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    Cadmium biosorption by Bacillus circulans strain EB1
    (Springer, 2005) Yilmaz, EI; Ensari, NY
    A heavy metal resistant bacterium, Bacillus circulans strain EB1 showed a high cadmium biosorption capacity coupled with a high tolerance to this metal when grown in its presence. Bacillus circulans EB1 cells grown in the presence of 28.1 mg cadmium/l were capable of removing cadmium with a specific biosorption capacity of 5.8 mg Cd/g dry wt biomass in the first 8 h. When the cells were pre-conditioned with low concentrations of cadmium in pre-grown medium, the uptake was increased to 6.7 mg Cd/g dry wt biomass. The maximum uptake of cadmium was during mid-logarithmic phase of growth. The resting cells (both wet and dry) of EB1 were also able to biosorb cadmium. Specific biosorption capacities of wet and dry biomass were 9.8 and 26.5 mg Cd/g dry wt biomass, respectively. Maximum cadmium removals by both wet and dry cells were at pH 7.0. The results showed that the cadmium removal capacity of resting cells was markedly higher than that of growing cells. Since both growing and resting cells had a high biosorption capacity for cadmium, EB1 cells could serve as an excellent biosorbent for removal of cadmium from natural environments.
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    Effect of bovine serum albumine on production of alpha-amylase and amylase thermostability in Bacillus subtilis
    (Mbr Press Inc, 1997) Otludil, B; Ensari, NY; Aguloglu, S; Uyar, F
    Thermal stability of alpha-amylase from Bacillus subtilis isolated from thermal Cermik hot spring was studied. alpha-amylase was purified from media with and without bovine serum albumen (BSA). The enzyme was stable at 68 degrees C when purified from media with different concentrations of BSA;however,it was observed to be stable at 75 degrees 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 mu g/ml BSA. Production of alpha-amylase and proteases was induced in presence of 180-240 mu g/ml BSA.
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    Purification and characterization of alkaline proteinase from alkalophilic Bacillus sp.
    (Maik Nauka/Interperiodica/Springer, 2001) Muderriszade, A; Ensari, NY; Aguloglu, S; Otludil, B
    Alkaline proteinase was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37 degreesC. Calcium divalent cation was effective in stabilizing the enzyme, especially at higher temperatures. The proteolytic activity was inhibited by the specific serine proteinase inhibitor PMSF (phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, and Hg. The enzyme was stable in the presence of detergents, such as Triton-X100, Tween-80. SDS (sodium dodecyl sulfate), and EDTA (ethylenediaminetetraacetic acid), at pH 11.5 and 37 degreesC for 30 min. The optimum pH was 11.5 at 37 degreesC, and the optimum temperature was 62 degreesC at pH 11.5.