share & Cite This Article

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top