Effect of several germination conditions on total P, phytate P, phytase, and acid phosphatase activities and inositol phosphate esters in rye and barley

Two assays were conducted to study the evolution of rye and barley phosphatases (phytase and acid phosphatase) and the degradation of its substrates (inositol phosphate esters) during seed germination. In this manner we could obtain a low-phytate, endogenous phosphatase rich ingredient to be used in animal nutrition. In the first assay, the seeds were soaked for 1 and 14 h and germinated for 3 and 5 days with and without the addition of gibberellic acid (GA3). In the second assay, the seeds were soaked for 1 h and germinated for 1, 3, and 5 days with GA3. Phytase (up to 5739 and 3151 U kg-1) and acid phosphatase (up to 18288 and 3151 U g-1) activities, and IP6 (6.09 and 6.01 mg g-1), IP5 (0.48 and 0.48 mg g-1), and IP4 (0.13 and 0.06 mg g-1) were detected in ungerminated rye and barley, respectively. The germination process caused a significant increase of Phy and AcPh activities in rye (up to 112 and 213%) and barley (up to 212 and 634%) and a reduction in the phytate phosphorus content (up to 84 and 58%, respectively). Phytate phosphorus content was affected only by soaking time in the case of rye. Finally, during the course of germination, IP6 and IP5 were rapidly degraded in rye (88 and 79%) and barley (67 and 52%), and IP4 was only a short-living intermediate, which was increased during hydrolysis and degraded to IP3. In conclusion, a marked increase of Phy and AcPh activities in rye and barley with a concomitant decrease in phytate phosphorus content and an increase in the content of lower inositol phosphates were observed during the rye and barley germination.

Bibliographic Details

Main Authors:	Centeno, C., Viveros, A., Brenes, A., Canales, R., Lozano, A., De La Cuadra, C.
Format:	artículo biblioteca
Language:	English
Published:	American Chemical Society 2001
Subjects:	Rye, Barley, Germination, Gibberellic acid, Phosphorus, Inositol phosphates, Phytase and acid phosphatase activities,
Online Access:	http://hdl.handle.net/20.500.12792/5836 http://hdl.handle.net/10261/291985
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