کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10233238 | 42737 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
One step purification and characterization of an extracellular α-amylase from marine Vibrio sp.
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موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: One step purification and characterization of an extracellular α-amylase from marine Vibrio sp. One step purification and characterization of an extracellular α-amylase from marine Vibrio sp.](/preview/png/10233238.png)
چکیده انگلیسی
An α-amylase was purified from marine Vibrio sp. using starch affinity method with molecular mass of 52.480 kDa. This amylase showed maximum activity at 55-60 °C and pH 6.5 and retain 85% of maximal activity after 30 min preincubation at 65 °C. The enzyme was inhibited by ethylenediaminetetra-acetate (EDTA) and [ethylenebis(oxonitrilo)]tetra-acetate (EGTA) while divalent metal ions, such as Fe2+, Mn2+, Co2+, Ca2+, Mg2 and Cu2+ could restored near 25-55% of maximal activity suggesting that the metal ions need for the enzyme activity. Digestion of corn-starch by the enzyme showed random cleavage with various sizes of products, indicating endo action of the enzyme. Chemical modification suggested involvement of Lys, Trp, Asp/Glu and His in the enzyme activity. The starch affinity method used here showed high yield purified amylase with very low experimental cost.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 36, Issue 4, 2 March 2005, Pages 535-539
Journal: Enzyme and Microbial Technology - Volume 36, Issue 4, 2 March 2005, Pages 535-539
نویسندگان
Mohsen Fathi Najafi, Asha Kembhavi,