کد مقاله کد نشریه سال انتشار مقاله انگلیسی ترجمه فارسی نسخه تمام متن
20109 43158 2016 6 صفحه PDF ندارد دانلود رایگان
عنوان انگلیسی مقاله
Purification and characterization of a thermophilic 1,3-1,4-β-glucanase from Bacillus methylotrophicus S2 isolated from booklice
ترجمه فارسی عنوان
خالص سازی و خصوصی سازی یک ترموفیلیک 1،3-1،4-β-گلوکاناز از Bacillus methylotrophicus S2 جدا شده از کتابچه
کلمات کلیدی
Booklice؛ Bacillus methylotrophicus S2؛ 1،3-1،4-β-گلوکاناز؛ pH پایدار؛ ترموفیل
Booklice; Bacillus methylotrophicus S2; 1,3-1,4-β-Glucanase; pH stable; Thermophilic
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
چکیده انگلیسی

An extracellular 1,3-1,4-β-glucanase-producing strain S2 was isolated from booklice and identified as Bacillus methylotrophicus. Furthermore, a homogeneous extracellular 1,3-1,4-β-glucanase GCS2 was purified by ammonium sulfate precipitation and cation-exchange chromatography. The gene for the 1,3-1,4-β-glucanase was cloned, and the nucleotide sequence was determined. Characterization of the purified enzyme revealed the molecular mass of 26 kDa and the optimum activity at pH 7.5, 55°C. The purified enzyme can highly hydrolyze carboxymethylcellulose including oat gum, barley β-glucan, CMC and lichenan, while low activity on avicel, cellobiose, filter paper, p-nitrophenyl β-d-cellobioside, and p-nitrophenyl β-d-glucoside, but no activity against microcrystalline cellulose or salicin. The enzyme was stable at wide range of pHs 5–10 and still maintained above 60% activity at 70°C. The enzyme activity was stimulated by Trixon X-100. The property of the enzyme GCS2 makes this enzyme a broad prospect in brewing and commercial detergent industry. To our knowledge, this is the first report of a 1,3-1,4-β-glucanase from microbes associated with booklice.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Bioscience and Bioengineering - Volume 121, Issue 5, May 2016, Pages 503–508
نویسندگان
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