Yazar "Aguloglu S." seçeneğine göre listele

Listeleniyor 1 - 4 / 4
  • [ X ]
    Öğe
    Effect of bovine serum albumine on production of ?-amylase and amylase thermostability in Bacillus subtilis
    (1997) Otludil B.; Ensari N.Y.; Aguloglu S.; Uyar F.
    Thermal stability of ?-amylase from Bacillus subtilis isolated from thermal Cermik hot spring was studied ?-amylase was purified from media with and without bovine serum albumen (BSA). The enzyme was stable at 68°C when purified from media with different concentrations of BSA; however, it was observed to be stable at 75°C when interacted with different concentrations of BSA. B. subtilis was grown in different concentrations of BSA. The best bacterial growth was identified to be in the medium with 180 ?g/ml BSA. Production of ?-amylase and proteases was induced in presence of 180-240 ?g/ml BSA.
  • [ X ]
    Öğe
    Evaluating the fracture strength of three different provisional crowns
    (2010) Zortuk M.; Ozdemir E.; Aguloglu S.
    With the advent of new provisional crown materials, it has become imperative to evaluate their strength in order to select the appropriate crown material. This study examined the fracture resistance of three different provisional materials. To simulate oral conditions, the specimens were fabricated in brass molds, ensuring their similarity to premolars. The 33 fabricated specimens were divided into three groups (n=11) and stored at 37°C in artificial saliva (1.6 g NaHCO3, 0.4 g NaH2PO4H2O, and 0.1 g CaCl2H2O per L H2O). After conditioning, the fracture resistance was assessed using a universal testing machine (Testometric). Analysis of variance and Student's t-test were used for statistical analysis. The study concluded that the mechanical properties of provisional restorative materials are strongly influenced by their proportions of methyl methacrylate and bisphenol A glycidyl methacrylate.
  • [ X ]
    Öğe
    Purification and characteristics of alkaline proteinase from alkalophylic Bacillus sp.
    (2001) Muderrizade A.; Ensari N.Y.; Aguloglu S.; Otludil B.
    Alkaline protease was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37 degrees C. Calcium divalent cation was effective to stabilize the enzyme especially at higher temperatures. The proteolytic activity was inhibited by active site inhibitors of PMSF (Phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, Hg. The enzyme was stable in the presence of some detergents, such as Triton-X-100, Tween-80, SDS (sodium dodecyl sulfate) and EDTA (ethylendiaminetetraacetic acid), pH 11.5 and 37 degrees C for 30 min. The optimum pH was 11.5 at 37 degrees C and the optimum temperature was 62 degrees C at pH 11.5.
  • [ X ]
    Öğe
    Purification and characterization of alkaline protease from alkalophilic Bacillus sp.
    (2001) Muderriszade A.; Ensari N.Y.; Aguloglu S.; Otludil B.
    Alkaline protease was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37°C. Calcium divalent cation was effective to stabilize the enzyme especially at higher temperatures. The proteolytic activity was inhibited by active site inhibitors of PMSF (Phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, Hg. The enzyme was stable in the presence of some detergents, such as Triton-X-100, Tween-80, SDS (sodium dodecyl sulfate) and EDTA (ethylendiaminetetraacetic acid), pH 11.5 and 37°C for 30 min. The optimum pH was 11.5 at 37°C and the optimum temperature was 62°C at pH 11.5.