Heteroexpression and functional characterization of glucose 6-phosphate dehydrogenase from industrial Aspergillus oryzae

Molecular Cloning and Exploration of the Biochemical and Functional Analysis of Recombinant Glucose-6-Phosphate Dehydrogenase from Gluconoacetobacter diazotrophicus PAL5

“…Furthermore, we observed that the G6PD enzyme loses about 60% of its activity when incubated at temperatures below 30 °C. The stability of the G6PD enzyme from GDI is in agreement with that previously reported for G6PDs from A. Orizae and Homo sapiens [33,35,36], as it has been observed that these enzymes have no alteration in their enzymatic activity from 35 to 50 °C. However, the G6PD enzymes from B. malayi and Y. lipolytica [25,37] lost 100% of their activity at 50 °C, while the G6PD of GDI showed 100% activity at this temperature, which indicates that this protein is more stable under high temperatures.…”

“…Furthermore, this result agrees with those previously reported, where the enzyme had a similar pH profile compared with the other previously purified G6PDs. For example, pH values of around 7.5 to 8 were found in G6PDs from Homo sapiens , P. aeruginosa , B. malayi , buffalo liver, camel liver, dog liver, T. crassiceps , T. cruzy , T. maritima , E. coli DH5α, and A. Oryzae [20,21,22,24,25,28,29,30,31,32,33]. However, an optimal pH value of around 9 has also been reported for G6PDs from A. niger and A. midulms [34].…”

“…These results are similar to those reported for G6PDs from different organisms, where the K m values for NADP + ranged from 6 to 10 μM [21,29,36], but the K m for G6PD is lower than previously reported values (Table 1) [20,21,34]. In addition, as can be observed in Table 1, the G6PD protein has a higher catalytic constant (k cat ) value (293,181 s −1 ) compared to that of human G6PD (233 s −1 ), P. aeruginosa (540 s −1 ), A. orizae (1000 s −1 ), and T. maritima (35,000 s −1 ) [20,21,33].…”