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Preparations of 6-phytase A (EC 3.1.3.26) and phytase B (acid phosphatase, EC 3.1.3.2) were applied alone and combined in the preparation of dough to estimate their catalytic potential for myo- inositol liberation from rye flour in the breadmaking technology. The experimental bread samples were ground after baking and subjected to determination of myo- inositol bioavailability by an in vitro method that simulated digestion in a human alimentary tract, followed by measurements of myo- inositol transport through enterocyte- -like differentiated Caco-2 cells to determine its bioaccessibility. Myo- inositol content was measured by a high-performance anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD) technique. The concentration of myo- inositol in the dialysates of control bread was 25.3 µg/mL, whereas in the dialysates of bread sample baked with 6-phytase A, the concentration increased to 35.4 µg/mL, and in the bread baked with phytase B to 64.98 µg/mL. Simultaneous application of both enzymes resulted in myo- inositol release of 64.04 µg/mL. The highest bioaccessibility of myo- inositol, assessed by the measurement of the passage through the Caco-2 monolayer was determined in the bread baked with the addition of 6-phytase A. Enzymatically modified rye bread, particularly by the addition of 6-phytase A, may be therefore a rich source of a highly bioaccessible myo - -inositol.

Phytases Improve Myo-Inositol Bioaccessibility in Rye Bread: A Study Using an In Vitro Method of Digestion and a Caco-2 Cell Culture Model