Phytochemical Profile and Antibacterial Activity of Retama raetam and R. sphaerocarpa cladodes from Algeria

Retama raetam (RR) and R. sphaerocarpa (RS) are shrubs growing in Algeria desert areas, where are commonly used as healing remedies because of their antiseptic, antipyretic and anti-diarrheal properties. Phytochemical studies have shown that these species are very rich in flavonoids (isoflavones) and alkaloids (quinolizidine and bipiperidyl). The aim of this study was to compare the chemical composition of both Retama species by GC/MS and LC/MS and to determinate their antimicrobial activity of two Retama species growing naturally in Algeria. Ten alkaloids and seven flavonoids were identified in cladodes of RR and RS. The quantitative analysis showed that the most abundant flavonoid of both the aqueous extract from RR and RS was the isoflavone genistein (610.0±2.8 and 408.0±14.1 mg/100 g respectively), whereas sparteine was the predominant alkaloid in RR and retamine in RS. The antibacterial activity of Retama extracts against standard strains was performed by minimum inhibitory concentration (MIC), and by the disc diffusion method (expressed by inhibition zone, IZ). Both Retama species showed the best activity against Staphylococcus aureus and methicillin-resistant S. aureus (MRSA), being RS aqueous extract more active than RR aqueous extract, with MIC 125 µg/mL and bactericidal activity against both strains

Inhibition of hyperthermostable xylanases by superbase ionic liquids

The use of enzymes in aqueous solutions of ionic liquids (ILs) could be useful for the enzymatic treatment of lignocellulose. Hydrophilic ILs that dissolve lignocellulose are harmful to enzymes. The toleration limits and enzyme-friendly superbase IL combinations were investigated for the hyperthermophilic Thermopolyspora flexuosa GH10 xylanase (endo-1,4-beta-xylanase EC 3.2.1.8) TfXYN10A and Dictyoglomus thermophilum GH11 xylanase DtXYN11B. TfXYN10A was more tolerant than DtXYN11B to acetate or propionate-based ILs. However, when the anion of the ILs was bigger (guaiacolate), GH11 xylanase showed higher tolerance to ILs. 1-Ethyl-3-methylimidazolium acetate ([EMIM]OAc), followed by 1,1,3,3-tetramethylguanidine acetate ([TMGH]OAc), were the most enzyme-friendly ILs for TfXYN10A and [TMGH](+)-based ILs were tolerated best by DtXYN11B. Double-ring cations and a large size anion were associated with the strongest enzyme inhibition. Competitive inhibition appears to be a general factor in the reduction of enzyme activity. However, with guaiacolate ILs, the denaturation of proteins may also contribute to the reduction in enzyme activity. Molecular docking with IL cations and anions indicated that the binding mode and shape of the active site affect competitive inhibition, and the cobinding of cations and anions to separate active site positions caused the strongest enzyme inhibition.Peer reviewe

Retama species growing in different ecological-climatic areas of northeastern Algeria have a narrow range of rhizobia that form a novel phylogenetic clade within the Bradyrhizobium genus

International audienceSixty-seven isolates were isolated from nodules collected on roots of Mediterranean shrubby legumes Retama raetam and Retama sphaerocarpa growing in seven ecological-climatic areas of northeastern Algeria. Genetic diversity of the Retama isolates was analyzed based on genotyping by restriction fragment length polymorphism of PCR-amplified fragments of the 16S rRNA gene, the intergenic spacer (IGS) region between the 16S and 23S rRNA genes (IGS), and the symbiotic genes nifH and nodC. Eleven haplotypes assigned to the Bradyrhizobium genus were identified. Significant biogeographical differentiation of the rhizobial populations was found, but one haplotype was predominant and conserved across the sites. All isolates were able to cross-nodulate the two Retama species. Accordingly, no significant genetic differentiation of the rhizobial populations was found in relation to the host species of origin. Sequence analysis of the 16S rRNA gene grouped the isolates with Bradyrhizobium elkanii, but sequence analyses of IGS, the housekeeping genes (dnaK, glnII, recA), nifH, and nodC yielded convergent results showing that the Retama nodule isolates from the northeast of Algeria formed a single evolutionary lineage, which was well differentiated from the currently named species or well-delineated unnamed genospecies of bradyrhizobia. Therefore, this study showed that the Retama species native to northeastern Algeria were associated with a specific clade of bradyrhizobia. The Retama isolates formed three sub-groups based on IGS and housekeeping gene phylogenies, which might form three sister species within a novel bradyrhizobial clad

Use of dansyl N-acetyl glucosamine as substrate for chitin synthetase activities

International audienc

Optimization and partial characterization of endoglucanase produced by Streptomyces SP B-PNG23

