%0 Journal Article %A Geng, Xueran %A Te, Rigen %A Tian, Guoting %A Zhao, Yongchang %A Zhao, Liyan %A Wang, Hexiang %A Ng, Tzi Bun %D 2016 %I Begell House %K Lyophyllum shimeji, medicinal mushrooms, protease, purification %N 6 %P 547-554 %R 10.1615/IntJMedMushrooms.v18.i6.90 %T Purification and Characterization of a Novel Serine Protease from the Fruiting Bodies of a Rare Edible Medicinal Mushroom, Lyophyllum shimeji (Agaricomycetes) %U https://www.dl.begellhouse.com/journals/708ae68d64b17c52,1e217131685b463b,31e9bb783820dd74.html %V 18 %X In this study, a novel protease with a molecular mass of 30 kDa was purified from Lyophyllum shimeji using a purification procedure that involved anion exchange chromatography on a Q-Sepharose column, cation chromatography on an SP-Sepharose column, and gel filtration on a Superdex 75 column. The protease was purified 57-fold, and its specific activity was 6.67 U/mg. Its inner amino acid sequence, determined by liquid chromatography-tandem mass spectrometry, contains AASIIAVLVLSDK, which has 93% identity with the sequence of Hypsizygus marmoreus serine protease. The optimal reaction temperature and pH for L. shimeji protease were 50°C and 10.0, respectively. It is an alkaline protease and has higher activity when the pH lies between 6.8 and 10.0. The Km and Vmax at 50°C and pH 9.0 were 1.32 mg/mL and 454.55 μg/mL/min, respectively. The activity of L. shimeji protease was significantly suppressed by Cd2+, Hg2+, Cu2+, and Fe3+ ions, as well as by phenylmethylsufonyl fluoride; therefore, it is a serine protease. %8 2016-09-01