کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | ترجمه فارسی | نسخه تمام متن |
---|---|---|---|---|---|
9749238 | 1493804 | 2005 | 5 صفحه PDF | سفارش دهید | دانلود رایگان |
عنوان انگلیسی مقاله ISI
One-step purification of α-amylase from the cultivation supernatant of recombinant Bacillus subtilis by high-speed counter-current chromatography with aqueous polymer two-phase systems
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Purification of α-amylase from the cultivation supernatant of recombinant Bacillus subtilis by high-speed counter-current chromatography (HSCCC) in polyethylene glycol (PEG) 4000-inorganic salt aqueous polymer two-phase systems was studied. The effects of sodium chloride concentration on the partition coefficients of α-amylase and total protein were respectively tested in PEG4000-phosphate and PEG4000-citrate aqueous polymer two-phase systems to find the proper range of sodium chloride concentration for the HSCCC purification of α-amylase. α-Amylase was purified from the cultivation supernatant by HSCCC in PEG4000-phosphate system containing 2% (w/w) sodium chloride, yet with considerable loss of activity. PEG4000-citrate aqueous polymer two-phase system containing 2% (w/w) sodium chloride and supplemented with 0.56% (w/w) CaCl2 as protective agent was then successfully applied to purify α-amylase from cultivation supernatant by HSCCC to homogeneity and significantly increased the recovery of α-amylase activity from around 30 to 73.1%.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Chromatography A - Volume 1070, Issues 1â2, 8 April 2005, Pages 215-219
Journal: Journal of Chromatography A - Volume 1070, Issues 1â2, 8 April 2005, Pages 215-219
نویسندگان
Wenbo Zhi, Qiuyun Deng, Jiangnan Song, Ming Gu, Fan Ouyang,
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