scholarly journals Interactions between supplemented mineral phosphorus and phytase on phytate hydrolysis and inositol phosphates in the small intestine of broilers ,

2015 ◽  
Vol 94 (5) ◽  
pp. 1018-1029 ◽  
Author(s):  
Ellen Zeller ◽  
Margit Schollenberger ◽  
Maren Witzig ◽  
Yauheni Shastak ◽  
Imke Kühn ◽  
...  
Keyword(s):  
Small Intestine ◽  
Inositol Phosphates ◽  
Mineral Phosphorus ◽  
Phytate Hydrolysis

scholarly journals Relationship between stimulated phosphatidic acid production and inositol lipid hydrolysis in intestinal longitudinal smooth muscle from guinea pig

1987 ◽  
Vol 244 (3) ◽  
pp. 763-768 ◽  
Author(s):  
R S E Mallows ◽  
T B Bolton
Keyword(s):  
Smooth Muscle ◽  
Small Intestine ◽  
Substance P ◽  
Guinea Pig ◽  
Phosphatidic Acid ◽  
Inositol Phosphates ◽  
Muscle Layer ◽  
Phospholipid Hydrolysis ◽  
Longitudinal Smooth Muscle ◽  
Inositol Phospholipid

Accumulation of [32P]phosphatidic acid (PA) and total [3H]inositol phosphates (IPs) was measured in the longitudinal smooth-muscle layer from guinea-pig small intestine. Stimulation with carbachol, histamine and substance P produced increases in accumulation of both [3H]IPs and [32P]PA over the same concentration range. The increase in [32P]PA accumulation in response to carbachol (1 microM-0.1 mM) was inhibited in the presence of atropine (0.5 microM). Buffering the external free [Ca2+] to 10 nM did not prevent the carbachol-stimulated increase in [32P]PA accumulation. Carbachol and Ca2+ appear to act synergistically to increase accumulation of [32P]PA. In contrast, although incubation with noradrenaline also increased accumulation of [3H]IPs, no increase in accumulation of [32P]PA could be detected. These results suggest that an increase in formation of IPs is not necessarily accompanied by an increase in PA formation, and imply the existence of receptor-modulated pathways regulating PA concentrations other than by phospholipase-C-catalysed inositol phospholipid hydrolysis.

Phytate hydrolysis in pigs fed a barley-rapeseed meal diet treated with Aspergillus niger phytase or steeped with whey

1998 ◽  
Vol 78 (2) ◽  
pp. 175-180 ◽  
Author(s):  
Erika Skoglund ◽  
Matti Näsi ◽  
Ann-Sofie Sandberg
Keyword(s):  
Aspergillus Niger ◽  
High Performance ◽  
Inositol Phosphates ◽  
Rapeseed Meal ◽  
Growing Pigs ◽  
Initial Weight ◽  
Hydrolysis Products ◽  
Microbial Phytase ◽  
Phytate Hydrolysis ◽  
Aspergillus Niger Phytase

The degradation of phytate (myo-inositol hexaphosphate) in a barley-rapeseed meal (80:20) diet due to supplemented Aspergillus niger phytase and steeping (soaking at 40 °C for 3 h with feed to water ratio 1 kg:1 L) with whey was studied in eight growing pigs (initial weight 27.8 kg). Phytate and its hydrolysis products (inositol penta-, tetra- and triphosphates, abbreviated IP5, IP4 and IP3) in diets and feces were determined using ion-pair high-performance liquid chromatography (HPLC). Different isomeric forms of inositol tetra- and pentaphosphates were studied utilizing high-performance ion chromatography (HPIC). Supplementing the diet with microbial phytase resulted in a 47% reduction in the amount of fecal phytate. Whey steeping of the diet reduced fecal phytate by 35%. Further reduction of the amount of fecal phytate (64%) was demonstrated in pigs fed the diet both steeped with whey and supplemented with microbial phytase, compared with pigs fed the untreated diet. Identification of IP4 and IP5 isomers in fecal samples showed which kind of phytase enzyme was active during phytate hydrolysis in the digestive tract. From these data, it was concluded that pigs fed the basal or whey steeped diet, without supplemented microbial phytase, had higher relative fecal amounts of DL-Ins(1,2,3,4,5)P5, compared with pigs fed the microbial phytase supplemented diets. Adding microbial phytase to the diet increased the relative amount of DL-Ins(1,2,4,5,6)P5 in feces. With whey steeping of the diet, the relative amount of DL-Ins(1,2,3,4)P4 isomer in feces was increased and the relative amount of DL-Ins(1,2,5,6)P4 isomer was decreased. Key words: Inositol phosphates, steeping, Aspergillus niger phytase, pig

scholarly journals Effects of the composition of the basal diet on the evaluation of mineral phosphorus sources and interactions with phytate hydrolysis in broilers

2014 ◽  
Vol 93 (10) ◽  
pp. 2548-2559 ◽  
Author(s):  
Y. Shastak ◽  
E. Zeller ◽  
M. Witzig ◽  
M. Schollenberger ◽  
M. Rodehutscord
Keyword(s):  
Basal Diet ◽  
Mineral Phosphorus ◽  
Phosphorus Sources ◽  
Phytate Hydrolysis

scholarly journals A comparative study of phytate hydrolysis in the gastrointestinal tract of the golden hamster (Mesocricetus auratus) and the laboratory rat

