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30 results on '"Zaraî Jaouadi, Nadia"'

22. A novel peroxidase from white-rot Agaricomycetes fungus Phlebia radiata strain KB-DZ15: Its purification, characterisation, and potential application for dye-decolorisation and lignin-biodegradation.

Author

Bouacem, Khelifa, Allala, Fawzi, Zaraî Jaouadi, Nadia, Hamdi, Sondes, Mechri, Sondes, Ighilahriz, Kahina, Rekik, Hatem, Hacene, Hocine, Bouanane-Darenfed, Amel, and Jaouadi, Bassem

Subjects
TIME-of-flight mass spectrometry, PEROXIDASE, MATRIX-assisted laser desorption-ionization, POTASSIUM cyanide, HORSERADISH peroxidase, MOLECULAR weights
Abstract

A novel extracellular lignin peroxidase (LiP) has been produced (65 U/mL) in potato dextrose broth (PDB)-optimized media by a white-rot Agaricomycetes fungus strain KB-DZ15 newly isolated from dead deciduous trees at Zimoula Forest (Tizi-Ouzou, Algeria). This strain was identified as Phlebia radiata based on internal transcribed spacer (ITS) rDNA gene sequencing. The peroxidase enzyme (called LiP PR40) was purified and characterised. The matrix-assisted laser desorption-ionization – time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that LiP PR40 enzyme was a monomer with a molecular mass of 40,125.31 Da. The 25 N-terminal residue sequence of LiP PR40 showed high similarity with those of fungi LiPs. Interestingly, LiP PR40 presents premium activity at pH 3 and 80 °C with specific activity and Reinheitzahl (RZ) level of 510 U/mg and 2.81, respectively. Furthermore, it was completely inhibited by sodium azide (NaN3) and potassium cyanide (KCN), suggesting the presence of haem components in its tertiary structure. More interestingly, LiP PR40 illustrated more upper catalytic efficiency and dye-decolorisation aptitude than that of commercial well-known horseradish peroxidase (HRP) from roots of Armoracia rustanica and the purified reported LiP BA45 from Bjerkandera adusta strain CX-9. Consequently, these properties make LiP PR40 a potential candidate for destaining synthetic-dyes and lignin-biodegradation. [ABSTRACT FROM AUTHOR]

Published
2022
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23. A novel peroxidase from white-rot Agaricomycetes fungus Phlebia radiata strain KB-DZ15: Its purification, characterisation, and potential application for dye-decolorisation and lignin-biodegradation

Author

Bouacem, Khelifa, primary, Allala, Fawzi, additional, Zaraî Jaouadi, Nadia, additional, Hamdi, Sondes, additional, Mechri, Sondes, additional, Ighilahriz, Kahina, additional, Rekik, Hatem, additional, Hacene, Hocine, additional, Bouanane-Darenfed, Amel, additional, and Jaouadi, Bassem, additional

Published
2021
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27. Biochemical and molecular characterization of a thermo- and detergent-stable alkaline serine keratinolytic protease from Bacillus circulans strain DZ100 for detergent formulations and feather-biodegradation process

Author

Zaraî Jaouadi Nadia, Boulkour Touioui Soraya, Bassem Jaouadi, Belgacem Naili, Hatem Rekik, Samir Bejar, Fatma Zohra Ferradji, Feriel Rebzani, Amina Benkiar, and Abdelmalek Badis

Subjects
Serine protease, chemistry.chemical_classification, Proteases, Protease, Chromatography, Molecular mass, medicine.medical_treatment, Biology, Microbiology, Biomaterials, chemistry.chemical_compound, Enzyme, Biochemistry, chemistry, biology.protein, medicine, Bacillus circulans, PMSF, Waste Management and Disposal, Thermostability
Abstract

An extracellular keratinolytic protease (SAPDZ) was produced and purified from a newly isolated Bacillus circulans strain DZ100. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme is a monomer with a molecular mass of 32019.10 Da. The sequence of the 25 N-terminal residues of SAPDZ showed high homology with those of Bacillus proteases. Optimal activity was achieved at pH 12.5 and 85 °C. This enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP), which suggests that it belongs to the serine protease family. Compared to the other tested proteases, SAPDZ exhibited broader substrate specificity, higher levels of catalytic efficiency, and greater keratinolytic activity, which made it able to accomplish the entire feather-biodegradation process on its own. The sapDZ gene encoding SAPDZ was cloned, sequenced, and expressed in Escherichia coli. The biochemical properties exhibited by the extracellular purified recombinant enzyme (rSAPDZ) were similar to those of the native one. Above all, SAPDZ exhibited marked stability to detergents, making it a potential candidate for future applications in detergent formulations and an efficient eco-friendly enzyme for the biodegradation of feather keratin.

