کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10843758 1069292 2005 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20
چکیده انگلیسی
A Bacillus subtilis AX20 from soil with ability to produce extracellular α-amylases was isolated. The characterization of microorganism was performed by biochemical tests as well as 16S rDNA sequencing. Maximum amylase activity (38 U/ml) was obtained at stationery phase when the culture was grown at 37 °C. The enzyme was purified to homogeneity with an overall recovery of 24.2% and specific activity of 4133 U/mg. The native protein showed a molecular mass of 149 kDa composed of a homodimer of 78 kDa polypeptide by SDS-PAGE. The optimum pH and temperature of the amylase were 6 and 55 °C, respectively. The enzyme was inhibited by Hg2+, Ag2+, and Cu2+ and it did not show an obligate requirement of metal ions. The enzyme was not inhibited by EDTA or EGTA, suggesting that this enzyme is not a metalloenzyme. The end products of corn starch and soluble starch were glucose (70-75%) and maltose (20-25%). Rapid reduction of blue value and the end products suggest an endo mode of action for the amylase. The purified amylase shows interesting properties useful for industrial applications.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 41, Issue 2, June 2005, Pages 349-354
نویسندگان
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