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( Zhixiang Lv ),( Qingmei Yu ),( Zhou Wang ),( Ruijiang Liu ) 한국미생물생명공학회(구 한국산업미생물학회) 2019 Journal of microbiology and biotechnology Vol.29 No.6
Magnetic Ni<sub>0.7</sub>Co<sub>0.3</sub>Fe<sub>2</sub>O<sub>4</sub> nanoparticles that were prepared via the rapid combustion process were functionalized and modified to obtain magnetic Ni<sub>0.7</sub>Co<sub>0.3</sub>Fe2O<sub>4</sub>@SiO<sub>2</sub>-CHO nanocomposites, on which penicillin G acylase (PGA) was covalently immobilized. Selections of immobilization concentration and time of fixation were explored. Catalytic performance of immobilized PGA was characterized. The free PGA had greatest activity at pH 8.0 and 45 ℃ while immobilized PGA’s a ctivities p eaked at p H 7.5 and 4 5 ℃. Immobilized PGA had better thermal stability than free PGA at the range of 30-50 ℃ for different time intervals. The activity of free PGA would be 0 and that of immobilized PGA still retained some activities at 60 ℃ after 2 h. V<sub>max</sub> and K<sub>m</sub> of immobilized PGA were 1.55 mol/min and 0.15 mol/l, respectively. Free PGA’s V<sub>max</sub> and K<sub>m</sub> separately were 0.74 mol/min and 0.028 mol/l. Immobilized PGA displayed more than 50% activity after 10 successive cycles. We concluded that immobilized PGA with magnetic Ni<sub>0.7</sub>Co<sub>0.3</sub>Fe<sub>2</sub>O<sub>4</sub>@SiO<sub>2</sub>-CHO nanocomposites could become a novel example for the immobilization of other amidohydrolases.