A halotolerant bifunctional ß-xylosidase/α-l-arabinofuranosidase from Colletotrichum graminicola: Purification and biochemical characterization.

A ß-xylosidase from Colletotrichum graminicola (Bxcg) was purified. The enzyme showed high halotolerance, retaining about 63% of the control activity in the presence of 2.5molL-1 NaCl. The presence of NaCl has not affected the optimum reaction temperature (65°C), but the optimum pH was slightly altered (from 4.5 to 5.0) at high salt concentrations. Bxcg was fully stable at 50°C for 24h and over a wide pH range even in the presence of NaCl. In the absence of salt Bxcg hydrolyzed p-nitrophenyl-ß-d-xylopyranoside with maximum velocity of 348.8±11.5Umg-1 and high catalytic efficiency (1432.7±47.3Lmmol-1s-1). Bxcg revealed to be a bifunctional enzyme with both ß-xylosidase and α-l-arabinofuranosidase activities, and hydrolyzed xylooligosaccharides containing up to six pentose residues. The enzyme showed high synergistic effect (3.1-fold) with an endo-xylanase for the hydrolysis of beechwood xylan, either in the absence or presence of 0.5molL-1 NaCl, and was tolerant to different organic solvents and surfactants. This is the first report of a halotolerant bifunctional ß-xylosidase/α-l-arabinofuranosidase from C. graminicola, and the enzyme showed attractive properties for application in lignocellulose hydrolysis, particularly under high salinity and/or in the presence of residues of pretreatment steps.