کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10602138 | 982370 | 2011 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of 1,3-β-d-glucanase from Eisenia foetida
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
1,3-β-d-glucanase from the earthworm Eisenia foetida was purified to electrophoretically homogeneous state. The molecular weight of the purified enzyme was estimated 42,000 by SDS-PAGE. The N-terminal amino acid sequence of the enzyme was very similar to those of CCF-I from E. foetida and CCF-like protein from Aprorrectodea caliginosa. The enzyme was most active at pH 6.0 and 60 °C, and stable at pH 6.0-10.5 and 60 °C. The enzyme was inhibited by metal ions Mn2+, Cu2+, Fe2+, Al3+, and hydrolyzed 1,3-β-d-linked oligosaccharides (triose, tetraose, and pentose) into glucose, and biose as end products.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Carbohydrate Polymers - Volume 86, Issue 1, 1 August 2011, Pages 271-276
Journal: Carbohydrate Polymers - Volume 86, Issue 1, 1 August 2011, Pages 271-276
نویسندگان
Mitsuhiro Ueda, Koh Yamaki, Takahiro Goto, Masami Nakazawa, Kazutaka Miyatake, Minoru Sakaguchi, Kuniyo Inouye,