EVALUATION OF ANTIOXIDANT, ANTIRADICALIC AND ANTIMICROBIAL ACTIVITIES OF OLIVE PITS (Olea eurOpaea L.)

The antioxidant and radical scavenging properties of olive pits (Olea europaea L.) were investigated through the following analyses in this study: The total antioxidant activity by the ferric thiocyanate method; 2,2'-azino-bis-(3-ethylbenzothiazole-6-sulphonate) (ABTS) radical scavenging activity; superoxide anion radical (O 2 -) scavenging activity; the total reduction power by the potassium ferricyanide reduction method; Cupric ions (Cu ). Besides, the total phenolic and flavonoid contents of the olive pits (OP) were determined. In addition, α-tocopherol, butylatedhydroxyanisole (BHA) and quercetin were used as reference antioxidant compounds. OP-aqueous and OP-ethanol extractsboth exhibited the highest phenol (OP-AE:95.3; OP-EE: 144.3 μg GAE mg -1 extract) and flavonoid (OP-AE: 183.7; OP-EE:262.4μg QE mg -1 extract) contents, and displayed the highest antioxidant activity. In addition, OP-AE and OP-EE exhibited higher antibacterial activity against eleven bacteria with Minimum Inhibitory Concentrations (MIC) values, ranging from 12.50 to 250 mu l/mL

Purification and characterisation of laccase from lactarius volemus and its application in removal of phenolic compounds from fruit juice

Laccases are multicopper oxidases (EC 1.10.3.2.), widely distributed in fungi, higher plants and bacteria. In this research, a laccase from Lactarius volemus (Russulaceae) was purified by 73.08 fold using precipitate of saturation (NH4)2SO4, DEAE-cellulose and Sephacryl S200. It was shown that purified enzyme was homogeneous in term of SDS-PAGE with molecular mass estimated of 30 kDa. The pH was optimal at 4.0, enzyme was stable at pH 3.0-5.0 and optimal temperature was at 50°C. Cu2+ and Fe2+ were activated to the purified laccase enzyme, and it was partially inhibited by 5 mM concentration of some metal salts and EDTA, urea, SDS, L-cysteine, dithioeritritol and ?-mercaptoethanol. In addition, it was investigated whether the purified and characterized laccase enzyme would remove the phenolic compound of some fruit juices which are responsible for haze formation and browning during storage. Their application led to reduction of total phenolic compounds for apple, apricot, cherry and grape juice. As a result, the effect of these enzymatic treatments on total phenol content and clarity of the juice were evaluated using a central composite design. This laccase enzyme had potential application in food processing

Purification, characterization of phytase enzyme from Lactobacillus plantarum bacteria and determination of its kinetic properties

Phytases (myo-inositol hexakisphosphate phosphohydrolase, EC 3.1.3.8) catalyze the release of phosphate from phytates. Many of the cereal grains, legumes and oilseeds store phosphorus in phytate form. Phytases can be produced by plants, animals and microorganisms. However, the ones with microbial origin are the most promising for commercial uses and biotechnological applications. In this study, phytase enzyme isolation from Lactobacillus spp. ATCC strain and its characterization was carried out. Phytase production from bacterial strains was determined by zone production formed around colonies after 48 h of incubation at 30°C in MRS medium. Optimum pH and optimum temperature values of the phytase enzyme that was partially purified by precipitation of ammonium sulphate from Lactobacillus plantarum, extracellularly from bacteria put into liquid culture medium, were measured. Optimum activity of the enzyme derived from L. plantarum bacterium was at 30°C and pH 6.0. It was observed that L. plantarum's extracellular enzyme maintains its 90% of activity at 10-100°C for 120 min. Effects of certain metal ions on activity of phytase enzyme derived from L. plantarum were also investigated. Of these, CuCl2, MnCl2, CoCl2, CaCl2 and ZnCl2 decreased enzyme activity significantly. FeCl2 increased enzyme activity by 121%. Based on these results, the phytase enzyme of L. plantarum is considered suitable for use in many industrial areas, in feed and food industries in particular, due to its thermal stability and resistance to metal ions.Keywords: Purification, characterization, phytase, Lactobacillus plantarum.African Journal of Biotechnology, Vol 13(23) 2373-237

Investigation of in vivo effect of florfenicol on metabolic-antioxidantenzymes’ activities on Morkaraman normal and lactating sheep

AbstractFlorfenicol is a broad-spectrum, primarily bacteriostatic, antibiotic with a range of activity including many gram-negative and gram-positive organisms. This study was carried out to determine the in vivo effect of florfenicol on the paraoxonase (PON), catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GPX) activities on Morkaraman normal and lactating sheep. For these studies, three normal and three lactating sheep groups (55–60kg) were selected for each of intramuscular administration for 24h of florfenicol (30mg/kg). Three normal and three lactating sheep groups were included in the study for a control group, which were not subjected to drug administration. For florfenicol, the mean of the hemolysate paraoxonase, glutathione peroxidase, superoxide dismutase, catalase activities and milk paraoxonase, catalase, lactoperoxidase, superoxide dismutase activity was determined and compared to the control group. According to the research results, while PON1 and CAT enzymes were activated, SOD and GPX enzymes were inhibited by florfenicol in both normal and lactating Morkaraman sheep. While florfenicol did not change milk PON1 and SOD activities, it significantly inhibited milk CAT and LPO enzyme activities

Experimental study to remediate acid fuchsin dye using laccase-modified zeolite from aqueous solutions

This paper studies, the removal of acid fuchsin dye from aqueous solutions using zeolite natural material after its modification with laccase from Russulaceae (Lactarius volemus). Batch adsorption experiments were performed as a function of pH, contact time, temperature, and adsorbent dosage. The optimum results were obtained at pH 5, contact time of 60 min, temperature of 60ºC, and an adsorbent dosage of 1.5 mg/mL. The isotherm studies show that the adsorption experimental data are fitted well by Langmuir isotherm model. The adsorption capacity found is 31 mg/g. The kinetics of AFD adsorption on LMZ is best described with the pseudo-first-order kinetics model. Thermodynamic parameters including Gibbs free energy, enthalpy, and entropy changes indicate that the adsorption of Acid Fuchsin dye onto laccase-modified zeolite is feasible, spontaneous, and exothermic. The results show that laccase-modified zeolite can be used as an alternative lowcost adsorbent for dye removal from aqueous solutions. © 2015, HARD Publishing Company. All rights reserved