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This study explores the production and characterization of an extracellular β-fructofuranosidase (FFase-I) by Aspergillus versicolor newly isolated from Atlantic Forest-Brazil. The β-fructofuranosidase production by fungus, after the optimization process using central composite design and response surface methodology, showed that 3% (w/v) apple pomace, an initial pH 7.5, and 12 days of cultivation provided the best conditions. The β-fructofuranosidase (FFase-I) was purified from the crude extract by 75% (NH4)2SO4 precipitation followed by DEAE-Sephadex, and the molecular mass of the FFase-I was estimated to be 75 kDa by SDS-PAGE. Furthermore, the enzyme exhibited unusual tolerance to Cu2+, sodium dodecyl sulfate (SDS), Tween 80, ethanol and acetone. The purified enzyme had an optimum pH of 6.0 and was stable over an acidic pH range of 3.0–6.0. The optimum temperature of the FFase-I was 55°C but was stable at 60°C for 7 h. Thus, the β-fructofuranosidase A. versicolor which has thermal stability and activity under acidic conditions would have potential application in sugar cane molasses hydrolysis for subsequent ethanol production.   Key words: Aspergillus, factorial design, fruit wastes, invertase.

-Fructofuranosidase production by Aspergillus versicolor isolated from Atlantic forest and grown on apple pomace