The purification and characterization of an extracellular lichenase from the fungus Penicillium occitanis Pol6 were studied. The strain produced the maximum level of extracellular lichenase (45 +/- 5 U ml(-1)) when grown in a medium containing oat flour (2%, w/v) at 30 degrees C for 7 days. The purified enzyme EG(L) showed as a single protein band on SDS-PAGE with a molecular mass of 20 kDa. Its N-terminal sequence of 10 amino acid residues was determined as LDNGAPLLNV. The purified enzyme showed an optimum activity at pH 3.0 and 50-60 degrees C. The half-lives of EG(L) at 60 degrees C and 70 degrees C were 80 min and 21 min, respectively. Substrate specificity studies revealed that the enzyme is a true beta-1,3-1,4-D-glucanase. The enzyme hydrolyzed lichenan to yield trisaccharide, and tetrasaccharide as the main products. Under simulated mashing conditions, addition of EG(L) (20 U/ml) or a commercial beta-glucanase (20 U/ml) reduced the filtration time (25% and 21.3%, respectively) and viscosity (10% and 8.18%, respectively). These characteristics indicate that EG(L) is a good candidate in the malting and brewing industry. (C) 2014 Elsevier Ltd. All rights reserved.