laccase from the medicinal mushroom Ganoderma lucidum

• Published in: Applied microbiology and biotechnology Vol. 72; no. 3; pp. 508 - 513
• Main Authors: Wang, H. X, Ng, T. B
• Format: Journal Article
• Language: English
• Published: Berlin Berlin/Heidelberg : Springer-Verlag 01-09-2006; Springer; Springer Nature B.V
• Subjects: Biological and medical sciences; Biotechnology; Cellulose; Chromatography - methods; Fruiting Bodies, Fungal - enzymology; Fundamental and applied biological sciences. Psychology; Ganoderma lucidum; HIV; HIV Reverse Transcriptase - antagonists & inhibitors; Human immunodeficiency virus; Hydrogen-Ion Concentration; Laccase - chemistry; Laccase - genetics; Laccase - isolation & purification; Mushrooms; Reishi - enzymology; Sequence Homology, Amino Acid; Temperature; Fungi; Enzyme; Basidiomycetes; Oxidoreductases; Cultivated mushroom; Ganoderma; Thallophyta; Laccase
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s00253-006-0314-9

A protein demonstrating laccase activity and potent inhibitory activity towards human immunodeficiency virus (HIV)-1 reverse transcriptase (IC₅₀ 1.2 μM) was isolated from fresh fruiting bodies of the medicinal mushroom Ganoderma lucidum. The laccase had a novel N-terminal sequence and a molecular mass of 75 kDa, which is higher than the range (55-56 kDa) reported for most other mushroom laccases. It was isolated by sequential chromatography on DEAE-cellulose and Affi-gel blue gel and adsorption on Con A-Sepharose. Unlike some of the previously isolated laccases, it was adsorbed only on Con A-Sepharose. The enzyme required a pH of 3-5 and a temperature of 70°C to exhibit maximal activity. Minimal activity was detected at pH 6 and 7. Activity was undetectable at pH 8 and 9 and after exposure to 100°C for 10 min.