Characterization of Extracellular β- d -Galactosidase from Fusarium moniliforme Grown in Whey

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Abstract
Extracellular lactase (β-d-galactosidase, EC 3.2.1.23) was prepared as an ethanol precipitate from a culture of Fusarium moniliforme grown on whey. The enzyme functioned optimally at pH 3.8 to 5.0 and at 50 to 60°C on both o-nitrophenyl-β-d-galactopyranoside (ONPG) and lactose. The activation energy of the enzymic hydrolysis of ONPG and lactose in the range of 20 to 55°C was 8,500 and 7,200 cal (ca. 3.57 × 104 and 3.02 × 104 J)/mol, respectively. The Km values were 4.4 and 12.4 mM for ONPG and lactose, respectively. At optimum pH, the enzyme lost half of its activity when it was heated at 50°C for 6 h; at the same pH, the loss was only 5% when the enzyme was heated at 37°C for 6 h. At optimum conditions, 50% of the lactose in whey was hydrolyzed by 10 U of this enzyme in 50 h.