Applied Microbiology and Biotechnology

, Volume 72, Issue 3, pp 508–513

A laccase from the medicinal mushroom Ganoderma lucidum

Biotechnologically Relevant Enzymes and Proteins

DOI: 10.1007/s00253-006-0314-9

Cite this article as:
Wang, H.X. & Ng, T.B. Appl Microbiol Biotechnol (2006) 72: 508. 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.

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  1. 1.State Key Laboratory for Agrobiotechnology and Department of MicrobiologyChina Agricultural UniversityBeijingChina
  2. 2.Ministry of AgricultureBeijingChina
  3. 3.Department of Biochemistry, Faculty of MedicineThe Chinese University of Hong KongShatinChina

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