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    Turnip (brassica rapa) peroxidase: Purification and characterization

    , Article Industrial and Engineering Chemistry Research ; Volume 48, Issue 23 , Volume 48, Issue 23 , 2009 , Pages 10614-10618 ; 08885885 (ISSN) Motamed, S ; Ghaemmaghami, F ; Alemzadeh, I ; Sharif University of Technology
    ACS  2009
    Partial purification of plant peroxidase from turnip (Brassica rapa) was optimized. Aqueous two phase system and precipitation by ammonium sulfate (as two parallel purification methods) were used. Polyethylene glycol/ammonium sulfate/NaCl (25:7:3%, w/v) system followed by gel-filtration chromatography gave a purification factor of about 36 fold. On the other hand, ammonium sulfate precipitation (60-80% deg) followed by gel filtration gave only about 13 purification fold. Hence, the aqueous two-phase system was more efficient and useful method as a primary purification step since it was less laborious, less time-consuming, and led to more purification factor. The partially purified turnip... 

    Biodegradation of synthetic dye using partially purified and characterized laccase and its proposed mechanism

    , Article International Journal of Environmental Science and Technology ; Volume 16, Issue 12 , 2019 , Pages 7805-7816 ; 17351472 (ISSN) Ghobadi Nejad, Z ; Borghei, S. M ; Yaghmaei, S ; Sharif University of Technology
    Center for Environmental and Energy Research and Studies  2019
    The supernatant obtained from the extracellular laccase produced by Phanerochaete chrysosporium was used as the enzyme source to conduct a partial purification, characterization and dye decolorization study. The partially purified enzyme was stable in the pH range of 3–5 and showed an optimum activity at pH 4.0, using guaiacol as a substrate. Laccase stability of pH was determined and discovered to retain 100% of its activity at a pH of 4.0 after 2 h. The maximum enzyme activity was obtained between 30 and 50 °C. The maximum velocity and Michaelis constant were calculated as 3.171 µM−1·min and 1628.23 µM, respectively. The enzyme was activated by Fe2+, Zn2+, Ca2+ and Cu2+, while Hg2+, Mn2+,...