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Biochemical characteristics of a novel protease from the basidiomycete Amanita virgineoides

文献类型： 外文期刊

作者： Yuan, Xianghe 1 ; Zhu, Mengjuan 3 ; Tian, Guoting 4 ; Zhao, Yongchang 4 ; Zhao, Liyan 5 ; Ng, Tzi Bun 6 ; Wang, Hexian 1 ;

作者机构： 1.China Agr Univ, State Key Lab Agrobiotechnol, Yuanmingyuan West Rd 2, Beijing 100193, Peoples R China

2.China Agr Univ, Dept Microbiol, Yuanmingyuan West Rd 2, Beijing 100193, Peoples R China

3.Shandong Agr Univ, Dept Fungal Resource, Tai An, Shandong, Peoples R China

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

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

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

关键词： Amanita virgineoides;properties;protease;purification;peptide sequences

期刊名称：BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY （ 影响因子：2.431； 五年影响因子：2.124 ）

ISSN： 0885-4513

年卷期： 2017 年 64 卷 4 期

页码：

收录情况： SCI

摘要： The characterization of a novel protease from Amanita virgineoides is described. The A. virgineoides protease was purified to homogeneity using Q-Sepharose, carboxymethyl-cellulose, diethylaminoethyl-cellulose, and a gel filtration step on Superdex 75. The molecular mass of the purified protease was estimated to be 16.6kDa. The protease was purified 32.1-fold, and its specific activity was 301.4 U/mg. The optimum pH was 4.0, and the optimum temperature was 50 degrees C. Kinetic constants (K-m, V-max) were determined under the optimum reaction conditions, with K-m and V-max, being 3.74mg/mL and 9.98 g mL(-1) Min(-1), respectively. The activity of the protease was curtailed by Cu2+, Pb2+, Fe3+, Cd2+, and Hg2+ ions but enhanced by Mg2+, Ca2+, and K+ ions at low concentrations. The protease activity was adversely affected by ethylene diamine tetraacetic acid, suggesting that it is a metalloprotease. Four peptide sequences were obtained from liquid chromatography-tandem mass spectrometry, including KQALSGIR, TIAMDGTEGLVR, VALTGLTVAEYFR, and AGAGSATLSMAYAGAR, which showed 86%, 64%, 60%, and 75% identity with peptides of Hypsizygus marmoreus, Dacryopinax sp. DJM-731 SS1, Trametes versicolor FP-101664 SS1, and Paxillus involutus ATCC 200175, respectively. The newly isolated protease showed good hydrolytic activity and biochemical characteristics, which expanded the knowledge of biologically active proteins and provided further insight on this poisonous fungus. (C) 2016 International Union of Biochemistry and Molecular Biology, Inc.

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