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. 2020 Jul 11;19:140. doi: 10.1186/s12934-020-01397-y

Table 1.

Catalytic constants of α-glucosidases from M. gruessii and M. reukaufii

Substrate Sucrose Maltose
Enzyme Km (mM) kcat (s−1) kcat/Km (s−1mM−1) Km (mM) kcat (s−1) kcat/Km (s−1mM−1)
Mg-αGlu 54.1 ± 5.8 269.7 ± 10.9 4.9 ± 0.7 42.8 ± 5.6 365.6 ± 16.7 8.5 ± 1.5
Mr-αGlu 64.9 ± 4.6 477.2 ± 13.7 7.4 ± 0.7 79.8 ± 12.8 405.9 ± 28.1 5.1 ± 1.2

Reaction rates measurements were performed by triplicate. Values of kcat were calculated from Vmax considering the theoretical molecular mass of 66 kDa. Standard errors are indicated