Previous studies have shown isoflavone aglycones to have more biological effects than their counterparts, isoflavone glycones. Some beta-glucosidases can hydrolyze isoflavone glucosides to release aglycones, and discovery of these has attracted great interest. A glycoside hydrolase (GH) family 3 beta-glucosidase (bgl2) gene from Neurospora crassa was heterologously expressed in Pichia pastoris with high purity. The recombinant BGL2 enzyme displayed its highest activity at pH 5.0 and 60 degrees C, and had its maximum activity against p-nitrophenyl-beta-D-glucopyranoside (pNPG) (143.27 +/- 4.79 U/mg), followed by cellobiose (74.99 +/- 0.78 U/mg), gentiobiose (47.55 +/- 0.15 U/mg), p-nitrophenyl-beta-D-cellobioside (pNPC) (40.07 +/- 0.87 U/mg), cellotriose (1231 +/- 0.36 U/mg) and cellotetraose (9.04 +/- 0.14 U/mg). The kinetic parameters of K-m and Vmax were 0.21 +/- 0.01 mM and 147.93 +/- 2.77 mu M/mg/min for pNPG. The purified enzyme showed a heightened ability to convert the major soybean isoflavone glycosides (daidzin, genistin and glycitin) into their corresponding aglycone forms (daidzien, genistein and glycitein). With this activity against soybean isoflavone glycosides, BGL2 shows great potential for applications in the food, animal feed, and pharmaceutical industries. (C) 2015 Elsevier Inc. All rights reserved.