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An efficient methodology for the purification of date palm peroxidase: Stability comparison with horseradish peroxidase (HRP).
Saud Al-Bagmi, Moneera; Shahnawaz Khan, Mohd; Alhasan Ismael, Mohamad; Al-Senaidy, Abdulrahman M; Ben Bacha, Abir; Mabood Husain, Fohad; Alamery, Salman Freeh.
Afiliación
  • Saud Al-Bagmi M; Protein Research Chair, Department of Biochemistry, College of Sciences, King Saud University, Riyadh, Saudi Arabia.
  • Shahnawaz Khan M; Protein Research Chair, Department of Biochemistry, College of Sciences, King Saud University, Riyadh, Saudi Arabia.
  • Alhasan Ismael M; Protein Research Chair, Department of Biochemistry, College of Sciences, King Saud University, Riyadh, Saudi Arabia.
  • Al-Senaidy AM; Protein Research Chair, Department of Biochemistry, College of Sciences, King Saud University, Riyadh, Saudi Arabia.
  • Ben Bacha A; Protein Research Chair, Department of Biochemistry, College of Sciences, King Saud University, Riyadh, Saudi Arabia.
  • Mabood Husain F; Department of Food and Agriculture science, King Saud University, Riyadh, Saudi Arabia.
  • Alamery SF; Center of Excellence in Biotechnology Research, Dept. Of Biochemistry, College of Science, King Saud University, Saudi Arabia.
Saudi J Biol Sci ; 26(2): 301-307, 2019 Feb.
Article en En | MEDLINE | ID: mdl-31485169
In the present study, Peroxidase from date palm (Phoenix dactylifera) leaves was purified to homogeneity by three-step procedure including aqueous two-phase system, hydrophobic and Ion-exchange chromatography. The enzyme migrated as single band on SDS-PAGE giving molecular weight of 68 ±â€¯3 kDa. The purification factor for purified date palm peroxidase was 68 with high 41% yield. Enzymatic assays together with far-UV circular dichroism (CD), intrinsic and extrinsic fluorescence studies were carried out to monitor the structural stability of date palm and horseradish peroxidase (HRP) against various pH and temperatures. Activity measurements illustrated different pH stability for date palm and HRP. Both peroxidases are more susceptible to extreme acidic conditions as suggested by 4 & 15 nm red shift in date palm and HRP, respectively. Secondary structure analysis using far UV-CD exhibited predominance of α-helical (43.8%) structure. Also, pH induces loss in the secondary structure of date palm peroxidase. Thermal stability analysis revealed date palm peroxidase is more stable in comparison to HRP. In summary, date palm peroxidases could be promising enzymes for various applications where extreme pH and temperature is required.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Saudi J Biol Sci Año: 2019 Tipo del documento: Article País de afiliación: Arabia Saudita Pais de publicación: Arabia Saudita
Texto completo
Añadir a Mi BVS
Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Saudi J Biol Sci Año: 2019 Tipo del documento: Article País de afiliación: Arabia Saudita Pais de publicación: Arabia Saudita