Baseline levels of integrated biomarker response index (IBR) in Mytilus galloprovincialis (Lamarck, 1819) of BouIsmail bay for monitoring Algerian Bays (Mediterranean Sea).

The Multiple Linear Regression (MLR) technique was used to determine the relationship between the integrated biomarker response index (IBR) with the most important confounding factors (Temperature, pH, Salinity and Dissolved oxygen), in order to define: (1) the baseline assessment criteria (BAC), (2) the environmental assessment criteria (EAC) and (3) the BouIsmail Bay (BIB) -Taxonomy by using Mytilus galloprovincialis sampled from two references sites in BIB (W. Tipaza, Algeria) during one season. Therefore, our results show that, the temperature appeared as a major factor for the explanation of the model.

Modeling integrated biomarker response (IBR) index for the mussel Mytilus galloprovincialis (Lamark 1819) exposed to heavy metal mixture using the CCF design.

Marine pollutants such as heavy metals (HMs) are considered among the most copious oxidative stress (OS) inducers in marine organisms which leads to reactive oxygen species (ROS) formation. Complementary to our previous bioassays studies, the present research focuses on Catalase (CAT), Glutathione S-transferase (GST) and Malondialdehyde (MDA) as oxidative stress biomarkers and the integrated biomarker response (IBR) indexes (IBR and IBR) as an ecotoxicological assessment tool in Mytilus galloprovincialis using central composite face centered (CCF) design. The oxidative stress biomarkers were measured in adult mussels (45-55 mm) on 3 days-exposed under different sub-lethal concentrations of cadmium (Cd), zinc (Zn), and copper (Cu).

Extraction and characterization of chitin, chitosan, and protein hydrolysate from the invasive Pacific blue crab, Portunus segnis (Forskål, 1775) having potential biological activities.

The diversity of marine biomasses is a set of exploitable and renewable resources with application in several sectors. In this context, a co-culture based on three protease-producing bacterial isolates, namely Aeribacillus pallidus VP3, Lysinibacillus fusiformis C250R, and Anoxybacillus kamchatkensis M1V strains, was carried out in a medium based on the blue swimming crab Portunus segnis bio-waste. Proteases production was optimized using a central composite design (CCD).

Physical and enzymatic properties of a new manganese peroxidase from the white-rot fungus Trametes pubescens strain i8 for lignin biodegradation and textile-dyes biodecolorization.

A new manganese peroxidase-producing white-rot basidiomycete fungus was isolated from symptomatic wood of the camphor trees Cinnamomum camphora (L.) at the Hamma Botanical Garden (Algeria) and identified as Trametes pubescens strain i8. The enzyme was purified (MnP TP55) to apparent electrophoretic homogeneity and biochemically characterized.

Purification and biochemical characterization of two keratinases from Bacillus amyloliquefaciens S13 isolated from marine brown alga Zonaria tournefortii with potential keratin-biodegradation and hide-unhairing activities.

The current paper reports the purification and biochemical characterization of two extracellular keratinolytic enzymes, with moderate elastolytic activity, from Bacillus amyloliquefaciens strain S13 newly isolated from the brown alga Zonaria tournefortii. The enzymes were purified to homogeneity by precipitation with (NH)SO-dialysis, followed by size exclusion HPLC column, and submitted to biochemical characterization assays. The findings revealed that the pure enzymes designated KERZT-A and B were monomers with molecular masses of 28 and 47 kDa, respectively.

Electrochemical disinfection of bacterial contamination: Effectiveness and modeling study of E. coli inactivation by electro-Fenton, electro-peroxi-coagulation and electrocoagulation.

The present work undertakes an examination and comparison of electro-Fenton (EF), electro-peroxi-coagulation (EPC) and electrocoagulation (EC) applied to the E. coli inactivation in batch reactor. Indeed, platinum (Pt (anode), EF), stainless steel (SS (cathode), EF, EPC) and ordinary steel (Fe (anode), EPC) and aluminum (Al, EC) were used respectively.

Purification, biochemical, and molecular characterization of novel protease from Bacillus licheniformis strain K7A.

A novel extracellular alkaline protease, called SAPHM, from Bacillus licheniformis strain K7A was purified by four steps procedure involving heat treatment (30 min at 70 °C) followed by ammonium sulfate precipitation (40-70%)-dialysis, UNO Q-12 FPLC, and ZORBAX PSM 300 HPLC, and submitted to biochemical characterization assays. The purified enzyme is a monomer of molecular mass of 30,325.12 Da.

A non-toxic microbial surfactant from Marinobacter hydrocarbonoclasticus SdK644 for crude oil solubilization enhancement.

This study aims to investigate the ability of a biosurfactant produced by Marinobacter hydrocarbonoclasticus strain SdK644 isolated from hydrocarbon contaminated sediment to enhance the solubilization rate of crude oil contaminated seawater. Phylogenetic analysis shows that strain SdK644 was very closely related to M. hydrocarbonoclasticus with 16S rRNA gene sequence similarity of 97.

Biochemical and molecular characterization of a novel metalloprotease from Pseudomonas fluorescens strain TBS09.

A novel extracellular protease called MPDZ was purified and characterized from Pseudomonas fluorescens strain TBS09. The enzymatic properties of MPDZ were investigated using biochemical and biophysical methods. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that it was a monomer with a molecular mass of 50013.

Purification and characterization of two novel peroxidases from the dye-decolorizing fungus Bjerkandera adusta strain CX-9.

