Table 1 Mutations reported in the literature for improving the activity, glucose tolerance, and stability of β-glucosidases
From: Glutantβase: a database for improving the rational design of glucose-tolerant β-glucosidases
# | Mutation | Effect | Source |
|---|---|---|---|
1 | H228T | Responsible for attracting glucose to the middle of the substrate channel and, then, to the exit, which improves the resistance to product inhibition. | [9] |
2 | V174C | Mutations were described to increase the optimal temperature from 50 ° C to 60°, reduce the optimal pH from 6 to 5.5, and increases the half-life from 1 to 2-20 h. | [12] |
3 | A404V | ||
4 | L441F | ||
5 | H184F | This mutation has been reported as responsible for promoting an increase in the inhibition constant for glucose. | [27] |
6 | E96K | Described as responsible for improving the protein thermostability. | [47] |