RT Journal Article
ID 31e9bb783820dd74
A1 Geng, Xueran
A1 Te, Rigen
A1 Tian, Guoting
A1 Zhao, Yongchang
A1 Zhao, Liyan
A1 Wang, Hexiang
A1 Ng, Tzi Bun
T1 Purification and Characterization of a Novel Serine Protease from the Fruiting Bodies of a Rare Edible Medicinal Mushroom, Lyophyllum shimeji (Agaricomycetes)
JF International Journal of Medicinal Mushrooms
JO IJM
YR 2016
FD 2016-09-01
VO 18
IS 6
SP 547
OP 554
K1 Lyophyllum shimeji
K1 medicinal mushrooms
K1 protease
K1 purification
AB 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.
PB Begell House
LK https://www.dl.begellhouse.com/journals/708ae68d64b17c52,1e217131685b463b,31e9bb783820dd74.html