کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
683287 | 888998 | 2010 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
تکنولوژی و شیمی فرآیندی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13 Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13](/preview/png/683287.png)
چکیده انگلیسی
Chitinase from Bacillus licheniformis DSM13 consists of an N-terminal catalytic domain (GH) and a C-terminal chitin binding domain (ChBD). A deletion mutant BliGH and a hybrid chitinase BliGH-CeBD were developed using polymerase chain reaction (PCR) to study the role of substrate-binding domain. Both recombinant chitinases retained their ability to bind to glycol-chitin (GC). BliGH was more effective on colloidal chitin (CC) than BliGH-CeBD as evident from the increased Vmax and kcat values. The fusion of CeBD improved the affinity to colloidal chitin, activity and conformational stability in BliGH-CeBD when compared with deletion mutant BliGH.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioresource Technology - Volume 101, Issue 10, May 2010, Pages 3635-3641
Journal: Bioresource Technology - Volume 101, Issue 10, May 2010, Pages 3635-3641
نویسندگان
Chilukoti Neeraja, Bruno Moerschbacher, Appa Rao Podile,