Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 85-86, Issue -, Pages 31-36Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2012.08.001
Keywords
Lepiota ventriosospora; Mycorrhizal fungi; Laccase; Purification; HIV-1 reverse transcriptase inhibitory activity
Funding
- National Grants of China [2010CB732202, 2012BAD14B09]
- Beijing Innovative Grant of Modern Agricultural Technology System
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An isolation procedure that comprised three ion-exchange chromatography steps on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and one gel-filtration step by fast protein liquid chromatography on Superdex 75 was utilized to isolate a laccase with a molecular mass of 65 kDa from fresh fruiting bodies of the mycorrhizal fungus Lepiota ventriosospora. Laccase activity was adsorbed on both DEAE-cellulose and Q-Sepharose but unadsorbed on CM-cellulose. An overall 26.3-fold of purification was obtained. The enzyme demonstrated an optimum temperature at 60 degrees C and an optimum pH 4.0. The purified laccase was quite stable at pH range of 3.6-4.4, but only 17.8% of total activity left after 1 h incubating at 60 degrees C. The ranking of its degradative activity toward aromatic substrates was catechol > hydroquinone > ABTS > 2,6-dimethoxy-phenol. It demonstrated the highest inhibitory activity toward HIV-1 reverse transcriptase with an IC50 value of 0.60 mu M among fungal laccaes reported up to now. (C) 2012 Elsevier B.V. All rights reserved.
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