Purification and characterization of manganese peroxidase produced by Fusarium equisetti
Microbial ligninolytic enzymes including laccase, manganese peroxidase, and lignin peroxidase are increasingly valued across diverse industries, with manganese peroxidase standing out as a principal component of the microbial lignin‑degrading arsenal. This study was aimed at isolating managanese producing fungi from environmental samples. The fungi was revealed as Fusarium equisetum, and was used for the production of managanese peroxidase using Sawdust as substrate. The enzyme was purified and characterized. Specific activity in the pooled fraction equals 148.4 µmol min⁻¹ ml⁻¹. The 23.3-fold increase was also comparable. ). The enzyme retained more than 80 % of its initial activity across the 30 °C – 50 °C when held for two hours. The residual activity slowly declined with longer incubation hours. The Fusarium equisetum managanese peroxidase was an acidophilic one retaining one-third of its activity at pH 3.0. The enzyme was relatively stable in the presence of metal ions Magnesium, aluminium, copper, and mercury salts. This manganese peroxidase showed relative potential for further biotechnological uses.
Key words: Manganese peroxidase, Fusarium, purification
