کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9604430 | 43625 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Effects of the PT region of EngD and HLD of CbpA on solubility, catalytic activity and purification characteristics of EngD-CBDCbpA fusions from Clostridium cellulovorans
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
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چکیده انگلیسی
Chimeric proteins combining the catalytic N-terminal region of native EngD with its proline-threonine-threonine (PT) linker region, hydrophilic domain (HLD) and cellulose binding domain (CBD) of cellulose binding protein A (CbpA) from Clostridium cellulovorans were constructed, expressed, and analyzed. The chimeric proteins with CBDCbpA all demonstrated strong affinity to Avicel. The chimeric protein with the PT region of EngD and the HLD had the best catalytic activity and the highest estimated percentage of soluble protein amongst the chimeric proteins. Native EngD and two of the chimeric proteins (EngD-PT-HLD-CBD and EngD-CBD) were purified and their characteristics analyzed. Their binding affinities to Avicel as well as their enzymatic activities against various substrates were found to be consistent with the results we saw from protein lysate samples, which was good binding to Avicel but a decrease in solubility and catalytic activities in chimeric proteins without PT and/or HLD. The reasons for these are discussed. These fusion proteins may be important in applications, such as immobilization to solid cellulose substrate for purification of proteins and enrichment/aggregation of protein complexes.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Biotechnology - Volume 116, Issue 3, 30 March 2005, Pages 233-244
Journal: Journal of Biotechnology - Volume 116, Issue 3, 30 March 2005, Pages 233-244
نویسندگان
Michael Yeh, Scott Craig, May-Ghee Lum, Frances C. Foong,