کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
641302 | 1456999 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The use of papain inhibitor immobilized onto polyaniline for bioaffinity chromatography of cysteine proteases
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
تصفیه و جداسازی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
In this work, a papain inhibitor extracted from seeds of Adenanthera pavonina was covalently immobilized onto glutaraldehyde modified polyaniline (PANIG). The immobilization was very efficient, presenting 54.24% inhibitor retention in the following conditions: immobilization time of 30 min, at 4 °C, pH 7.0, inhibitor concentration of 20 mg and 5 mg of PANIG. The resultant material (PANIG-I) was tested as stationary phase for the cysteine proteases papain, ficin and bromelain purification through bioaffinity chromatography. A commercial preparation of papain was efficiently purified, resulting in a single band with 25 kDa. SDS-PAGE of purified bromelain showed a characteristic band around 28 kDa and this procedure resulted in 0.89-fold purification and 32.4% yield. The purification process was more effective for ficin reaching 2.6-fold purification and a single band of 25 kDa in the SDS-PAGE. These results showed that the stationary phase containing A. pavonina inhibitors immobilized onto PANIG is a very promising material for a single step purification of cysteine proteases through bioaffinity chromatography.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Separation and Purification Technology - Volume 120, 13 December 2013, Pages 467-472
Journal: Separation and Purification Technology - Volume 120, 13 December 2013, Pages 467-472
نویسندگان
Adriane G. Gamboa, Karla A. Batista, Flavio M. Lopes, Kátia F. Fernandes,