Fig 1.
Influence of incubation period on laccase production in the basal medium.
The samples were withdrawn after every 24 h and were estimated for laccase activity and fungal growth.
Table 1.
Influence of nitrogen sources on the production of laccase in Aspergillus sp. HB_RZ4.
Table 2.
Summary of purification of laccase of Aspergillus sp. HB_RZ4 by various methods.
Fig 2.
SDS-PAGE analysis for the molecular mass of the protein of Aspergillus sp. HB_RZ4.
Purified fractions of laccase (Lane 2) and standard protein marker (Lane 1) were electrophoresed on SDS-PAGE, followed by staining with Coomassie BrilliantBlue R-250. The molecular mass of purified proteins was estimated by comparing it with the standard protein markers.
Fig 3.
MALDI-TOF mass spectrum of the trypsin digested peptide map of the laccase.
The purified enzyme band obtained in SDS-PAGE was digested by the trypsin and subjected for PMF analysis using the Flex analysis software. The Mascot search in the database and peptide/proteins were compared with the NCBI-nr database.
Fig 4.
Influence of various concentrations of CuSO4 on the laccase activity.
The reaction mixture contained the enzyme, along with CuSO4 (0–50 μM), for 15 min at 34 °C. The enzyme activity was measured with 1.0 mM ABTS, keeping reference enzyme as 100%.
Table 3.
Peptide ions of trypsin digest of laccase of Aspergillus sp.HB_RZ4.
Table 4.
Amino acid content of sequenced peptides of laccase obtained by trypsin digestion.