کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8327763 | 1540203 | 2018 | 36 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
An antioxidant rich novel β-amylase from peanuts (Arachis hypogaea): Its purification, biochemical characterization and potential applications
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
β-Amylase from un-germinated seeds of peanut (Arachis hypogaea) was purified to apparent electrophoretic homogeneity with final purification fold of 205 and specific activity of 361 μmol/min/mg protein. The enzyme was purified employing simple purification techniques for biochemical characterization. The purified enzyme was identified as β-amylase with Mr of 31 kDa. The enzyme displayed its optimum catalytic activity at pH 5.0 and 60 °C with activation energy of 4.5 kcal/mol and Q10 1.2. The enzyme displayed Km and Vmax values, for soluble potato starch of 1.28 mg/mL and 363.63 μmol/min/mg, respectively. Thermal inactivation of β-amylase at 65 °C resulted into first-order kinetics with rate constant 0.0126 minâ 1 and t½ 55 min. The enzyme was observed to act on native granular potato starch, which could minimize the high cost occurring from solubilization of starch in industries. Enzyme fractions scavenge 2, 2-diphenyl-1-picrylhydrazyl (DPPH) free radical, indicating its antioxidative nature. In addition, the purified β-amylase was successfully utilized for the improvement of antioxidant potential of wheat. These findings suggest that β-amylase from peanuts have potential application in food and pharmaceutical industries.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 111, May 2018, Pages 148-157
Journal: International Journal of Biological Macromolecules - Volume 111, May 2018, Pages 148-157
نویسندگان
Ranjana Das, Arvind M. Kayastha,