Codon Optimization Significantly Improves the Expression Level of α-Amylase Gene from Bacillus licheniformis in Pichia pastoris

Figure 6

Influence of temperature on activity and stability of recombinant BlAmy (a) and deglycosylated recombinant BlAmy (b). -Amylase activity was determined by starch-iodine color method. The optimum temperature of purified recombinant BlAmy was measured at different temperatures ranging from 40 to 100°C. The relative activity at different temperatures was calculated by setting 90°C as 100%. The thermal stability was studied by incubating lipase at various temperatures (40–100°C) in sodium phosphate buffer (pH 7.0) up to 1 h. The residual enzyme activity was measured at 70°C and the residual activity was calculated by taking the nonheated lipase activity as 100%. All measurements were carried out in triplicate.

(a)

(b)