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Covalent immobilization of invertase on PAMAM-dendrimer modified superparamagnetic iron oxide nanoparticles

Uzun, K.; Cevik, E.; Senel, M.; Sozeri, H.; Baykal, A.; Abasiyanik, M. F.; Toprak, M. S.


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        "affiliation": "Fatih Univ, Fac Arts & Sci, Dept Chem, TR-34500 Istanbul, Turkey", 
        "name": "Uzun, K."
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      {
        "affiliation": "Fatih Univ, Fac Arts & Sci, Dept Chem, TR-34500 Istanbul, Turkey", 
        "name": "Cevik, E."
      }, 
      {
        "affiliation": "Fatih Univ, Fac Arts & Sci, Dept Chem, TR-34500 Istanbul, Turkey", 
        "name": "Senel, M."
      }, 
      {
        "affiliation": "Natl Metrol Inst, TUBITAK UME, TR-41470 Gebze, Turkey", 
        "name": "Sozeri, H."
      }, 
      {
        "affiliation": "Fatih Univ, Fac Arts & Sci, Dept Chem, TR-34500 Istanbul, Turkey", 
        "name": "Baykal, A."
      }, 
      {
        "affiliation": "Fatih Univ, Fac Engn, Dept Genet & Bioengn, TR-34500 Istanbul, Turkey", 
        "name": "Abasiyanik, M. F."
      }, 
      {
        "affiliation": "Royal Inst Technol KTH, Dept Funct Mat, S-16440 Stockholm, Sweden", 
        "name": "Toprak, M. S."
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    "description": "In this study, polyamidoamine (PAMAM) dendrimer was synthesized on the surface of superparamagnetite nanoparticles to enhance invertase immobilization. The amount of immobilized enzyme on the surface-hyperbranched magnetite nanoparticle was up to 2.5 times (i.e., 250%) as much as that of magnetite nanoparticle modified with only amino silane. Maximum reaction rate (V (max)) and Michaelis-Menten constant (K (m)) were determined for the free and immobilized enzymes. Various characteristics of immobilized invertase such as; the temperature activity, thermal stability, operational stability, and storage stability were evaluated and results revealed that stability of the enzyme is improved upon immobilization.", 
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