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

Abstract

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.

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Saparrat, M.C.N., Martínez, M.J., Tournier, H.A. et al. Production of ligninolytic enzymes by Fusarium solani strains isolated from different substrata. World Journal of Microbiology and Biotechnology 16, 799–803 (2000). https://doi.org/10.1023/A:1008923804859

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  • Aryl-alcohol oxidase
  • extracellular enzymes
  • Fusarium
  • laccase
  • lignin peroxidase
  • manganese-dependent peroxidase
  • manganese-independent peroxidase