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In vitro and in vivo degradation of myo-inositol hexakisphosphate by a phytase from Citrobacter braakii

Pontoppidan, K. (author)
Novozymes A/S
Glitsoe, V. (author)
Novozymes A/S
Guggenbuhl, P. (author)
DSM Nutritional Products Ltd
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Quintana, A. P. (author)
Nunes, C. S. (author)
DSM Nutritional Products Ltd
Pettersson, Dan (author)
Novozymes A/S
Sandberg, Ann-Sofie, 1951 (author)
Chalmers tekniska högskola,Chalmers University of Technology
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 (creator_code:org_t)
2012
2012
English.
In: Archives of Animal Nutrition. - 1477-2817 .- 1745-039X. ; 66:6, s. 431-444
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Phytases (EC 3.1.3) are widely used in animal feed to increase the availability of phosphorus and decrease the anti nutritive effect of myo-inositol hexakisphosphate (InsP(6)). The aim of this work was to investigate the stereospecific degradation of InsP(6) in vitro and in vivo by a phytase from Citrobacter braakii (C. braakii), and to study gastric survival of the phytase as well as the site of action in the gastrointestinal tract. The in vitro results showed that the C. braakii phytase belongs to the group of 6-phytases (EC 3.1.3.26). However, in approximately one out of 10 instances the phytase initiated hydrolysis at the D-3 (L-1) position, demonstrating that phytase specificity is not unambiguous. Following the main degradation pathway, InsP(6) was degraded by stepwise removal of the phosphate groups on positions 6/1/5. The stereospecificity was found to be similar under in vitro and in vivo conditions. The phytase was found to be stable in the gastric environment and to be active in the stomach and possibly also in the proximal small intestine. While InsP(4) was accumulated under in vitro conditions this was not the case in vivo, where both InsP(5) and InsP(4) were seen to be hydrolysed in the small intestine, possibly as a combined action of the C. braakii phytase and endogenous phosphatases present in the mucosa. The ability of the C. braakii phytase to focus its activity on degrading InsP(6) to InsP(4) is believed to be a favourable complement to the endogenous phosphatases.

Subject headings

NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)
NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

Keyword

pigs
phytase
stereospecificity
peniophora-lycii
in vivo
isomers
phytate
ion chromatography
performance
in vitro
inositol phosphates
inositol phosphates
dephosphorylation
degrading enzyme
pigs
Citrobacter braakii
gastric ph
degradation

Publication and Content Type

art (subject category)
ref (subject category)

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