Merck
  • Home
  • Search Results
  • The degradation of phytate by microbial and wheat phytases is dependent on the phytate matrix and the phytase origin.

The degradation of phytate by microbial and wheat phytases is dependent on the phytate matrix and the phytase origin.

Journal of the science of food and agriculture (2011-03-10)
Sarah M Brejnholt, Giuseppe Dionisio, Vibe Glitsoe, Lars K Skov, Henrik Brinch-Pedersen
ABSTRACT

Phytases increase utilization of phytate phosphorus in feed. Since wheat is rich in endogenous phytase activity it was examined whether wheat phytases could improve phytate degradation compared to microbial phytases. Moreover, it was investigated whether enzymatic degradation of phytate is influenced by the matrix surrounding it. Phytate degradation was defined as the decrease in the sum of InsP₆ + InsP₅. Endogenous wheat phytase effectively degraded wheat Ins₆ + InsP₅ at pH 4 and pH 5, while this was not true for a recombinant wheat phytase or phytase extracted from wheat bran. Only microbial phytases were able to degrade InsP₆ + InsP₅ in the entire pH range from 3 to 5, which is relevant for feed applications. A microbial phytase was efficient towards InsP₆ + InsP₅ in different phytate samples, whereas the ability to degrade InsP₆ + InsP₅ in the different phytate samples ranged from 12% to 70% for the recombinant wheat phytase. Wheat phytase appeared to have an interesting potential. However, the wheat phytases studied could not improve phytate degradation compared to microbial phytases. The ability to degrade phytate in different phytate samples varied greatly for some phytases, indicating that phytase efficacy may be affected by the phytate matrix.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Phytase from wheat, ≥0.01 unit/mg solid
Sigma-Aldrich
Phospholipase D from Arachis hypogaea (peanut), Type II, lyophilized powder, ≥60 units/mg protein