A thermostable humic acid peroxidase from Streptomyces sp. strain AH4: Purification and biochemical characterization

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• 作者：Djamila Fodil^a ; ¹ ; Bassem Jaouadi^b ; ¹ ; Abdelmalek Badis^a ; ^{badisabdelmalek@yahoo.fr} ; Zaraî ; Jaouadi Nadia^b ; Fatma Zohra Ferradji^a ; Samir Bejar^b ; Houcine Boutoumi^a
• 关键词：HaP ; Peroxidase ; Streptomyces ; Soil humic acids ; Purification
• 刊名：Bioresource Technology
• 出版年：2012
• 期刊代码：11_09608524
• 类别：ce
• 出版时间：May, 2012
• 卷：111
• 期：Complete
• 页码：383-390
• 文件大小：432 K

摘要

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 掳C. HaP3 was stable at pH and temperature ranges of 4-8 and 60-90 掳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.