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

• Published in: World journal of microbiology & biotechnology Vol. 16; no. 8-9; pp. 799 - 803
• Main Authors: NAZARENO SAPARRAT, Mario Carlos, MARTINEZ, Maria Jesus, TOURNIER, Horacio Alfio, CABELLO, Marta Noemi, ARAMBARRI, Angélica Margarita
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01.09.2000; Springer Nature B.V
• Subjects: Biological and medical sciences; Biotechnology; Enzyme engineering; Enzymes; Fermentation; Fundamental and applied biological sciences. Psychology; Fusarium solani; Methods. Procedures. Technologies; Microbiology; Production of selected enzymes; Culture medium; Enzyme; Carbon; Ligninolytic enzyme; Strain; Fungi; Enzymatic activity; Nutrient source; Concentration effect; Production; Microorganism culture; Fusarium solani; Fungi Imperfecti; Thallophyta
• ISSN: 0959-3993; 1573-0972
• DOI: 10.1023/A:1008923804859

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^sup -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^sup -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.[PUBLICATION ABSTRACT]