Abstract：
:An extracellular laccase-producing ascomycete was isolated from soil and identified as Paraconiothyrium variabile using rDNA sequence analysis. Typical laccase substrates including 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS), 2,6-dimethoxyphenol (DMP), and guaiacol were oxidized by the purified enzyme (designated as PvL). The molecular mass of PvL was 84 kDa and it showed a pI value of 4.2. The enzyme acted optimally at pH 4.8 and exhibited an optimum temperature of 50 °C. Using ABTS, PvL represented Km and Vmax of 203 μM and 40 μmol min(-1) mg(-1), respectively. After 24 h incubation at pH 4.8 and 4 °C, 80% of the initial activity of PvL remained. The enzyme was inhibited by Fe2+, Hg2+, and Mn2+, but induced by Cu2+. EDTA (10 mM), 1,4-dithiothreitol (DTT) (0.1 mM), and NaN3 (10 mM) were found to completely inhibit PvL. Sixty-eight percent of Malachite green was decolorized by 4 U/mL of PvL after 15 min incubation at 30 °C.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Forootanfar H,Faramarzi MA,Shahverdi AR,Yazdi MTdoi
10.1016/j.biortech.2010.09.043subject
Has Abstractpub_date
2011-01-01 00:00:00pages
1808-14issue
2eissn
0960-8524issn
1873-2976pii
S0960-8524(10)01556-7journal_volume
102pub_type
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