Published
2013
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28. A thermostable humic acid peroxidase from Streptomyces sp. strain AH4: Purification and biochemical characterization

Author

Samir Bejar, Bassem Jaouadi, Djamila Fodil, Houcine Boutoumi, Zaraî Jaouadi Nadia, Fatma Zohra Ferradji, and Abdelmalek Badis

Subjects
Environmental Engineering, Molecular Sequence Data, Potassium cyanide, Bioengineering, Streptomyces, Catalysis, Substrate Specificity, chemistry.chemical_compound, Enzyme Stability, Organic chemistry, Humic acid, Amino Acid Sequence, Enzyme Inhibitors, Hydrogen peroxide, Waste Management and Disposal, Heme, chemistry.chemical_classification, biology, Molecular mass, Renewable Energy, Sustainability and the Environment, Temperature, General Medicine, Hydrogen-Ion Concentration, biology.organism_classification, Molecular Weight, Peroxidases, chemistry, Spectrophotometry, biology.protein, Sodium azide, Electrophoresis, Polyacrylamide Gel, Peroxidase, Nuclear chemistry
Abstract

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.

Published
2012
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29. Characterization of a purified decolorizing detergent-stable peroxidase from Streptomyces griseosporeus SN9

Author

Maher Hmidi, Naim Sallem, Samir Bejar, Abdelmalek Badis, Amina Benkiar, Hatem Rekik, Zaraî Jaouadi Nadia, Wacim Bejar, Mouna Belhoul, Sidali Kourdali, and Bassem Jaouadi

Subjects
Detergents, Potassium cyanide, Biochemistry, Streptomyces, Substrate Specificity, chemistry.chemical_compound, Structural Biology, RNA, Ribosomal, 16S, Streptomyces griseosporeus, Enzyme Stability, Amino Acid Sequence, Molecular Biology, Heme, Phylogeny, Peroxidase, Ions, Chromatography, biology, Molecular mass, Temperature, General Medicine, Lignin peroxidase, Hydrogen Peroxide, Hydrogen-Ion Concentration, biology.organism_classification, Molecular Weight, Kinetics, chemistry, Metals, biology.protein, Sodium azide
Abstract

A novel extracellular lignin peroxidase (called LiP-SN) was produced and purified from a newly isolated Streptomyces griseosporeus strain SN9. The findings revealed that the pure enzyme was a monomeric protein with an estimated molecular mass of 43 kDa and a Reinheitzahl value of 1.63. The 19 N-terminal residue sequence of LiP-SN showed high homology with those of Streptomyces peroxidases. Its optimum pH and temperature were pH 8.5 and 65 °C, respectively. The enzyme was inhibited by sodium azide and potassium cyanide, suggesting the presence of heme components in its tertiary structure. Its catalytic efficiency was higher than that of the peroxidase from Streptomyces albidoflavus strain TN644. Interestingly, LiP-SN showed marked dye-decolorization efficiency and stability toward denaturing, oxidizing, and bleaching agents, and compatibility with EcoVax and Dipex as laundry detergents for 48 h at 40 °C. These properties make LiP-SN a potential candidate for future applications in distaining synthetic dyes and detergent formulations.

Published
2014

30. Probing the Crucial Role of Leu31 and Thr33 of the Bacillus pumilus CBS Alkaline Protease in Substrate Recognition and Enzymatic Depilation of Animal Hide

Author

Zaraî Jaouadi, Nadia, primary, Jaouadi, Bassem, additional, Ben Hlima, Hajer, additional, Rekik, Hatem, additional, Belhoul, Mouna, additional, Hmidi, Maher, additional, Aicha, Houda Slimene Ben, additional, Hila, Chiraz Gorgi, additional, Toumi, Abdessatar, additional, Aghajari, Nushin, additional, and Bejar, Samir, additional

Published
2014
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