Phytate dephosphorylation by Lactobacillus pentosus CFR3.

Studies on phytate-degrading enzymes from lactobacilli are scarce, despite its potential in improving the
nutritional quality of plant-based foods. Therefore, the current investigation deals with the phytatedegrading
enzyme produced by a native Lactobacillus pentosus strain. Phytase activity was highest towards
the end of the exponential phase. Activity increased in the presence of maltose (381.1%) compared with
glucose. The presence of phytate in the media stimulated the enzyme production. The enzyme of interest
was a 70 kDa protein with a pH and temperature optima of 5.0 and 55–60 °C, respectively. It retained
46% of activity after exposure to 70 °C for 20 min and also showed broad substrate specificity. It was
completely inhibited by Hg2+, Fe2+ and PMSF while being activated by Co2+. This report is the first to
show dephytinisation of autoclaved finger millet flour either by fermentation with L. pentosus or by treatment
with the corresponding cell-free extract.