1985 ◽  
Vol 54 (2) ◽  
pp. 429-435 ◽  
Author(s):  
P. J. Williams ◽  
T. G. Taylor
Keyword(s):  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Comparative Study ◽  
Large Intestine ◽  
Chromium Oxide ◽  
Golden Hamster ◽  
Solid Phase ◽  
Phytate Hydrolysis ◽  
Hydrolysis Of

1. The role of bacterial, dietary and intestinal phytases (EC 3. 1. 3. 8) in the hydrolysis of phytate was investigated in the golden hamster and rat by assaying phytase in the small intestine and by measuring the disappearance of phytate from the stomach and large intestine, using chromium oxide as an insoluble solid-phase marker.2. It was confirmed that an active phytase was present in the proximal third of the small intestine of the rat but the enzyme was undetectable in the hamster.3. Extensive bacterial breakdown of phytate occurred in the pregastric pouch and true stomach of the hamster with both phytase-containing and phytase-free diets, with phytate digestibilities in the true stomach ranging from 0.69–0.90, confirming that the hamster can be regarded as a pseudo-ruminant.4. With a phytase-free diet, the digestibility of phytate in the stomach of the rat was very low (0.05) but with a wheat-based diet substantial breakdown of phytate occurred (digestibility up to 0.49), presumably under the influence of the cereal phytase.5. Intestinal phytase did not appear to be of great significance in the rat but some further hydrolysis of the residual phytate probably occurred in the large intestine of both species by bacterial phytase.

Comparison between steeping and pelleting a mixed diet at different calcium levels on phytate degradation in pigs

1997 ◽  
Vol 77 (3) ◽  
pp. 471-477 ◽  
Author(s):  
Erika Skoglund ◽  
Torben Larsen ◽  
Ann-Sofie Sandberg
Keyword(s):  
Small Intestine ◽  
Calcium Carbonate ◽  
Room Temperature ◽  
Inositol Phosphates ◽  
Intestinal Content ◽  
P Uptake ◽  
Inositol Hexaphosphate ◽  
Phosphorus Absorption ◽  
Phytate Degradation ◽  
Phytate Content

The degradation of phytate (inositol hexaphosphate) in the stomach, small intestine and colon was studied in 36 female pigs. A comparison was made between steeped (9 h, room temperature, feed:water 1:2.5) and pelleted diets with or without calcium carbonate supplementation (12.5 g kg−1). The diet was composed of barley, rapeseed cake and peas in the proportion 70:15:15. Dietary and intestinal content of phytate and its hydrolysis products (inositol penta-, tetra- and triphosphates) were determined using HPLC ion-pair chromatography. Steeping the feed for 9 h at room temperature reduced the phytate content by 45% and increased the amount of free phosphorus threefold. Pelleting the diet reduced phytate content by 7%. Supplementation with Ca decreased dietary phytate reduction. Steeping of the diet reduced ileal phytate content by 40% compared with pelleting. Apparent phosphorus absorption from ileal digesta was 10% lower when pigs were fed the pelleted diet, as compared to the steeped diet. Calcium carbonate supplementation impared inositol hexaphosphate degradation in the colon of pigs, but did not affect phytate degradation in the stomach and small intestine. Calcium carbonate supplementation, moreover, depressed apparent P uptake in the stomach/small intestinal region, as well as in the total gastrointestinal tract, for all feed treatments. Key words: Phytate degradation, inositol phosphates, steeping, pelleting, calcium, pigs

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

The protease phenotype and crystalline nature of the granules of intraepithelial mast cells in Trichinella spiralis-infected mice

1995 ◽  
Vol 53 ◽  
pp. 818-819
Author(s):  
D.S. Friend ◽  
N. Ghildyal ◽  
M.F. Gurish ◽  
K.F. Austen ◽  
R.L. Stevens
Keyword(s):  
Small Intestine ◽  
Mast Cells ◽  
Epithelial Cells ◽  
Lamina Propria ◽  
Trichinella Spiralis ◽  
Intestinal Epithelial ◽  
Carboxypeptidase A ◽  
C3h Mice ◽  
Granule Morphology ◽  
Crystalline Nature

Trichinella spiralis induces a profound mastocytosis and eosinophilia in the small intestine of the infected mouse. Mouse mast cells (MC) store in their granules various combinations of at least five chymotryptic chymases [designated mouse MC protease (mMCP) 1 to 5], two tryptic proteases designated mMCP-6 and mMCP-7 and an exopeptidase, carboxypeptidase A (mMC-CPA). Using antipeptide, protease -specific antibodies to these MC granule proteases, immunohistochemistry was done to determine the distribution, number and protease phenotype of the MCs in the small intestine and spleen 10 to >60 days after Trichinella infection of BALB/c and C3H mice. TEM was performed to evaluate the granule morphology of the MCs between intestinal epithelial cells and in the lamina propria (mucosal MCs) and in the submucosa, muscle and serosa of the intestine (submucosal MCs).As noted in the table below, the number of submucosal MCs remained constant throughout the study. In contrast, on day 14, the number of MCs in the mucosa increased ~25 fold. Increased numbers of MCs were observed between epithelial cells in the mucosal crypts, in the lamina propria and to a lesser extent, between epithelial cells of the intestinal villi.

Sign in / Sign up

Export Citation Format

Share Document