Abstract
Lignin peroxidases are considered to be the primary enzyme for oxidative depolymerisation of lignin and are responsible for H2O2-dependent oxidation of both phenolic aromatic substrates and non-phenolic lignin model compounds. The present study was undertaken to study the production of Lignin peroxidase enzyme by Alternaria alternata ANF238 isolated from rotten wood sample using water hyacinth as a lignocellulosic substrate under solid state fermentation. Various production parameters like initial moisture content, various carbon sources, nitrogen sources, inducers and their concentrations were also optimized to further increase the production of this enzyme. Maximum lignin peroxidase yield of 7.6 U/g of dry substrate was obtained with water hyacinth as substrate supplemented with 0.5% mannitol as carbon source, 1% ammonium sulphate as nitrogen source and 3 mM MnSO4 as inducer under optimized conditions. These results indicate that Alternaria alternata ANF238 is a potential candidate for production of lignin peroxidase using solid state fermentation, an enzyme with wide industrial and biotechnological applications. This study also promises effective utilization of water hyacinth as a substrate for lignin peroxidase production. To the best of our knowledge, this is the first report on LiP production by Alternaria alternata.
Highlights
Lignin is a cementing, tough noncarbohydrate polyphenolic structural constituent of cell wall of all the vascular plants, interspersed with the hemicelluloses and keeping cellulose locked within structural confinements of cell wall
On the basis of the morphological characterization, the isolate ANF36 was identified as Alternaria sp. which was further confirmed by molecular characterization
It was identified as Alternaria alternata based on nucleotide homology and phylogenetic analysis (Table 1; Figure 2, 3)
Summary
Tough noncarbohydrate polyphenolic structural constituent of cell wall of all the vascular plants, interspersed with the hemicelluloses and keeping cellulose locked within structural confinements of cell wall. Lignin peroxidases [EC 1.11.1.14, 1, 2-bis(3,4-dimethoxyphenyl) propane-1,3-diol:hydrogen-peroxide oxidoreductase] are relatively nonspecific, have high redox potential and are responsible for H2O2-dependent oxidation of both phenolic aromatic substrates and non-phenolic lignin model compounds [1,5,6]. Out of these enzymes, lignin peroxidase plays a very important role and is considered to be the primary enzyme for oxidative depolymerisation of lignin by its long range electron transfer pathway [7]. LiP was first discovered in Phanerochaete chrysosporium, and various isoforms are known to exist with this microorganism and a number of other white-rot fungi [12, 13]
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