EC Number |
Protein Variants |
Reference |
---|
3.2.1.B1 | L122Q |
mutant enzyme shows similar thermostability with wild-type AgaB. Specific activity 1.3fold higher than that of wild-type enzyme |
695671 |
3.2.1.B1 | more |
to increase the thermostability of beta-agarase AgaB by directed evolution, the mutant gene libraries are generated by error-prone polymerase chain reaction and deoxyribonucleic acid shuffling. A mutant S2 is obtained through two rounds of error-prone polymerase chain reaction and a single round of DNA shuffling and selection. It has higher thermostability and slightly increased catalytic activity than wild-type AgaB. Melting temperature (Tm) of S2, as determined by circular dichroism, is 4.6°C higher than that of wild-type AgaB, and the half-life of S2 is 350 min at 40°C, which is 18.4-fold longer than that of the wild-type enzyme. Saturation mutagenesis and hydrophobic cluster analysis indicate that hydrophobic interaction might be the key factor that enhances the enzyme stability |
695671 |
3.2.1.B1 | N446I |
mutant enzyme has enhanced thermostability. 10-20% decrease of the specific activity compared to wild-type enzyme |
695671 |
3.2.1.B1 | N446L |
half-life of mutant enzyme at 40°C is 12.9fold longer than that of wild-type AgaB |
695671 |
3.2.1.B1 | N446V |
half-life of mutant enzyme at 40°C is 18.2fold longer than that of wild-type AgaB |
695671 |