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  • Metal-Chelate Immobilization of Lipase onto Polyethylenimine Coated MCM-41 for Apple Flavor Synthesis

    Author(s)
    Sadighi, Armin
    Motevalizadeh, Seyed Farshad
    Hosseini, Morteza
    Ramazani, Ali
    Gorgannezhad, Lena
    Nadri, Hamid
    Deiham, Behnaz
    Ganjali, Mohammad Reza
    Shafiee, Abbas
    Faramarzi, Mohammad Ali
    Khoobi, Mehdi
    Griffith University Author(s)
    Gorgannezhad, Lena
    Year published
    2017
    Metadata
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    Abstract
    An enzyme immobilized on a mesoporous silica nanoparticle can serve as a multiple catalyst for the synthesis of industrially useful chemicals. In this work, MCM-41 nanoparticles were coated with polyethylenimine (MCM-41@PEI) and further modified by chelation of divalent metal ions (M = Co2+, Cu2+, or Pd2+) to produce metal-chelated silica nanoparticles (MCM-41@PEI-M). Thermomyces lanuginosa lipase (TLL) was immobilized onto MCM-41, MCM-41@PEI, and MCM-41@PEI-M by physical adsorption. Maximum immobilization yield and efficiency of 75 ± 3.5 and 65 ± 2.7% were obtained for MCM@PEI-Co, respectively. The highest biocatalytic ...
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    An enzyme immobilized on a mesoporous silica nanoparticle can serve as a multiple catalyst for the synthesis of industrially useful chemicals. In this work, MCM-41 nanoparticles were coated with polyethylenimine (MCM-41@PEI) and further modified by chelation of divalent metal ions (M = Co2+, Cu2+, or Pd2+) to produce metal-chelated silica nanoparticles (MCM-41@PEI-M). Thermomyces lanuginosa lipase (TLL) was immobilized onto MCM-41, MCM-41@PEI, and MCM-41@PEI-M by physical adsorption. Maximum immobilization yield and efficiency of 75 ± 3.5 and 65 ± 2.7% were obtained for MCM@PEI-Co, respectively. The highest biocatalytic activity at extremely acidic and basic pH (pH = 3 and 10) values were achieved for MCM-PEI-Co and MCM-PEI-Cu, respectively. Optimum enzymatic activity was observed for MCM-41@PEI-Co at 75 °C, while immobilized lipase on the Co-chelated support retained 70% of its initial activity after 14 days of storage at room temperature. Due to its efficient catalytic performance, MCM-41@PEI-Co was selected for the synthesis of ethyl valerate in the presence of valeric acid and ethanol. The enzymatic esterification yield for immobilized lipase onto MCM-41@PEI-Co was 60 and 53%, respectively, after 24 h of incubation in n-hexane and dimethyl sulfoxide media.
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    Journal Title
    Applied Biochemistry and Biotechnology
    Volume
    182
    Issue
    4
    DOI
    https://doi.org/10.1007/s12010-017-2404-9
    Subject
    Biological Sciences not elsewhere classified
    Biological Sciences
    Technology
    Publication URI
    http://hdl.handle.net/10072/344147
    Collection
    • Journal articles

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