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 phytate-degrading 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 70kDa protein with a pH and temperature optima of 5.0 and 55-60 degrees C, respectively. It retained 46% of activity after exposure to 70 degrees 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.