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    Genotoxic and antigenotoxic potentials of two Usnea species
    (2015) Ceker S.; Orhan F.; Kizil H.E.; Alpsoy L.; Gulluce M.; Aslan A.; Agar G.
    For ages, lichens have long been investigated popularly for biological roles, mainly antitumor, antimicrobial and antioxidant activities. Many positive results were obtained in these previous research. Thus, in this study, we aimed to determine whether extracts of Usnea articulata (UAE) and Usnea filipendula (UFE) possessing a protection against aflatoxin B1(AFB1)-induced genotoxic and oxidative damage. The results of our studies showed that 5 ?M concentrations of AFB1increased the frequencies of sister chromatid exchange (SCE) and the level of malondialdehyde (MDA) and decreased the activities of superoxide dismutase (SOD), glutathione (GSH) and glutathione peroxidase (GPx). However, when 5, 10 and 20 µg/mL concentrations of UAE and UFE was added to AFB1, the frequencies of SCE and MDA level were decreased and SOD, GSH and GPx level were increased. The Ames (Salmonella typhimurium TA1535, TA1537) and WP2 (Escherichia coli) test systems carried out evinced that UAE and UFE possess any mutagenicity, but have antimutagenic effects. Consequently, the results of this experiment have clearly shown that UAE and UFE have strong antioxidative and antigenotoxic effects that are associated with its antioxidant nature. A detailed study can be performed to determine the antioxidant properties of each compound that will extend the use of lichen extracts in food and pharmacy industries. © 2013, SAGE Publications. All rights reserved.
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    Purification and characterization of a pectin lyase produced by Geobacillus stearothermophilus Ah22 and its application in fruit juice production
    (2011) Demir N.; Nadaroglu H.; Tasgin E.; Adiguzel A.; Gulluce M.
    Extracellular pectin lyase (PL) (EC 4.2.2.10) was produced by Geobacillus stearothermophilus Ah22 in solid state fermentation. The PL enzyme was purified 40.8-fold by DEAE-cellulose anion exchange column chromatography and characterized. The molecular weight of the enzyme was determined as 36 kDa by Sephadex G-100 gel filtration chromatography. Purification of the enzymewas verified by SDS-PAGE. The optimumpHand temperature of the enzyme were determined as pH 6.0 and 60°C, respectively. The PL was mostly stable at 40°C. Its activity deceased by 50% after 2 h at 60°C and by 60% after 6 h at 50°C. The V max and K m were calculated as 0.47 mg/mL and 355.3 ?mol/L•min, respectively. The presence of 10 mM Ca 2+, Cu 2+, Mn 2+, Mg 2+, Zn 2+, Hg 2+, Fe 2+ and EDTA, L-cysteine and ascorbic acid significantly enhanced enzyme activity. The purified PL enzyme was used in the production of fruit juices; yields of fruits juice improved significantly compared with controls. © 2011 Springer-Verlag and the University of Milan.
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    Purification and characterization of an alkaline pectin lyase produced by a newly isolated brevibacillus borstelensis (p35) and its applications in fruit juice and oil extraction
    (Springer Verlag, 2014) Demir N.; Nadaroglu H.; Demir Y.; Isik C.; Taskin E.; Adiguzel A.; Gulluce M.
    An alkaline pectin lyase (Pnl) (EC 4.2.2.10) secreted by Brevibacillus borstelensis P35 (genBank number: FJ417406) was purifed using ammonium sulfate fractionation, anion exchange chromatography on DEaE-cellulose and gel fltration chromatography on Sephadex g-150. The pH and temperature optima of the enzyme were found to be 8.0 and 60 °C. The enzyme does not loose activity up to 60 °C if exposed for 1 h. The values of Kmand Vmax of the enzyme were 0.625 mg/ml and 126.32 s-1, respectively. The molecular weight was found to be 36 ± 01 kDa. The presence of 10 mM concentration of Ca2+, Cu2+, Mn2+, Mg2+, Zn2+, Hg2+, Fe2+ and EDTa, L-cystein, ascorbic acid signifcantly enhanced the Pnl of the purifed enzyme. In the course of the laboratory trials, it was demonstrated that Pnl from B. borstelensis (P35) could be successfully applied to the production and clarif-cation of fruit juice and oil extraction. © Springer-Verlag Berlin Heidelberg 2014