کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
36689 | 45142 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Stabilization of α-chymotrypsin by chemical modification with monoamine cyclodextrin
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Bovine pancreatic α-chymotrypsin was chemically modified with mono-6-amino-6-deoxy-β-cyclodextrin. The modified enzymes contained about 2 mol of oligosaccharide per mol of protein and retained full proteolytic and esterasic activity. The optimum temperature for α-chymotrypsin was increased by 5 °C and its thermostability was enhanced by about 6 °C after modification. The glycosylated enzyme turned markedly more resistant to thermal inactivation at 50 °C and retained 70% of the original activity when pre-incubated at pH 9.0 for 180 min as compared to a complete inactivation seed for the unmodified protease.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Process Biochemistry - Volume 40, Issue 6, May 2005, Pages 2091–2094
Journal: Process Biochemistry - Volume 40, Issue 6, May 2005, Pages 2091–2094
نویسندگان
Michael Fernández, Alex Fragoso, Roberto Cao, Reynaldo Villalonga,