کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5512420 | 1540223 | 2017 | 36 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A novel alkaline surfactant-stable keratinase with superior feather-degrading potential based on library screening strategy
ترجمه فارسی عنوان
یک کراتیناز پایدار قلیایی سورفاکتانت با پتانسیل پراکنده پراکنش بر پایه استراتژی غربالگری کتابخانه
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کلمات کلیدی
کراتیناز، کتابخانه فسدم، تعیین مشخصات،
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
چکیده انگلیسی
A novel keratinase was mined and expressed in Escherichia coli BL21 (DE3) via function-driven screening with fosmid library. The catalytic properties of purified keratinase were investigated in detail following enzyme purification. The recombinant keratinase was purified to homogeneity with an estimated molecular weight of 26 kDa using nickel affinity chromatography, of which the optimal reaction pH and temperature were 10.0 and 55 °C, respectively. It could remain stable at pH 5.0-12.0 and 40-60 °C. Metal ions such as Ca2+, Mn2+, Ag+, Na+, Mg2+, Li+, Sn2+ (1 mM) displayed positive influence on keratinase, and particularly, Ca2+ exhibited remarkable improvement effect by 2.6 folds. It was strongly inhibited by PMSF as a protease inhibitor. On the contrary, it could be obviously activated by various surfactants, such as Tween 40 and Triton X-114. The recombinant keratinase showed high specificity towards casein, soluble keratin, BSA, and wool. The keratinase could efficiently degrade the feathers, which demonstrated its applicable potential for biodegradation of keratin wastes and regeneration of soluble protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 95, February 2017, Pages 404-411
Journal: International Journal of Biological Macromolecules - Volume 95, February 2017, Pages 404-411
نویسندگان
Chang Su, Jin-Song Gong, Rong-Xian Zhang, Li-Yan Tao, Wen-Fang Dou, Dan-Dan Zhang, Heng Li, Zhen-Ming Lu, Zheng-Hong Xu, Jin-Song Shi,