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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]