کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9602418 | 1156 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Directed evolution for engineering pH profile of endoglucanase III from Trichoderma reesei
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
The potential of cellulase has been revealed not only in biomass conversion but also in various industrial processes, including food, textiles, laundry, pulp, and paper. Due to the need for alkali-tolerant cellulase with high specific activity at alkaline pH, for example, for application in detergent industry an error-prone PCR approach was employed for enhancing the alkali-tolerant ability of endoglucanase III (EG III) from Trichoderma reesei by error-prone PCR. One mutant (N321T) which exhibited an optimal activity at pH 5.4, corresponded to a basic shift of 0.6 pH unit compared to the wild-type enzyme, was selected and characterized. In addition, two site-directed mutations, N321D and N321H, were designed to study the role of residue at position 321. As expected, the N321D mutation changed enzyme's optimal activity to pH 4.0, resulting in a large decrease in the specific activity. However, the N321H mutated enzyme was active over a broader pH range compared to the wild type, with no much change in the specific activity. These properties suggest that the residue at position 321 is important amino acid residue in determining the pH activity profile of the EG III from T. reesei.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biomolecular Engineering - Volume 22, Issues 1â3, June 2005, Pages 89-94
Journal: Biomolecular Engineering - Volume 22, Issues 1â3, June 2005, Pages 89-94
نویسندگان
Ting Wang, Xiangmei Liu, Qian Yu, Xi Zhang, Yinbo Qu, Peiji Gao, Tianhong Wang,