کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
36089 | 45120 | 2006 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Glycosidation of trypsin with end-group activated dextran
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A monoaminated dextran derivative was attached to trypsin via a carbodiimide-catalyzed reaction. The modified enzyme contained 3 mol of polysaccharide per mol of protein, and retained about 93% and 85% of the native esterolytic and proteolytic activity, respectively. The thermostability was enhanced from 49.7 to 67.4 °C for modified trypsin. The activation free energy of thermal inactivation at 55 °C was increased by 7.2 kJ/mol for the protease after modification with the polymer. The improved conformational stability of trypsin after glycosidation with dextran was confirmed by fluorescence spectroscopy. The glycosidated protease retained 70% of its initial activity after 3 h incubation at pH 9.0.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Process Biochemistry - Volume 41, Issue 5, May 2006, Pages 1155–1159
Journal: Process Biochemistry - Volume 41, Issue 5, May 2006, Pages 1155–1159
نویسندگان
Karel Hernández, Leyden Fernández, Leissy Gómez, Reynaldo Villalonga,