. 2009 Dec 1;40(4):795–807. doi: 10.1590/S1517-838220090004000010

Table 3.

Kinetic constants for enzymatic myo-inositol pentakisphosphate déphosphorylation

phytase	InsP5 generated by
phytase	kinetic constant	Aspergillus niger phytase	Pantoea agglomerans phytase
Aspergillus niger	K_M [μmol l^-1]	156 ± 12^a	159 ± 12^a
	k_cat [s^-1]	140 ± 12^a	136 ± 7^a
Pantoea agglomerans	K_M [μmol l^-1]	154 ± 5^a	155 ± 10^a
	k_cat [s^-1]	141 ± 11^a	139 ± 9^a

Temperature: 37°C; buffer: 100 mM sodium acetate, pH 5.0; enzyme concentration: 25 mU ml^-1. For calculation of k_cat the following molecular masses were used: Aspergillus niger, 85 kDa, Pantoea agglomerans, 42 kDa (9). The data are mean values of five independent experiments.

means within the same line with the same superscripts are not significantly different (P < 0.05)