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
| dc.contributor.author | Neeraja, Chilukoti | |
| dc.contributor.author | Moerschbacher, Bruno | |
| dc.contributor.author | Podile, Appa Rao | |
| dc.date.accessioned | 2022-03-27T03:51:58Z | |
| dc.date.available | 2022-03-27T03:51:58Z | |
| dc.date.issued | 2010-05-01 | |
| dc.description.abstract | 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. © 2009 Elsevier Ltd. All rights reserved. | |
| dc.identifier.citation | Bioresource Technology. v.101(10) | |
| dc.identifier.issn | 09608524 | |
| dc.identifier.uri | 10.1016/j.biortech.2009.12.118 | |
| dc.identifier.uri | https://www.sciencedirect.com/science/article/abs/pii/S0960852409018161 | |
| dc.identifier.uri | https://dspace.uohyd.ac.in/handle/1/5809 | |
| dc.subject | Bacillus licheniformis | |
| dc.subject | CD analysis | |
| dc.subject | Cellulose binding domain | |
| dc.subject | Chitinase | |
| dc.title | Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13 | |
| dc.type | Journal. Article | |
| dspace.entity.type |
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