Immobilization of Urease onto Modified Egg Shell Membrane through Cross Linking.

Background: Immobilization is an approach in industry to improve stability and reusability of urease. The efficiency of this technique depends on the type of membrane and the method of stabilization.Methods: The PEI-modified egg shell membrane was used to immobilize urease by absorption and glutaral...

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Publicado en:Iranian Biomedical Journal Vol. 26; no. 1; pp. 132 - 142
Autores principales: Morovvat, Fatemeh, Samsam Shariat, Seyed Ziae Aldin, Davoudi, Maryam, Norouzian, Dariush
Formato: Journal Article
Publicado: Pasteur Institute of Iran Jan2022
Acceso en línea:Ver este registro en EBSCOhost
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        1028852X
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      jtl: Iranian Biomedical Journal
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      dt: Jan2022
      vid: 26
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      pub: Pasteur Institute of Iran
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        10.52547/ibj.26.2.132
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        154943712
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        atl: Immobilization of Urease onto Modified Egg Shell Membrane through Cross Linking.
      aug:
        au:
          Morovvat, Fatemeh
          Samsam Shariat, Seyed Ziae Aldin
          Davoudi, Maryam
          Norouzian, Dariush
        affil: Department of Clinical Biochemistry, Isfahan Pharmaceutical Sciences Research Center, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
      sug:
        subj:
          Enzymes
          Urease
          Hydrogen-Ion Concentration
          Animals
          Kinetics
          Ways of Coping Questionnaire
      ab: Background: Immobilization is an approach in industry to improve stability and reusability of urease. The efficiency of this technique depends on the type of membrane and the method of stabilization.Methods: The PEI-modified egg shell membrane was used to immobilize urease by absorption and glutaraldehyde cross-linking methods. The membranes were characterized by Fourier-transform infrared spectroscopy (FTIR) and AFM, and Nessler method was applied to measure the kinetic of the immobilized enzymes. Finally, the storage stability (6 °C for 21 days) and reusability (until enzyme activity reached to zero) of the immobilized enzymes were investigated.Results: Based on FTIR, three new peaks were observed in both the absorption- (at 1389.7, 1230.8, and 1074.2 cm-1) and the cross-linking (at 1615-1690, 1392.7, 1450 cm-1) immobilized enzymes. The surface roughness of the native membrane was altered after PEI treatment and enzyme immobilization. The optimal pH of cross-linking immobilized enzymes was shifted to a more neutral pH, while it was alkaline in adsorption-immobilized and free enzymes. The reaction time decreased in all immobilized enzymes (100 min for free enzyme vs. 60 and 30 min after immobilizing by adsorption and cross-linking methods, respectively). The optimal temperature for all enzymes was 70 °C and they had a higher Km and a lower Vmax than free enzyme. The stability and reusability of urease were improved by both methods.Conclusion: Our findings propose these approaches as promising ways to enhance the urease efficiency for its applications in industries and medicines.
      pubtype: Academic Journal
      doctype: Journal Article
      ougenre: Article
    language: English
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