کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10243395 | 46933 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
کاتالیزور
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چکیده انگلیسی
Invertase was immobilised on microporous montmorillonite K-10 via adsorption and covalent binding. The immobilised enzymes were tested for sucrose hydrolysis activity in a batch reactor. Km for immobilised systems was greater than free enzyme. The immobilised forms could be reused for 15 continuous cycles without any loss in activity. After 25 cycles, 85% initial activity was retained. A study on leaching of enzymes showed that 100% enzyme was retained even after 15 cycles of reuse. Leaching increased with reaction temperature. Covalent binding resisted leaching even at temperatures of 70 °C.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Catalysis Communications - Volume 6, Issue 1, January 2005, Pages 81-86
Journal: Catalysis Communications - Volume 6, Issue 1, January 2005, Pages 81-86
نویسندگان
G. Sanjay, S. Sugunan,