کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8331932 | 1540246 | 2015 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expression of A. niger US368 xylanase in E. coli: Purification, characterization and copper activation
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The XAn11 cDNA was cloned in pET-28a(+) and the recombinant plasmid was transformed in Escherichia coli. The His-tagged r-XAn11 was purified using Ni-NTA affinity and anion exchange chromatography. The enzyme showed a specific activity of 415.1 U mgâ1 and a molecular mass of 25 kDa. It had an optimal activity at pH 5 and 50 °C. It was stable in a wide range of pH and in the presence of some detergents and organic solvents. In the presence of 3 mM Cu2+, the relative activity of the His-tagged r-XAn11 was enhanced by 54%. This is the first work reporting that copper is a strong activator for xylanase activity making this enzyme very attractive for future industrial applications. Molecular modeling suggests that the contact region between the catalytic site and the N-terminal His-tag fusion peptide could be responsible for the different behavior of the native and recombinant enzyme toward copper.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 74, March 2015, Pages 263-270
Journal: International Journal of Biological Macromolecules - Volume 74, March 2015, Pages 263-270
نویسندگان
Fatma Elgharbi, Hajer Ben Hlima, Ameny Farhat-Khemakhem, Dorra Ayadi-Zouari, Samir Bejar, Aïda Hmida-Sayari,