Yazar "Guduk, Elif" seçeneğine göre listele

Listeleniyor 1 - 2 / 2
  • Küçük Resim
    Öğe
    Isolation, Purification and Characterization of New Cold Active Subtilisin-like Protease from Bacillus sp. strain EL-GU1
    (2019) Guduk, Elif; Yasar, Gulhan; Gulhan, Unzile Guven; Aktaş, Fatih
    One of the important hydrolytic enzymes are proteases that slice peptide bonds between amino acid residues.Proteases have various industrial applications including detergent, food, pharmaceutical, leather and diagnosticreagent industries. Among them, the most commercialized enzymes are alkaline proteases in the industry. Due totheir potential applications in the detergent industry as cleaning additives, they are of particular interest. In thisstudy, a novel protease from Bacillus sp. strain EL-GU1 was reported showing highest activity at pH 6 and20°C. The novel protease was purified by using ammonium sulfate precipitation and identified by 16S rDNAsequencing. Highest activity was observed as 3300 µmol/min-1mg-1 when casein used as a substrate. Kineticparameters of the enzyme were determined; KM, Vmax, kcat and catalytic efficiency values were calculated as 1.4mM, 1 mM/s, 2.10-7s-1, 0.14 10-7s-1M-1, respectively. These results indicated that the novel cold active proteasefrom Bacillus sp. strain EL- GU1 can be a good candidate for the detergent industry.
  • Küçük Resim
    Öğe
    Screening, partial purification and characterization of the hyper-thermophilic lipase produced by a new isolate ofBacillus subtilisLP2
    (Taylor & Francis Ltd, 2020) Yasar, Gulhan; Gulhan, Unzile Guven; Guduk, Elif; Aktas, Fatih
    Lipases are one of the most important catalysts for several industries such as detergent, dairy, and textile industry due to their bio-catalytic ability in aqueous and non-aqueous media. Stability to extreme conditions is an important property since it makes enzymes suitable to several industrial processes. In this study, lipase producing soil bacteria were screened and identified with 16S rDNA sequencing. A new hyper-thermophilic lipase named asBacillus subtilis LP2isolate was partially purified by ammonium sulphate precipitation with 17.8-fold purification and 583 U/mg specific activity. Maximum activity was exhibited at pH 7 and 80 degrees C with the substrate tween 80 K(M)and V(max)values were calculated as 18.3 mM and 680 U/mg with a catalytic efficiency (k(cat)/K-M) of 307 s(-1)M(-1). These results indicate that lipase fromBacillus subtilis LP2can be a valuable candidate for industrial applications such as organic synthesis and fats and oils industry due to their efficient catalysis in higher temperatures.