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Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata

文献类型： 外文期刊

作者： Geng, Xueran 1 ; Te, Rigen 2 ; Tian, Guoting 4 ; Zhao, Yongchang 4 ; Zhao, Liyan 5 ; Wang, Hexiang 2 ; Ng, Tzi Bun 6 ;

作者机构： 1.Shanxi Agr Univ, Coll Food Sci & Engn, Taigu 030801, Shanxi, Peoples R China

2.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China

3.China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China

4.Yunnan Acad Agr Sci, Inst Biotechnol & Germplasm Resource, Kunming 650223, Yunnan, Peoples R China

5.Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Jiangsu, Peoples R China

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

关键词： edible mushroom;Oudemansiella radicata;protease;purification

期刊名称：ACTA BIOCHIMICA POLONICA （ 影响因子：2.149； 五年影响因子：2.175 ）

ISSN： 0001-527X

年卷期： 2017 年 64 卷 3 期

页码：

收录情况： SCI

摘要： In this study, a 39-kDa metalloprotease was purified from a rare edible mushroom with health-promoting activities, Oudemansiella radicata, using a purification protocol which entailed anion exchange chromatography on DEAE-cellulose and Q-Sepharose columns and gel filtration by fast protein liquid chromatography on a Superdex 75 column. Some peptide sequences were obtained by LC-MS/MS analysis and one of the sequences, DAWIQADVNR, manifested 90% identity to Coprinopsis cinerea metalloprotease. The optimal reaction pH and temperature for Oudemansiella radicata protease were pH 7.0 and 50 degrees C, respectively. The protease was purified 79-fold and demonstrated a specific protease activity of 2.42 U/mg. The K-m of the purified protease for the casein substrate was 0.65 mg/mL at pH 7.0 and 50 degrees C. The activity of the protease was inhibited by Cd2+, Hg2+, Cu2+, Pb2+ and Fe3+ ions, but was enhanced by K+, Mn2+ and Fe2+ ions. The marked suppression of the protease activity by EDTA indicates that the protease is a metalloprotease.

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