Production of combi-CLEAs of glycosidases utilized for aroma enhancement in wine

Katherine Ahumada, Paulina Urrutia, Andrés Illanes, Lorena Wilson

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Glycosidases are frequently used in winemaking to liberate glycosidically bound aroma compounds. Since most of the glycosidases used for diglycoside hydrolysis act sequentially, their co-immobilization is an attractive alternative from a technical and economical perspective. The enzymes α-l-arabinosidase (ARA) and β-d-glucosidase (βG) from the preparation Rapidase®AR2000 were co-immobilized in CLEAs (combi-CLEAs), evaluating the effect of bovine serum albumin (BSA) addition and the concentration of glutaraldehyde (Glu) on enzyme immobilization yield and expressed activity. Combi-CLEAs prepared with a Glu to Rapidase protein mass ratio of 0.053 and BSA to Rapidase protein mass ratios of 1, 0.33, and 0.2 were selected, evaluating their stability at simulated winemaking conditions: 25 °C, pH 3.5, and 10% (v/v) of ethanol. All combi-CLEAs were more stable than the soluble enzymes, the best result being obtained at a BSA to Rapidase protein mass ratio of 0.33. Half-lives of βG and ARA in combi-CLEAs were 43.9 and 54.9 days, respectively, whereas in the case of the soluble enzymes were only 1.3 and 6.2 days, respectively. Immobilization yields were 79.1 and 47.1% in terms of βG and ARA activity, respectively. Combi-CLEAs of glycosidases are technologically relevant robust biocatalysts for their application as aroma enhancers in winemaking.

Original languageEnglish
Pages (from-to)555-560
Number of pages6
JournalFood and Bioproducts Processing
Volume94
DOIs
StatePublished - 1 Apr 2015
Externally publishedYes

Keywords

  • Aroma
  • Cross-linked enzyme aggregates
  • Glycosidases
  • Immobilization
  • Stabilization
  • Wine

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