Mehmet Dogru

Equilibrium and thermodynamic studies on biosorption of Pb(II) onto Candida albicans biomass.

Biosorption of Pb(II) ions from aqueous solutions was studied in a batch system by using Candida albicans. The optimum conditions of biosorption were determined by investigating the initial metal ion concentration, contact time, temperature, biosorbent dose and pH. The extent of metal ion removed increased with increasing contact time, initial metal ion concentration and temperature. Biosorption equilibrium time was observed in 30min. The Freundlich and Langmuir adsorption models were used for the mathematical description of biosorption equilibrium and isotherm constants were also evaluated. The maximum biosorption capacity of Pb(II) on C. albicans was determined as 828.50+/-1.05, 831.26+/-1.30 and 833.33+/-1.12mgg(-1), respectively, at different temperatures (25, 35 and 45 degrees C). Biosorption showed pseudo second-order rate kinetics at different initial concentration of Pb(II) and different temperatures. The activation energy of the biosorption (Ea) was estimated as 59.04kJmol(-1) from Arrhenius equation. Using the equilibrium constant value obtained at different temperatures, the thermodynamic properties of the biosorption (DeltaG degrees , DeltaH degrees and DeltaS degrees ) were also determined. The results showed that biosorption of Pb(II) ions on C. albicans were endothermic and spontaneous. The optimum initial pH for Pb(II) was determined as pH 5.0. FTIR spectral analysis of Pb(II) adsorbed and unadsorbed C. albicans biomass was also discussed.

Production of Lipase by a Newly Isolated Bacillus coagulans Under Solid-State Fermentation Using Melon Wastes

SummaryAn extracellular lipase was produced by Bacillus coagulans by solid-state fermentation. Solid waste from melon was used as the basic nutrient source and was supplemented with olive oil. The highest lipase production (78,069 U/g) was achieved after 24h of cultivation with 1% olive oil enrichment. Enzyme had an optimal activity at 37°C and pH 7.0, and sodium dodecyl sulfate increased lipase activity. NH 4NO3 increased enzyme production, whereas organic nitrogen had no effect. The effect of the type of carbon sources on lipolytic enzyme production was also studied. The best results were obtained with starch and maltose (148,932 and 141,629 U/g, respectively), whereas a rather low enzyme activity was found in cultures grown on glucose and galactose (approx 118,769 and 123,622 U/g, respectively). Enzyme was inhibited with Mn+2 and Ni+2 by 68 and 74%, respectively. By contrast, Ca+2 enhanced enzyme production by 5%.

Production of Extracellular Alkaline α‐Amylase by Solid State Fermentation with a Newly Isolated Bacillus sp.

Abstract Production of alkaline α‐amylase employing our laboratory isolate, Bacillus sp., under solid state fermentation, was optimized. The effect of wheat bran and lentil husk was examined. Lentil husk exhibited the highest enzyme production. The appropriate incubation time, inoculum size, moisture level, and buffer solution level were determined. Maximum yields of 216,000 and 172,800 U/g were achieved by employing lentil husk and wheat bran as substrates in 0.1 M carbonate/bicarbonate buffer at pH 10.0 with 30% initial moisture level at 24 h. Inoculum size and buffer solution level were found to be 20% and 1:0.5 for two solid substrates.

Dyeing of wool fibres with natural dyes: effect of proteolytic enzymes.

Abstract In spite of the widespread use of proteins (casein, peptone, etc.) and protein fragments as a substrate for the proteolytic enzymes, a substrate prepared from dyes that adsorb onto appropriate materials, such as wool and cotton, are also used for enzyme activity determination. In the point of view of this thought, it was our aim to develop the substrates which are easily and economically obtainable and also environmentally safer for the frequently used proteolytic enzymes, such as subtilisin carlsberg, trypsin, chymotrypsin, and protease type XVI and, if possible, to prepare the specific substrate at least for one of these enzymes. For this aim, wool was dyed with natural dyes such as juglone, lawsone, berberine, and quercetin. The optimum pH, incubation time, and agitation rate were determinated. The results indicate that, of all the tested enzymes on wool‐dye complex as an insoluble subtrate, the most appropriate complex was found to be wool‐lawsone complex.

Barrier height enhancement of metal/ semiconductor contact by an enzyme biofilm interlayer

A metal/interlayer/semiconductor (Al/enzyme/p-Si) MIS device was fabricated using α-amylase enzyme as a thin biofilm interlayer. It was observed that the device showed an excellent rectifying behavior and the barrier height value of 0.78 eV for Al/α-amylase/p-Si was meaningfully larger than the one of 0.58 eV for conventional Al/p-Si metal/semiconductor (MS) contact. Enhancement of the interfacial potential barrier of Al/p-Si MS diode was realized using enzyme interlayer by influencing the space charge region of Si semiconductor. The electrical properties of the structure were executed by the help of current–voltage and capacitance–voltage measurements. The photovoltaic properties of the structure were executed under a solar simulator with AM1.5 global filter between 40 and 100 mW/cm2 illumination conditions. It was also reported that the α-amylase enzyme produced from Bacillus licheniformis had a 3.65 eV band gap value obtained from optical method.

Cu2+-attached pumice particles embedded composite cryogels for protein purification.

Abstract In this study, chromatographic performance of Cu2+-attached pumice particles embedded to monolithic cryogels (Cu2+-APPsEMC) for human serum albumin (HSA) was investigated. Monolithic composite cryogels were prepared by means of polymerization of gel-forming precursors at sub-zero temperatures. The chemical composition of pumice and surface of composite cryogels were determined by X-ray fluorescence spectrometer and scanning electron microscopy, respectively. The highest adsorption capacity (549.5 mg/g pumice) of cryogels was achieved at phosphate buffer of pH 8.0 with initial HSA solution of 3 mg/ml. SDS-PAGE analysis was performed for the samples studied on human serum to determine HSA adsorption/desorption performance of cryogel qualitatively.

Use of Natural Dye‐Casein Complexes: Effect of Proteolytic Treatment

Abstract The activity of proteolytic enzymes is commonly measured using casein as a substrate. A modified caseinolysis assay was developed with natural dyes such as juglone, lawsone, berberine, and quercetin for Subtilisin carlsberg, protease type XVI, and trypsin, respectively. The pH dependence and incubation time were determined. Km, Vmax, and kcat/Km values were also determined for these enzymes. Lawsone was found to be a better substrate than the others.