Isolation and Physicochemical Characterization of Laccase from Ganoderma lucidum-CDBT1 Isolated from Its Native Habitat in Nepal
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At present, few organisms are known to and capable of naturally producing laccases and white rot fungi are one such group. In the present study, three fungal species, namely, Ganoderma lucidum-CDBT1, Ganoderma japonicum, and Lentinula edodes, isolated from their native habitat in Nepal were screened for laccase production, and G. lucidum-CDBT1 was found to express highest levels of enzyme (day 10 culture media showed 0.92 IU/mg total protein or 92 IU/mL laccase activity with ABTS as substrate). Lignin extracted from rice straw was used in Olga medium for laccase production and isolation from G. lucidum-CDBT1. Presence of lignin (5 g/L) and copper sulfate (30 𝜇M) in the media increased the extracellular laccase content by 111% and 114%, respectively. The laccase enzyme produced by G. lucidum-CDBT1 was fractionated by ammonium sulfate and purified by DEAE Sepharose anion exchange chromatography. The purified enzyme was found to have a molecular mass of 43 kDa and exhibits optimal activity at pH 5.0 and 30∘ C. The isolated laccase was thermally stable for up to 70∘ C for 1 h and exhibited broad pH stability. The kinetic constants, 𝐾𝑚, 𝑉max, and 𝐾cat, determined using 2,2 -azinobis-(-3-ethylbenzothiazoline-6-sulfonic acid) as substrate were found to be 110 𝜇M, 36 𝜇mol/min/mg, and 246 min−1, respectively. The isolated thermostable laccase will be used in future experiments for delignification process.
- Chemistry & Earth Sciences [425 items ]
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