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    Biosorption of 2,4-D, 2,4-DP and 2,4-DB from aqueous solution by using thermophilic anoxybacillus flavitermus and analysis by high performance thin layer chromatography: equilibrium and kinetic studies
    (Environmental Progress & Sustainable Energy, 2012) Özdemir, Sadin; Matpan, Fatma; Okumuş, Veysi; Dündar, Abdurrahman; Kılınç, Ersin
    In this study, the potential biosorption characteristics of the thermophilic Anoxybacillus flavithermus (A. flavithermus) was investigated for the removal of the chlorophenoxy acid derivates, namely, 2,4-dichlorophenoxy acetic acid (2,4-D), 2,4-dichlorophenoxy propanoic acid (2,4-DP or dichlorprop), and 2,4-dichlorophenoxy butyric acid (2,4-DB). The experiments were performed for the simultaneous biosorption of the studied pesticides. Optimum biosorption conditions were determined as a function of contact time, pH of the solution, amount of biomass, and initial pesticides concentrations. The concentrations of the pesticides in the remaining solutions were simultaneously analyzed by high performance thin layer chromatography. The optimum parameters were found as pH: 4.0 for biosorption medium, 60 min of contact time, 50 mg of bacteria, and 50 mg L21 of initial pesticides concentrations. Langmuir and Freundlich models were applied to describe the biosorption isotherm of the pesticides by A. flavithermus as biomass. Biosorption of pesticides on to A. flavithermus showed pseudo first-order rate kinetics at different initial concentration of pesticides and different temperatures. The experimental adsorption data were fitted both the Langmuir and Freundlich adsorption models. Fourier-transform Infrared spectroscopy was used to understand the bonding mechanism of pesticides to biosorbent and surface functionality of the biosorbent The highest pesticide uptake was calculated from Langmuir isotherm and found to be 24.15 mg/g for 2,4-D Among the studied pesticides, 2,4-DP showed difference adsorption behavior. According to in your comments the reason of this that 2,4-DP contain an asymmetric carbon atom, which provide a molecular chirality.
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    Isolation a thermophilic anoxybacillus flavithermus sp. nov. and production of thermostable α-amylase under solid-state fermentation (SSF)
    (Annals of Microbiology, 2012) Özdemir, Sadin; Matpan, Fatma; Okumuş, Veysi; Dündar, Abdurrahman; Ulutaş, Sefa; Kumru, Mert
    A new bacteria was isolated from hot-spring water of Gazlıgöl, Afyonkarahisar in Turkey. Based on morphological and biochemical tests and 16S rRNA gene sequence analysis, the isolate belonged to the Anoxybacillus flavithermus species which has 99% similarity with the bacterium DNA. The production of α-amylase by thermophilic Anoxybacillus flavithermus was investigated under solid-state fermentation by using some agricultural waste as substrates. Solid substrates such as rice husk, banana husk, millet, water melon husk, lentil bran, wheat bran and maize oil cake were studied for enzyme production. Of these, rice husk was proved as the best substrate for α-amylase production (1,271 U/mg). The maximum α-amylase production was observed as 1,803 U/mg at 72 h, 1,000 μm particle size, 70% initial moisture content (w/v), and 40% inoculum level (v/w). Among the various nitrogen sources tested, 1% peptone (3,170 U/mg) was found to be the best nitrogen source for α-amylase production. As additional carbon sources, 1% starch (2,364 U/mg) enhanced α-amylase production. The optimum temperature for the activity of α-amylase was found to be 70°C. The enzyme was optimally active at pH 6.0 and stable in the pH range of 6.0–8.0.
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    Isolation of a thermophilic Anoxybacillus flavithermus sp nov and production of thermostable ?-amylase under solid-state fermentation (SSF)
    (Bmc, 2012) Ozdemir, Sadin; Matpan, Fatma; Okumus, Veysi; Dundar, Abdurrahman; Ulutas, Mehmet Sefa; Kumru, Mert
    A new bacteria was isolated from hot-spring water of Gazligol, Afyonkarahisar in Turkey. Based on morphological and biochemical tests and 16S rRNA gene sequence analysis, the isolate belonged to the Anoxybacillus flavithermus species which has 99% similarity with the bacterium DNA. The production of alpha-amylase by thermophilic Anoxybacillus flavithermus was investigated under solid-state fermentation by using some agricultural waste as substrates. Solid substrates such as rice husk, banana husk, millet, water melon husk, lentil bran, wheat bran and maize oil cake were studied for enzyme production. Of these, rice husk was proved as the best substrate for alpha-amylase production (1,271 U/mg). The maximum alpha-amylase production was observed as 1,803 U/mg at 72 h, 1,000 mu m particle size, 70% initial moisture content (w/v), and 40% inoculum level (v/w). Among the various nitrogen sources tested, 1% peptone (3,170 U/mg) was found to be the best nitrogen source for alpha-amylase production. As additional carbon sources, 1% starch (2,364 U/mg) enhanced alpha-amylase production. The optimum temperature for the activity of alpha-amylase was found to be 70A degrees C. The enzyme was optimally active at pH 6.0 and stable in the pH range of 6.0-8.0.
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    PRODUCTION AND CHARACTERIZATION OF PARTIALLY PURIFIED EXTRACELLULAR THERMOSTABLE ?-AMYLASE BY Bacillus subtilis IN SUBMERGED FERMENTATION (SmF)
    (Taylor & Francis Inc, 2011) Ozdemir, Sadin; Matpan, Fatma; Guven, Kemal; Baysal, Zubeyde
    A Bacillus strain was isolated from soil samples from the campus area of Dicle University. Based on 16S ribosomal RNA sequencing, the microorganism was closely related to Bacillus subtilis. Effects of different culture medium, incubation time, carbon and nitrogen sources, and various starches, flours, and chemicals on alpha-amylase production were examined. Maximum enzyme production (7516 U/mL) was obtained in a basal medium A containing 0.05% Tween 40 in 24 h. Partially purified enzyme showed maximum activity at 60 degrees C with an optimum pH of 6.0. The effects of 0.2% detergents (sodium dodecyl sulfate [SDS], CHAPS [3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate], and commercial detergent Omo Matic) on partially purified enzyme activity over a period of time (15-150 min) were examined and the order of inhibition effect from the most to the least was found as SDS> Omo Matic> CHAPS. Different metal ions inhibited alpha-amylase activity at low concentrations (1.5 mM). Co2+ was a mild inhibitor and Hg2+ and Cd2+ were potent inhibitors, whereas Ca2+ and Mg2+ increased the enzyme activity. At 20 mM, Ca2+ enhanced enzyme activity, and different Ca2+ concentrations (10-300 mM) were studied.