Hydrolysis of phytic acid by intrinsic plant and supplemented microbial phytase (Aspergillus niger) in the stomach and small intestine of minipigs fitted with re-entrant cannulas 2. Phytase activity

2001 ◽  
Vol 85 (11-12) ◽  
pp. 414-419 ◽  
Author(s):  
C. Rapp ◽  
H.-J. Lantzsch ◽  
W. Drochner
2005 ◽  
Vol 58 (5) ◽  
pp. 267-272 ◽  
Author(s):  
Akiko Matsuo ◽  
Kenji Sato ◽  
Yasushi Nakamura ◽  
Kozo Ohtsuki

1994 ◽  
Vol 77 (3) ◽  
pp. 760-764 ◽  
Author(s):  
Adrianus J Engelen ◽  
Fred C Van Der Heeft ◽  
Peter H G Randsdorp ◽  
Ed L C Smtt

Abstract A simple and rapid method is described for determining the enzymatic activity of microbial phytase. The method is based on the determination of inorganic orthophosphate released on hydrolysis of sodium phytate at pH 5.5.


2015 ◽  
Vol 12 (13) ◽  
pp. 4175-4184 ◽  
Author(s):  
C. von Sperber ◽  
F. Tamburini ◽  
B. Brunner ◽  
S. M. Bernasconi ◽  
E. Frossard

Abstract. Phosphorus (P) is an essential nutrient for living organisms. Under P-limiting conditions plants and microorganisms can exude extracellular phosphatases that release inorganic phosphate (Pi) from organic phosphorus compounds (Porg). Phytic acid (myo-inositol hexakisphosphate, IP6) is an important form of Porg in many soils. The enzymatic hydrolysis of IP6 by phytase yields available Pi and less phosphorylated inositol derivates as products. The hydrolysis of organic P compounds by phosphatases leaves an isotopic imprint on the oxygen isotope composition (δ18O) of released Pi, which might be used to trace P in the environment. This study aims at determining the effect of phytase on the oxygen isotope composition of released Pi. For this purpose, enzymatic assays with histidine acid phytases from wheat and Aspergillus niger were prepared using IP6, adenosine 5'-monophosphate (AMP) and glycerophosphate (GPO4) as substrates. For a comparison to the δ18O of Pi released by other extracellular enzymes, enzymatic assays with acid phosphatases from potato and wheat germ with IP6 as a substrate were prepared. During the hydrolysis of IP6 by phytase, four of the six Pi were released, and one oxygen atom from water was incorporated into each Pi. This incorporation of oxygen from water into Pi was subject to an apparent inverse isotopic fractionation (ϵ ~ 6 to 10 ‰), which was similar to that imparted by acid phosphatase from potato during the hydrolysis of IP6 (ϵ ~ 7 ‰), where less than three Pi were released. The incorporation of oxygen from water into Pi during the hydrolysis of AMP and GPO4 by phytase yielded a normal isotopic fractionation (ϵ ~ −12 ‰), similar to values reported for acid phosphatases from potato and wheat germ. We attribute this similarity in ϵ to the same amino acid sequence motif (RHGXRXP) at the active site of these enzymes, which leads to similar reaction mechanisms. We suggest that the striking substrate dependency of the isotopic fractionation could be attributed to a difference in the δ18O values of the C–O–P bridging and non-bridging oxygen atoms in organic phosphate compounds.


2000 ◽  
Vol 130 (8) ◽  
pp. 2020-2025 ◽  
Author(s):  
Hubert W. Lopez ◽  
Franck Vallery ◽  
Marie-Anne Levrat-Verny ◽  
Charles Coudray ◽  
Christian Demigné ◽  
...  

2007 ◽  
Vol 2007 ◽  
pp. 28-28
Author(s):  
A.A. Sadeghi ◽  
P. Shawrang ◽  
K. Karimi

Because digesta vary in pH in different gastrointestinal segments of poultry, exogenous phytase or xylanase may exhibit differences in activity along the gastrointestinal tract. Previous reports indicated that the stomach is the major site of exogenous microbial phytase activity, with no further activity found in the small intestine of piglets. Information regarding exogenous phytase or xylanase activity in the gastrointestinal tract of poultry is largely unavailable. Because exogenous phytase or xylanase activity in the digesta is extremely low, normal phytase or xylanase activity measurements are prone to errors resulting from background interference contributed by the exogenous inorganic phosphate or xylose in the digesta (Walsh et al., 1995). The aim of this study was to utilize electrophoresis activity stain to detect the activity of phytase or xylanase in different gastrointestinal segments of broiler chickens fed diets containing exogenous enzymes.


2003 ◽  
Vol 89 (3) ◽  
pp. 287-294 ◽  
Author(s):  
M. Marounek ◽  
D. Dušková ◽  
V. Skřivanová

Twenty weaned rabbits were fed ad libitum two granulated feeds containing lucerne meal, barley, oats, wheat bran, oilseed meals and sugarbeet pulp in different proportions. Phytate P in these feeds represented 28·6 and 29·3 % of the total P. Digestibility trials were carried out in rabbits 7 and 10 weeks old. Digestibility of phytate P was 82·1 %, on average. Apparent digestibility of total P was 48·1 and 35·5 % in rabbits aged 7 and 10 weeks, respectively. Concentration of P in the faecal DM of these rabbits averaged 11·9 and 14·7 m/. Most of the faecal P was phosphates P (68·1 %). Proportion of phytate P in total faecal P was 9·0 %. Age effect on total P digestibility and faecal P concentration was significant (P<0·05). In five in vitro experiments twenty-four rabbits were killed at the age of 11 weeks, digesta samples diluted with physiological saline containing phytic acid and incubated anaerobically. Calculations of phytase activity in segments of the digestive tract were based on the estimation of phytic acid hydrolysed during the first 2 h of incubation. The caecum contained 58·6 % of the phytase activity of the digestive tract. Corresponding relative values for the phytase activity in the stomach, small intestine and colon were 22·3, 7·7 and 11·4 %, respectively. In incubations of the caecal contents, phytic acid was hydrolysed more rapidly at pH 5–6 than in the neutral pH region. The hydrolysis was inhibited by Ca cations, and to a small extent also by phosphate anions. Commercial fungal phytase (Natuphos®) was highly active in incubations of the contents of the stomach at pH 1·9. It can be concluded that phytic acid is hydrolysed quite efficiently in the digestive tract of rabbits. This hydrolysis occurred mainly in the caecum. Absorption of soluble inorganic phosphates in the gut is incomplete.


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