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Related Experiment Videos

Interaction between protein, phytate, and microbial phytase. In vitro studies.

Arie K Kies1, Leon H De Jonge, Paul A Kemme

  • 1DSM Food Specialties, R&D-FTD, P.O. Box 1, 2600 MA Delft, The Netherlands. arie.kies@dsm.com

Journal of Agricultural and Food Chemistry
|March 2, 2006
PubMed
Summary

Phytase enzyme prevents protein-phytate complex formation in animal stomachs. This interaction may improve protein digestibility by aiding protein release and degradation.

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Area of Science:

  • Animal Nutrition
  • Biochemistry

Background:

  • Phytate is an anti-nutritional factor that can bind proteins and minerals.
  • Protein-phytate complexes can reduce nutrient bioavailability in animal diets.

Purpose of the Study:

  • To investigate in vitro the interaction between proteins from feedstuffs and phytate.
  • To study the formation and degradation of protein-phytate complexes under different pH conditions.
  • To evaluate the effect of pepsin and phytase on these complexes.

Main Methods:

  • Proteins were extracted from five feedstuffs and casein.
  • Complex formation was studied at various pH levels.
  • Degradation of complexes was assessed using pepsin and/or phytase.

Main Results:

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  • Minimal soluble protein-phytate complexes were observed, except possibly in rice pollards.
  • Phytate addition inhibited protein solubility at low pH.
  • Phytase prevented protein precipitation with phytate and increased protein release rate.
  • Pepsin released protein from precipitates, with phytase enhancing this process.
  • Both pepsin and phytase were required for protein release and degradation from complexes.

Conclusions:

  • Protein-phytate complexes primarily form at low pH, such as in the animal stomach.
  • Phytase can prevent complex formation and accelerate their dissolution.
  • These findings suggest phytase may enhance protein digestibility in animals.