Streptomyces sp. B-PNG23 was selected as a promising cellulolytic strain and tested for its ability to produce cellulases from agroindustrial residues. A pH value of 7 and temperature of 28 C were found to be optimal for maximum enzyme production. The highest endoglucanase activity was obtained in a medium comprised of wheat bran (2 g/l), yeast extract (2 g/l), NaCl (2 g/l), NH4Cl (2.5 g/l), and (0.4 g/l) of MgSO4. The enzyme was active at a broad range of pH (5-8) and temperatures (40-70 degrees C). The optimum pH and temperature were 6 and 50 degrees C, respectively. In the presence of metal ions Mn2+, Cu2+ and NH4+ the activity of the enzyme increased significantly. The enzyme retained 50% of its activity after heating at 50 degrees C for 6 h. This enzyme could be considered as a thermotolerant biocatalyst that could be utilized in biotechnological applications

Optimization and partial characterization of endoglucanase produced by Streptomyces sp. B-PNG23

Streptomyces sp. B-PNG23 was selected as a promising cellulolytic strain and tested for its ability to produce cellulases from agroindustrial residues. A pH value of 7 and temperature of 28°C were found to be optimal for maximum enzyme production. The highest endoglucanase activity was obtained in a medium comprised of wheat bran (2 g/l), yeast extract (2 g/l), NaCl (2 g/l), NH4Cl (2.5 g/l), and (0.4 g/l) of MgSO4. The enzyme was active at a broad range of pH (5-8) and temperatures (40-70°C). The optimum pH and temperature were 6 and 50°C, respectively. In the presence of metal ions Mn2+, Cu2+ and NH4 + the activity of the enzyme increased significantly. The enzyme retained 50% of its activity after heating at 50°C for 6 h. This enzyme could be considered as a thermotolerant biocatalyst that could be utilized in biotechnological applications

Optimization of β-1,4-endoxylanase production by an Aspergillus niger strain growing on wheat straw and application in xylooligosaccharides production

20 p.-6 fig.-6 tab.Plant biomass constitutes the main source of renewable carbon on the planet. Its valorization has traditionally been focused on the use of cellulose, although hemicellulose is the second most abundant group of polysaccharides on Earth. The main enzymes involved in plant biomass degradation are glycosyl hydrolases, and filamentous fungi are good producers of these enzymes. In this study, a new strain of Aspergillus niger was used for hemicellulase production under solid-state fermentation using wheat straw as single-carbon source. Physicochemical parameters for the production of an endoxylanase were optimized by using a One-Factor-at-a-Time (OFAT) approach and response surface methodology (RSM). Maximum xylanase yield after RSM optimization was increased 3-fold, and 1.41- fold purification was achieved after ultrafiltration and ion-exchange chromatography, with about 6.2% yield. The highest activity of the purified xylanase was observed at 50 °C and pH 6. The enzyme displayed high thermal and pH stability, with more than 90% residual activity between pH 3.0–9.0 and between 30–40 °C, after 24 h of incubation, with half-lives of 30 min at 50 and 60 °C. The enzyme was mostly active against wheat arabinoxylan, and its kinetic parameters were analyzed (Km = 26.06 mg·mL−1 and Vmax = 5.647 U·mg−1). Wheat straw xylan hydrolysis with the purified β-1,4 endoxylanase showed that it was able to release xylooligosaccharides, making it suitable for different applications in food technology.This work has been funded by Projects GLYSUS RTI2018-093683-Β-I00 (MCIU/AEI/FEDER) and RETOPROSOST2 S2018/EMT-4459 (Comunidad de Madrid).Peer reviewe

Biochemical properties of a new thermo- and solvent-stable xylanase recovered using three phase partitioning from the extract of Bacillus oceanisediminis strain SJ3

The present study investigates the production and partial biochemical characterization of an extracellular thermostablexylanase from the Bacillus oceanisediminis strain SJ3 newly recovered from Algerian soil using three phasepartitioning (TPP). The maximum xylanase activity recorded after 2 days of incubation at 37 °C was 20.24 U/ml in thepresence of oat spelt xylan. The results indicated that the enzyme recovered in the middle phase of TPP system usingthe optimum parameters were determined as 50% ammonium sulfate saturation with 1.0:1.5 ratio of crude extract:t-butanol at pH and temperature of 8.0 and 10 °C, respectively. The xylanase was recovered with 3.48 purificationfold and 107% activity recovery. The enzyme was optimally active at pH 7.0 and was stable over a broad pH range of5.0–10. The optimum temperature for xylanase activity was 55 °C and the half-life time at this temperature was of 6 h.At this time point the enzyme retained 50% of its activity after incubation for 2 h at 95 °C. The crude enzyme resist tosodium dodecyl sulfate and β-mercaptoethanol, while all the tested ions do not affect the activity of the enzyme. Therecovered enzyme is, at least, stable in tested organic solvents except in propanol where a reduction of 46.5% wasobserved. Further, the stability of the xylanase was higher in hydrophobic solvents where a maximum stability wasobserved with cyclohexane. These properties make this enzyme to be highly thermostable and may be suggested asa potential candidate for application in some industrial processes. To the best of our knowledge, this is the first reportof xylanase activity and recoverey using three phase partitioning from B. oceanisediminis