Neeraja, Chilukoti ; Moerschbacher, Bruno ; Podile, Appa Rao (2010) Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacilluslicheniformis DSM13 Bioresource Technology, 101 (10). pp. 3635-3641. ISSN 0960-8524
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/j.biortech.2009.12.118
Abstract
Chitinase from Bacilluslicheniformis 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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Bacillus licheniformis; Cellulose Binding Domain; Chitinase; CD Analysis |
| ID Code: | 103857 |
| Deposited On: | 09 Mar 2018 11:09 |
| Last Modified: | 09 Mar 2018 11:09 |
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