کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10233125 | 42685 | 2010 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Isolation and characterization of a β-glucosidase from Penicillium decumbens and improving hydrolysis of corncob residue by using it as cellulase supplementation
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
A β-glucosidase from Penicillium decumbens was purified and characterized. The enzyme presented as a single band of 120 kDa on SDS-PAGE, showed optimal temperature of 65-70 °C and optimal pH of 4.5-5.0. The β-glucosidase showed relatively higher affinity to pNPG and the highest affinity to salicin with the Km value as 0.0064 and 0.0188 mM, respectively. The gene coding for it was obtained with an ORF of 2586 bp coding for 861 amino acids belonging to glycoside hydrolases family 3. The purified enzyme could improve the saccharifying ability of cellulose when it was added to the cellulase systems of Trichoderma reesei QM 9414. The several properties of it, including its pH and temperature optima, the high affinity to substrates and high specific activity, make it has great potential to be utilized as supplementation in conversion of corncob residue and other lignocellulosic biomass into simple sugars.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 46, Issue 6, 5 May 2010, Pages 444-449
Journal: Enzyme and Microbial Technology - Volume 46, Issue 6, 5 May 2010, Pages 444-449
نویسندگان
Mei Chen, Yuqi Qin, Ziyong Liu, Kai Liu, Fengshan Wang, Yinbo Qu,