一种来自链霉菌 AH4 的热稳定腐殖酸过氧化物酶：纯化和生化特性。
A thermostable humic acid peroxidase from Streptomyces sp. strain AH4: purification and biochemical characterization.
机构信息
Laboratory of Biochemistry and Industrial Microbiology (LBIM), Department of Industrial Chemistry, Faculty of Engineering Sciences, University of Saad Dahlab of Blida, B.P 270, 09000 Blida, Algeria.
出版信息
Bioresour Technol. 2012 May;111:383-90. doi: 10.1016/j.biortech.2012.01.153. Epub 2012 Feb 6.
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 60,215.18Da. The 26N-terminal residues of HaP3 displayed high homology with Streptomyces peroxidases. Optimal peroxidase activity was obtained at pH 5 and 80°C. HaP3 was stable at pH and temperature ranges of 4-8 and 60-90°C for 72 and 4h, respectively. HaP3 catalyzed the oxidation of 2,4-dichlorophenol, commercial humic acid, guiacol, and 2,6-dichlorophenol (50mM); 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.
从链霉菌属 AH4 菌株中分离到一种细胞外耐热腐殖酸过氧化物酶 (HaP3)。MALDI-TOF MS 分析表明，纯化的酶是一种单体，分子量为 60215.18Da。HaP3 的 26N 端残基与链霉菌过氧化物酶具有高度同源性。HaP3 的最适过氧化物酶活性在 pH 5 和 80°C 下获得。HaP3 在 pH 4-8 和温度 60-90°C 范围内分别稳定 72 和 4h。HaP3 催化 2,4-二氯苯酚、商业腐殖酸、愈创木酚和 2,6-二氯苯酚 (50mM)、L-3,4-二羟基苯丙氨酸 (40mM)、4-氯苯酚、2,4,5-三氯苯酚和 2,4,6-三氯苯酚 (30mM) 在过氧化氢存在下的氧化。叠氮化钠和氰化钾抑制 HaP3，表明存在血红素成分。这些特性使 HaP3 成为未来在饮用水中消除天然腐殖酸的潜在有力候选物。
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