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. 2006 Jun;72(6):4397–4403. doi: 10.1128/AEM.02612-05

TABLE 2.

Comparison of kinetics of the WT and E228K mutant PhyA phytasesa

pH Phytase Km (μM) Vmax (μmol m−1 mg−1) kcat (m−1) kcat/Km (m−1 μM−1)
5.5 WT 177.3 ± 22.4 94.7 ± 5.4 7,385.3 ± 421.1 41.64
E228K 38.6 ± 13.2* 34.5 ± 3.9* 2,690.2 ± 304.1* 69.71*
3.5 WT 321.9 ± 37.9 33.8 ± 5.4 2,638.4 ± 421.1 8.20
E228K 227.8 ± 18.5* 62.1 ± 3.9* 4,844.3 ± 304.1* 21.27*
a

Enzymatic reactions (n = 3) were conducted at 37°C in 0.2 M glycine-HCl buffer for pH 3.5 and in 0.2 M citrate buffer for pH 5.5 using various sodium phytate concentrations (0.1 to 10 Km) and 100 mU phytase (purified) per ml reaction mixture. An asterisk indicates a difference (P < 0.05) from the WT.