| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6531280 | Journal of Molecular Catalysis B: Enzymatic | 2013 | 26 Pages |
Abstract
- Structures of the native and truncated Taka amylase were compared.
- C-terminal domain is essential for the stability of the structure.
- The barrel region and the large cleft remained native in truncated enzymes.
- Binding affinity of maltoheptaose toward enzymes is more than those of maltotriose.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Mohammad Reza Housaindokht, Mohammad Reza Bozorgmehr, Hossein Eshtiagh Hosseini, Razieh Jalal, Ahmad Asoodeh, Mahin Saberi, Zeinab Haratipour, Hassan Monhemi,