• immobilized invertase studies on glass–ceramic support from coal fly ashes

    جزئیات بیشتر مقاله
    • تاریخ ارائه: 1392/01/01
    • تاریخ انتشار در تی پی بین: 1392/01/01
    • تعداد بازدید: 432
    • تعداد پرسش و پاسخ ها: 0
    • شماره تماس دبیرخانه رویداد: -
     invertase was covalently immobilized on new coal fly ashes glass-ceramic support with zinc sulfate (gcszn). the coupling process of proteins was demonstrated by x-ray diffraction (xrd). there was no change in the optimum ph (4.6) but optimum temperature increased from 55 °c for free invertase to 60 °c for immobilized derivative. the activation energy decreased after immobilization (37.31 ± 3.40 kj/mol) in spite of free invertase (51.34 ± 5.21 kj/mol). there was an improvement in the michaelis–menten constant for sucrose hydrolysis after immobilization being 15 times lower compared to that for free invertase (0.30 ± 0.01 mmol). after ten reuses at 25 ± 2 °c, the immobilized invertase lost only 9% of initial activity, but at the optimum temperature (60 °c), the activity decrease was about 70%, what it is economically feasible under energetic view point for industrial application.

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