An efficient methodology for the purification of date palm peroxidase: Stability comparison with horseradish peroxidase (HRP)

被引:32
|
作者
Al-Bagmi, Moneera Saud [1 ]
Khan, Mohd Shahnawaz [1 ]
Ismael, Mohamad Alhasan [1 ]
Al-Senaidy, Abdulrahman M. [1 ]
Ben Bacha, Abir [1 ]
Husain, Fohad Mabood [2 ]
Alamery, Salman Freeh [3 ]
机构
[1] King Saud Univ, Coll Sci, Dept Biochem, Prot Res Chair, Riyadh, Saudi Arabia
[2] King Saud Univ, Dept Food & Agr Sci, Riyadh, Saudi Arabia
[3] King Saud Univ, Coll Sci, Ctr Excellence Biotechnol Res, Dept Biochem, Riyadh, Saudi Arabia
关键词
Peroxidases; HRP; Date palm; pH; Thermal; CD fluorescence; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURE; OXIDASE;
D O I
10.1016/j.sjbs.2018.04.002
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 +/- 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 a-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. (C) 2018 Production and hosting by Elsevier B.V. on behalf of King Saud University.
引用
收藏
页码:301 / 307
页数:7
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