In the presence of
L-arabitol as sole carbon source,
Aspergillus terreus CECT 2663 produces three
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L-arabinofuranosidases (ABFs) named ABF1, ABF2, andABF3, with molecular masses of 90 000,82 000, and 78 500 Da, respectively. The synthesis of theseenzymes is under carbon cataboliterepression. Western blotting revealed that ABF2 is immunologicallyrelated to the
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L-arabinofuranosidase B previously isolated from
Aspergillus niger.The three
A. terreus proteins have beenpurified to homogeneity. They are acidic proteins with optimal pHsof 5.0 for ABF1 and ABF2 and5.5 for ABF3 and optimal temperatures of 50, 60, and 65
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C,respectively. Kinetic constants for thepurified enzymes on
p-nitrophenyl
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L-arabinofuranoside (
pNPA) as substrate havebeen determined.The three enzymes maintain elevated activities in the presence ofethanol or glucose at thoseconcentrations normally present in must or wine.Keywords:
Aspergillus terreus;
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L-arabinofuranosidase;
L-arabitol; enzymepurification; winearoma