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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

作者： Geng, Xueran 1 ; Te, Rigen 1 ; Tian, Guoting 3 ; Zhao, Yongchang 3 ; Zhao, Liyan 4 ; Wang, Hexiang 1 ; Ng, Tzi Bun 5 ;

作者机构： 1.China Agr Univ, State Key Lab Agrobiotechnol, Beijing, Peoples R China

2.China Agr Univ, Dept Microbiol, Beijing, Peoples R China

3.Yunnan Acad Agr Sci, Inst Biotechnol & Germplasm Resource, Kunming, Peoples R China

4.Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing, Jiangsu, Peoples R China

5.Chinese Univ Hong Kong, Fac Med, Sch Biomed Sci, Shatin, Hong Kong, Peoples R China

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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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.

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