α-l-Arabinofuranosidase 3 from Penicillium purpurogenum (ABF3): Potential application in the enhancement of wine flavour and heterologous expression of the enzyme

Maria Cristina Ravanal, Lorena Rosa, Jaime Eyzaguirre

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

An α-l-arabinofuranosidase (ABF3) from Penicillium purpurogenum was purified and its possible biotechnological application in the enhancement of wine flavour combined with P. purpurogenum β-glucosidase was studied. A must from Muscat of Alexandria was used to isolate the glycosides. The total monosaccharide (glucose, arabinose and xylose) levels in the glycosides were determined after acid hydrolysis, and were compared with the result of enzymatic hydrolysis. These results were analogous to those obtained in similar experiments using a commercial preparation, thus suggesting that the enzyme from P. purpurogenum may prove useful in this particular application. This prompted us to express the enzyme heterologously. The abf3 gene was thus expressed in Pichia pastoris. The recombinant enzyme was purified and it shows the same properties of the native ABF3 (substrate specificity, kinetic constants, pH and temperature optima and antibody cross-reactivity).

Original languageEnglish
Pages (from-to)888-893
Number of pages6
JournalFood Chemistry
Volume134
Issue number2
DOIs
Publication statusPublished - 15 Sep 2012

Keywords

  • Arabinofuranosidase
  • Heterologous expression
  • Penicillium purpurogenum
  • Pichia pastoris
  • Wine aroma enhancement
  • β-Glucosidase

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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