Purification and Characterization of a Novel Serine Protease from the Fruiting Bodies of a Rare Edible Medicinal Mushroom, Lyophyllum shimeji (Agaricomycetes)
文献类型: 外文期刊
第一作者: Geng, Xueran
作者: Geng, Xueran;Te, Rigen;Wang, Hexiang;Geng, Xueran;Te, Rigen;Wang, Hexiang;Tian, Guoting;Zhao, Yongchang;Zhao, Liyan;Ng, Tzi Bun
作者机构:
关键词: Lyophyllum shimeji;medicinal mushrooms;protease;purification
期刊名称:INTERNATIONAL JOURNAL OF MEDICINAL MUSHROOMS ( 影响因子:1.921; 五年影响因子:1.879 )
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年卷期:
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收录情况: SCI
摘要: 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 degrees 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 K-m and V-max at 50 degrees C and pH 9.0 were 1.32 mg/mL and 454.55 mu g/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.
分类号: Q94
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