期刊
BIORESOURCE TECHNOLOGY
卷 111, 期 -, 页码 383-390出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2012.01.153
关键词
HaP; Peroxidase; Streptomyces; Soil humic acids; Purification
资金
- Algerian Ministry of Higher Education and Scientific Research (CNEPRU) [JO100420070004]
An extracellular thermostable humic acid peroxidase (HaP3) was isolated from a Streptomyces sp. strain AH4. MALDI-TOF MS analysis showed that the purified enzyme was a monomer with a molecular mass of 60,215.18 Da. The 26 N-terminal residues of HaP3 displayed high homology with Streptomyces peroxidases. Optimal peroxidase activity was obtained at pH 5 and 80 degrees C. HaP3 was stable at pH and temperature ranges of 4-8 and 60-90 degrees C for 72 and 4 h, respectively. HaP3 catalyzed the oxidation of 2,4-dichlorophenol, commercial humic acid, guiacol, and 2,6-dichlorophenol (50 mM); L-3,4-dihydroxyphenylalanine (40 mM); 4-chlorophenol, 2,4,5-trichlorophenol, and 2,4,6-trichlorophenol (30 mM) in the presence of hydrogen peroxide. Sodium azide and potassium cyanide inhibited HaP3, which indicated the presence of heme components. These properties make HaP3 a potential strong candidate for future application in the elimination of natural humic acids in drinking water. (C) 2012 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据