Production of ligninolytic enzymes by Fusarium solani strains isolated from different substrata

SAPARRAT, M.C.N.; MARTÍNEZ, M.J.; TOURNIER, H.A.; CABELLO, M.N.; ARAMBARRI, A.M.

WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY

SPRINGER

Lugar: Berlin; Año: 2000 vol. 16 p. 799 - 803

0959-3993

A comparative study on the extracellular ligninolytic enzymatic activity of five strains of Fusarium solani in a carbon-limited medium under shaking, revealed a differential production of these enzymes. Aryl alcohol oxidase (AAO) activity was observed only in the supernatant of strain CLPS no. 568 with levels higher than 57 mU ml-1. Free extracellular laccase activity was detected in strains CLPS nos. 493, 568 and 570, strain no. 568 being the one which showed the highest activity (over 8.6 mU ml-1). Free extracellular lignin peroxidase (LiP) activity was not detected in any isolate tested, whereas low levels of manganese-dependent peroxidase (MnP) and manganese-independent peroxidase (MIP) activities were detected in certain isolates used. The AAO activity of F. solani on primary α-alcohols such as veratryl alcohol, is reported for the first time; this enzyme activity is hydrogen-peroxide independent. This is also the first report for extracellular MnP and MIP activities of F. solani.