| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10235551 | Process Biochemistry | 2012 | 8 Pages |
Abstract
⺠We attempted to improve CGTase thermostability by whole B domain engineering. ⺠Whole B domain was substituted and the approach has never reported before. ⺠A mutant exhibited 2.5-fold thermostability enhancement. ⺠Improvement may be cause by better structural packing and molecular interactions. ⺠Five mutants lost activity conceivably due to substrate-binding cleft distortion.
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Authors
Poh Hong Goh, Rosli Md. Illias, Kian Mau Goh,