α-l-Arabinofuranosidases from Aspergillus terreus with Potential Application in Enology:  Induction, Purification, and Characterization

In the presence of l-arabitol as sole carbon source, Aspergillus terreus CECT 2663 produces three α-l-arabinofuranosidases (ABFs) named ABF1, ABF2, and ABF3, with molecular masses of 90 000, 82 000, and 78 500 Da, respectively. The synthesis of these enzymes is under carbon catabolite repression. We...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1997-07, Vol.45 (7), p.2379-2383
Main Authors: Le Clinche, Florence, Piñaga, Francisco, Ramón, Daniel, Vallés, Salvador
Format: Article
Language:English
Subjects:
ASPERGILLUS TERREUS
Biological and medical sciences
ENOLOGIA
ENZIMAS
ENZYME
ENZYMES
Food industries
Food microbiology
Fundamental and applied biological sciences. Psychology
OENOLOGIE
OENOLOGY
PURIFICACION
PURIFICATION
VINIFICACION
VINIFICATION
WINEMAKING
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Summary:In the presence of l-arabitol as sole carbon source, Aspergillus terreus CECT 2663 produces three α-l-arabinofuranosidases (ABFs) named ABF1, ABF2, and ABF3, with molecular masses of 90 000, 82 000, and 78 500 Da, respectively. The synthesis of these enzymes is under carbon catabolite repression. Western blotting revealed that ABF2 is immunologically related to the α-l-arabinofuranosidase B previously isolated from Aspergillus niger. The three A. terreus proteins have been purified to homogeneity. They are acidic proteins with optimal pHs of 5.0 for ABF1 and ABF2 and 5.5 for ABF3 and optimal temperatures of 50, 60, and 65 °C, respectively. Kinetic constants for the purified enzymes on p-nitrophenyl α-l-arabinofuranoside (pNPA) as substrate have been determined. The three enzymes maintain elevated activities in the presence of ethanol or glucose at those concentrations normally present in must or wine. Keywords: Aspergillus terreus; α-l-arabinofuranosidase; l-arabitol; enzyme purification; wine aroma
ISSN:0021-8561
1520-5118
DOI:10.1021/jf970046k