چاپ صفحه |  صفحه نخست سامانه |  چکیده مقاله |  نویسندگان |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده ثبت کننده مقاله | حامد همیشه کار |
| مرحله جاری مقاله | تایید نهایی |
| دانشکده/مرکز مربوطه | دانشکده علوم نوین پزشکی |
| کد مقاله | 61153 |
| عنوان فارسی مقاله | Enhanced stability and catalytic activity of immobilized a-amylase on modified Fe3O4 nanoparticles for potential application in food industries |
| عنوان لاتین مقاله | Enhanced stability and catalytic activity of immobilized a-amylase on modified Fe3O4 nanoparticles for potential application in food industries |
| ناشر | 4 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ | خیر |
| عنوان نشریه (خارج از لیست فوق) | |
| نوع مقاله | Original Article |
| نحوه ایندکس شدن مقاله | ایندکس شده سطح یک – ISI - Web of Science |
| آدرس لینک مقاله/ همایش در شبکه اینترنت | https://www.scopus.com/record/display.uri?eid=2-s2.0-84942258711&origin=resultslist&sort=plf-f&src=s&st1=salehi&st2=roya&nlo=1&n |
| Enzymes play an essential role in catalyzing various reactions. However, their instability upon repetitive/prolonged use, elevated temperature, acidic or alkaline pH remains an area of concern. a-Amylase, a widely used enzyme in food industries for starch hydrolysis, was covalently immobilized on the surface of two developed matrices, amino-functionalized silica-coated magnetite nanoparticles (AFSMNPs) alone and covered with chitosan. The synthesis steps and characterizations of NPs were examined by FT-IR, VSM, and SEM. Modified nanoparticles with average diameters of 20–80 nm were obtained. Enzyme immobilization efficiencies of 89 and 74 were obtained for AFSMNPs and chitosan-coated AFSMNPs, respectively. The optimum pH obtained was 6.5 and 8.0 for the enzyme immobilized on AFSMNPs and chitosancoated AFSMNPs, respectively. Optimum temperature for the immobilized enzyme shifted toward higher temperatures. Considerable enhancements in thermal stabilities were observed for the immobilized enzyme at elevated temperatures up to 80 C. A frequent use experiment demonstrated that the immobilized enzyme retained 74 and 85 % of its original activity even after 20 times of repeated use in AFSMNPs and chitosan-coated AFSMNPs, respectively. Storage stability demonstrated that free enzyme lost its activity completely within 30 days. But, immobilized enzyme on AFSMNPs and chitosan-coated AFSMNPs preserved 65.73 and 78.63 % of its initial activity, respectively, after 80 days of incubation. In conclusion, a substantial improvement in the performance of the immobilized enzyme with reference to the free enzyme was obtained. Furthermore, the relative activities of immobilized enzyme are superior than free enzyme over the broader pH and temperature ranges. |
| نویسنده | نفر چندم مقاله |
|---|---|
| حامد همیشه کار | سوم |
| رویا صالحی قره ورن | چهارم |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| 26-Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy,2015, Rasulzadeh,cdot.pdf | 1396/05/17 | 1055597 | دانلود |
