A laccase from the medicinal mushroom Ganoderma lucidum.
A protein demonstrating laccase activity and potent inhibitory activity towards human immunodeficiency virus (HIV)-1 reverse transcriptase (IC50 1.2 microM) 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 degrees 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 degrees C for 10 min.
Wang
H X
HX
State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing 100094, China.
Ng
T B
TB
D002845:Chromatography / Q000379:methods; D048690:Fruiting Bodies, Fungal / Q000201:enzymology; D054303:HIV Reverse Transcriptase / Q000037:antagonists & inhibitors; D006863:Hydrogen-Ion Concentration; D042845:Laccase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D020940:Reishi / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013696:Temperature
D042845:Laccase; D054303:HIV Reverse Transcriptase