Inhibition of Fungi and Gram-Negative Bacteria by Bacteriocin BacTN635 Produced by Lactobacillus plantarum sp. TN635

The aim of this study was to evaluate 54 lactic acid bacteria (LAB) strains isolated from meat, fermented vegetables and dairy products for their capacity to produce antimicrobial activities against several bacteria and fungi. The strain designed TN635 has been selected for advanced studies. The supernatant culture of this strain inhibits the growth of all tested pathogenic including the four Gram-negative bacteria (Salmonella enterica ATCC43972, Pseudomonas aeruginosa ATCC 49189, Hafnia sp. and Serratia sp.) and the pathogenic fungus Candida tropicalis R2 CIP203. Based on the nucleotide sequence of the 16S rRNA gene of the strain TN635 (1,540 pb accession no FN252881) and the phylogenetic analysis, we propose the assignment of our new isolate bacterium as Lactobacillus plantarum sp. TN635 strain. Its antimicrobial compound was determined as a proteinaceous substance, stable to heat and to treatment with surfactants and organic solvents. Highest antimicrobial activity was found between pH 3 and 11 with an optimum at pH = 7. The BacTN635 was purified to homogeneity by a four-step protocol involving ammonium sulfate precipitation, centrifugal microconcentrators with a 10-kDa membrane cutoff, gel filtration Sephadex G-25, and C18 reverse-phase HPLC. SDS-PAGE analysis of the purified BacTN635, revealed a single band with an estimated molecular mass of approximately 4 kDa. The maximum bacteriocin production (5,000 AU/ml) was recorded after a 16-h incubation in Man, Rogosa, and Sharpe (MRS) medium at 30 °C. The mode of action of the partial purified BacTN635 was identified as bactericidal against Listeria ivanovii BUG 496 and as fungistatic against C. tropicalis R2 CIP203

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

Background Proteases are hydrolytic enzymes that catalyze peptide linkage cleavage reactions at the level of proteins and peptides with different degrees of specificity. This group draws the attention of industry. More than one protease in three is a serine protease. Classically, they are active at neutral to alkaline pH. The serine proteases are researched for industrial uses, especially detergents. They are the most commercially available enzyme group in the world market. Overall, fungi produced extracellular proteases, easily separated from mycelium by filtration. Results A new basidiomycete fungus CTM10057, a hyperproducer of a novel protease (10,500U/mL), was identified as Pleurotus sajor-caju (oyster mushroom). The enzyme, called SPPS, was purified to homogeneity by heat-treatment (80 C for 20min) followed by ammonium sulfate precipitation (35-55%)-dialysis, then UNO Q-6 FPLC ion-exchange chromatography and finally HPLC-ZORBAX PSM 300 HPSEC gel filtration chromatography, and submitted to biochemical characterization assays. The molecular mass was estimated to be 65 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Native-PAGE, casein-zymography, and size exclusion by HPLC. A high homology with mushroom proteases was displayed by the first 26 amino-acid residues of the NH2-terminal aminoacid sequence. Phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP) strongly inhibit SPPS, revealing that it is a member of the serine-proteases family. The pH and temperature optima were 9.5 and 70 C, respectively. Interestingly, SPPS possesses the most elevated hydrolysis level and catalytic efficiency in comparison with SPTC, Flavourzyme 500 L, and Thermolysin type X proteases. More remarkably, a high tolerance towards organic solvent tolerance was exhibited by SPPS, together with considerable detergent stability compared to the commercial proteases Thermolysin type X and Flavourzyme 500 L, respectively. Conclusions This proves the excellent proprieties characterizing SPPS, making it a potential candidate for industrial applications especially detergent formulations

Designing an Efficient Surfactant–Polymer–Oil–Electrolyte System: A Multi-Objective Optimization Study

This research aimed to study the effects of individual components on the physicochemical properties of systems composed of surfactants, polymers, oils, and electrolytes in order to maximize the recovery efficiency of kerosene while minimizing the impact on the environment and human health. Four independent factors, namely anionic surfactant sodium dodecylbenzene sulfonate (X1) (SDBS), oil (X2) (kerosene), water-soluble polymer poly(ethylene glycol) (X3) (PEG), and sodium chloride (X4) (NaCl), were studied using the full factorial design (FFD) model. Four output variables, namely conductivity (Y1), turbidity (Y2), viscosity (Y3), and interfacial tension (IFT) (Y4), were taken as the response variables. All four FFD models have high coefficients of determination and low errors. The developed models were used in a multi-objective optimization (MOO) framework to determine the optimal conditions. The obtained optimal conditions are X1 = 0.01, X2 = 50, X3 = 5, and X4 = 0.1, with an error of 0.9414 between the predicted and experimental objective function values. This result shows the efficiency of the model developed and the system used for the recovery of kerosene, while also having a positive effect on the protection of the environment

The overexpression of the SAPB of Bacillus pumilus CBS and mutated sapB-L31I/T33S/N99Y alkaline proteases in Bacillus subtilis DB430: New attractive properties for the mutant enzyme

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Therapeutic effects of soy isoflavones on -amylase activity, insulin deficiency, liver-kidney function and metabolic disorders in diabetic rats

International audienceNatural estrogens have demonstrated a wide variety of biological activities, which makes them a good candidate for the treatment of diabetes. In vitro, this study evidenced that isoflavones enhanced insulin secretion and inhibited α-amylase activity. In vivo, the findings indicated that soy isoflavones stimulated insulin secretion, increased the hepatic glycogen content and suppressed blood glucose level. The soy isoflavones were also protected hepatic-kidney functions showed by the significant increase in superoxide dismutase, catalase and glutathione peroxidase activities and the decrease in thiobarbituric acid reactive substances, total bilirubin, creatinine and transaminases content. Moreover, soy isoflavones induced a decrease in LDL-cholesterol and triglycerides and an increase in HDL-cholesterol in plasma and liver. Overall, the findings of the current study indicate that soy isoflavones exhibit attractive properties and can, therefore, be considered a promising candidate for future application as alternative therapeutic agents, particularly in the development of anti-diabetic and hypolipidaemic drugs