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

Robert Duliński*, Emilia Katarzyna Cielecka, Małgorzata Pierzchalska and Krzysztof Żyła

Department of Food Biotechnology, Faculty of Food Technology, University of Agriculture in Krakow, ul. Balicka 122,
PL-30-149 Krakow, Poland

Article history
Received June 10, 2014
Accepted January 12, 2015

Key words:
phytic acid, myo-inositol, enzymatically modified bread, Caco-2 cells

Preparations of 6-phytase A (EC and phytase B (acid phosphatase, EC 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 modifi ed rye bread, particularly by the addition of 6-phytase A, may be therefore a rich source of a highly bioaccessible myo-inositol.

*Corresponding author: 
                                        +48 12 662 4796
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