Two extracellular peroxidases from Bjerkandera adusta strain CX-9, namely a lignin peroxidase (called LiP BA45) and manganese peroxidase (called MnP BA30), were purified simultaneously by applying successively, ammonium sulfate precipitation-dialysis, Mono-S Sepharose anion-exchange and Sephacryl S-200 gel filtration and biochemically characterized. The sequence of their NH-terminal amino acid residues showed high homology with those of fungi peroxidases. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzymes MnP BA30 and LiP BA45 were a monomers with a molecular masses 30125.

Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50.

A new extracellular thermostable keratinolytic protease, designated KERDZ, was purified and characterized from a thermophilic actinomycetes Actinomadura viridilutea DZ50 isolated from Algerian fishing port. The isolate exhibited high keratinase production when grown in chicken-feather meal media (18,000U/ml) after 96-h of incubation at 45°C. The enzyme was purified by ammonium sulfate precipitation (35-55%)-dialysis and heat treatment (30min at 75°C) followed by UNO S-1 FPLC cation exchange chromatography and size exclusion HPLC column.

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101.

A protease-producing fungus was isolated from an alkaline wastewater of chemical industries and identified as Trametes cingulata strain CTM10101 on the basis of the ITS rDNA gene-sequencing. It was observed that the fungus strongly produce extracellular protease grown at 30°C in potato-dextrose-broth (PDB) optimized media (13500U/ml). The pure serine protease isolated by Trametes cingulata (designated SPTC) was purified by ammonium sulfate precipitation-dialysis followed by heat-treatment and UNO S-1 FPLC cation-exchange chromatography.

Preliminary characterization of biosurfactant produced by a PAH-degrading Paenibacillus sp. under thermophilic conditions.

The capacities of a biosurfactant producing and polycyclic aromatic hydrocarbon (PAH) utilizing bacterium, namely, strain 1C, isolated from an Algerian contaminated soil, were investigated. Strain 1C belonged to the Paenibacillus genus and was closely related to the specie Paenibacillus popilliae, with 16S rRNA gene sequence similarity of 98.4 %.

A novel keratinase from Bacillus tequilensis strain Q7 with promising potential for the leather bating process.

The present paper reports on the purification and characterization of an extracellular keratinase (KERQ7) newly purified from Bacillus tequilensis Q7. Pure protein was obtained after ammonium sulfate fractionation (30-60%), followed by Mono S Sepharose cation-exchange chromatography. MALDI-TOF/MS analysis revealed that the purified enzyme was a monomer with a molecular mass of 28,355.

Purification and biochemical characterization of two detergent-stable serine alkaline proteases from Streptomyces sp. strain AH4.

Streptomyces sp. strain AH4 exhibited a high ability to produce two extracellular proteases when cultured on a yeast malt-extract (ISP2)-casein-based medium. Pure proteins were obtained after heat treatment (30 min at 70 °C) and ammonium sulphate fractionation (30-60 %), followed by size exclusion HPLC column.

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

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.

Degradation of direct yellow 9 by electro-Fenton: process study and optimization and, monitoring of treated water toxicity using catalase.

The present study was undertaken to investigate the degradation and removal of direct yellow 9 (DY9) by the electro-Fenton (EF) process in batch reactor using iron and stainless steel electrodes. DY9 removal decreased with the increase in pH (3 to 8) and increased with the increase in current intensity (0.05 to 0.

Biochemical and molecular characterization of a serine keratinase from Brevibacillus brevis US575 with promising keratin-biodegradation and hide-dehairing activities.

Dehairing is one of the highly polluting operations in the leather industry. The conventional lime-sulfide process used for dehairing produces large amounts of sulfide, which poses serious toxicity and disposal problems. This operation also involves hair destruction, a process that leads to increased chemical oxygen demand (COD), biological oxygen demand (BOD), and total suspended solid (TSS) loads in the effluent.

Purification and biochemical characterization of a detergent-stable keratinase from a newly thermophilic actinomycete Actinomadura keratinilytica strain Cpt29 isolated from poultry compost.

An extracellular thermostable keratinase (KERAK-29) was purified and biochemically characterized from a thermophilic actinomycete Actinomadura keratinilytica strain Cpt29 newly isolated from Algerian poultry compost. The isolate exhibited high keratinase production when grown in chicken feather meal media (24,000 U/ml). Based on matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis, the purified enzyme is a monomer with a molecular mass of 29,233.

Purification and characterization of a highly thermostable chitinase from the stomach of the red scorpionfish Scorpaena scrofa with bioinsecticidal activity toward cowpea weevil Callosobruchus maculatus (Coleoptera: Bruchidae).

This present study is the first attempt to report on the purification and characterization of a chitinase from the stomach of the red scorpionfish Scorpaena scrofa. A 50-kDa chitinase (SsChi50) was purified to homogeneity, and matrix assisted laser desorption ionization-time of flight/mass spectrometry (MALDI-TOF/MS) analysis showed that SsChi50 was a monomer with a molecular mass of 50,103 Da. The 25 N-terminal residues of SsChi50 displayed high homology with family-18 chitinases.

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

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.

Characterization of a novel biosurfactant produced by Staphylococcus sp. strain 1E with potential application on hydrocarbon bioremediation.

A biosurfactant-producing bacterium (Staphylococcus sp. strain 1E) was isolated from an Algerian crude oil contaminated soil. Biosurfactant production was tested with different carbon sources using the surface tension measurement and the oil displacement test.

Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents.

A keratinolytic alkaline proteinase (KERAB) was isolated from Streptomyces sp. strain AB1. Based on MALDI-TOF mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 29850.