Hh. Shin et Hs. Choi, PURIFICATION AND CHARACTERIZATION OF CYSTEINE PROTEASE FROM PLEUROTUS-OSTREATUS, Bioscience, biotechnology, and biochemistry, 62(7), 1998, pp. 1416-1418
Cysteine protease activity in mycelial culture increased 7.7-fold afte
r fruit body formation in Pleurotus ostreatus, using the Leu PNA (LPNA
) cleavage assay. The enzyme was purified from fruit bodies and its M-
r was 97,000 by gel filtration and 48,500 by SDS-PAGE, indicating that
it is a dimer. The enzyme was sensitive to iodoacetic acid, p-chlorom
ercuribenzoate, N-ethylmaleimide, and HgCl2. The sequence of the first
9 N-terminal amino acids of cysteine protease was ASGLXXAIL.