The anti-nutritional effect of phytates - the extraphosphorus effect of phytase (review)

2022 ◽  
pp. 74-84
Author(s):  
S. Zinoviev ◽  
V. Kryukov ◽  
H. Mutieva ◽  
I. Glebova ◽  
N. Yarovan
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Gastrointestinal Tract ◽  
The Body ◽  
Acidic Environment ◽  
Protein Digestion ◽  
Nutritional Effect ◽  
Analytical Review ◽  
Hydrolysis Of ◽  
Positively Charged

An analytical review was conducted on the availability of phosphorus from phytates, which increase the inclusion of phytase in the feed, while not only phytic acid is broken down, but also as a result of a decrease in concentration reduces its anti-nutritional effect.Phosphorus from plant feeds is not fully available to animals, as it is part of phytates, the cleavage of which in the gastrointestinal tract (gastrointestinal tract) of animals is limited. Phytates, getting into the acidic environment of the stomach, ionize and react with positively charged minerals, proteins, amino acids, creating compounds inaccessible for further digestion. The inclusion of phytase in compound feed is accompanied by an extra phosphoric effect, which is expressed in an increase in the availability of amino acids and energy. The decision on the feasibility of including phytase in feed is made on the basis of production tests of the proposed drugs.The studies carried out by the authors of invitro confirm the assumption that phytates enter into chemical interactions with peptides, as well as amino acids formed in the processes of protein digestion, turning them into compounds inaccessible to absorption. The proposed explanation does not affect the results of the balance experiment, but allows us to develop the study of the mechanism in terms of the interaction of digested amino acids with phytates. Based on this, another conclusion can be seen: the destruction of phytates should occur in the body before the digestion and dissolution of protein. In birds, this place is the goiter and stomachs, in pigs - the stomach. The hydrolysis of newly formed phytates (FC-amino acid) requires phytases that are active in the environment of the small intestine at pH 6 -7. As a result, the bound amino acids will be re-released and available for absorption. The development of new phytase preparations, taking into account the proposed explanation, will make it possible to create more effective feed preparations.

scholarly journals Modulating protein adsorption onto hydroxyapatite particles using different amino acid treatments

2011 ◽  
Vol 9 (70) ◽  
pp. 918-927 ◽  
Author(s):  
Wing-Hin Lee ◽  
Ching-Yee Loo ◽  
Kim Linh Van ◽  
Alexander V. Zavgorodniy ◽  
Ramin Rohanizadeh
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Adsorption ◽  
Langmuir Model ◽  
The Body ◽  
Mineral Phase ◽  
Adsorption Ability ◽  
Adsorption Study ◽  
Lower Protein ◽  
Positively Charged

Hydroxyapatite (HA) is a material of choice for bone grafts owing to its chemical and structural similarities to the mineral phase of hard tissues. The combination of osteogenic proteins with HA materials that carry and deliver the proteins to the bone-defective areas will accelerate bone regeneration. The study investigated the treatment of HA particles with different amino acids such as serine (Ser), asparagine (Asn), aspartic acid (Asp) and arginine (Arg) to enhance the adsorption ability of HA carrier for delivering therapeutic proteins to the body. The crystallinity of HA reduced when amino acids were added during HA preparation. Depending on the types of amino acid, the specific surface area of the amino acid-functionalized HA particles varied from 105 to 149 m 2 g –1 . Bovine serum albumin (BSA) and lysozyme were used as model proteins for adsorption study. The protein adsorption onto the surface of amino acid-functionalized HA depended on the polarities of HA particles, whereby, compared with lysozyme, BSA demonstrated higher affinity towards positively charged Arg-HA. Alternatively, the binding affinity of lysozyme onto the negatively charged Asp-HA was higher when compared with BSA. The BSA and lysozyme adsorptions onto the amino acid-functionalized HA fitted better into the Freundlich than Langmuir model. The amino acid-functionalized HA particles that had higher protein adsorption demonstrated a lower protein-release rate.

scholarly journals The Influence of Amino Acids on Iron Absorption

Blood ◽  
1963 ◽  
Vol 21 (5) ◽  
pp. 546-552 ◽  
Author(s):  
DONALD KROE ◽  
THOMAS D. KINNEY ◽  
NATHAN KAUFMAN ◽  
J. V. KLAVINS
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Serum Iron ◽  
Iron Absorption ◽  
Iron Deposition ◽  
Series Of Experiments

Abstract A series of experiments were devised to determine the effect of various amino acids upon the absorption of iron from the gastrointestinal tract. This was done by introducing single amino acids and Fe59 into isolated loops of small intestine and measuring the serum for radioactivity and the uptake of Fe59 by the liver. It was found that under the conditions of the experiments all of the amino acids studied effected an increase in the serum iron and iron deposition in the liver.

scholarly journals Cystine and Theanine as Stress-Reducing Amino Acids—Perioperative Use for Early Recovery after Surgical Stress

Nutrients ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 129
Author(s):  
Takashi Tsuchiya ◽  
Shigekazu Kurihara
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Glutamic Acid ◽  
Surgical Stress ◽  
Resting Energy Expenditure ◽  
Nutritional Therapy ◽  
The Body ◽  
Early Recovery ◽  
Reactive Protein ◽  
As Stress

Perioperative nutritional therapy requires the consideration of metabolic changes, and it is desirable to reduce stress aiming at early metabolic normalization. Glutathione (GSH) is a tripeptide composed of glutamic acid, cysteine, and glycine. It is one of the strongest antioxidants in the body and important for adjusting immune function. Cystine and theanine (γ-glutamylethylamide) provide substrates of GSH, cysteine and glutamic acid, promoting the synthesis of GSH. It has been reported that the ingestion of cystine (700 mg) and theanine (280 mg) exhibits inhibitory effects against excess inflammation after strong exercise loads in athletes, based on which its application for invasive surgery has been tried. In patients undergoing gastrectomy, ingestion of cystine (700 mg) and theanine (280 mg) for 10 days from 5 days before surgery inhibited a postoperative increase in resting energy expenditure, promoted recovery from changes in interleukin-6, C-reactive protein, lymphocyte ratio, and granulocyte ratio and inhibited an increase in body temperature. In a mouse small intestine manipulation model, preoperative 5-day administration of cystine/theanine inhibited a postoperative decrease in GSH in the small intestine and promoted recovery from a decrease in behavior quantity. Based on the above, cystine/theanine reduces surgical stress, being useful for perioperative management as stress-reducing amino acids.

scholarly journals Bacillus coagulans GBI-30, 6086 improves amino acid absorption from milk protein

2020 ◽  
Vol 17 (1) ◽  
Author(s):  
Richard A. Stecker ◽  
Jessica M. Moon ◽  
Travis J. Russo ◽  
Kayla M. Ratliff ◽  
Petey W. Mumford ◽  
...  
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Milk Protein ◽  
Bacillus Coagulans ◽  
Protein Concentrate ◽  
Protein Digestion ◽  
Milk Protein Concentrate ◽  
Mean Differences

Abstract Background Probiotic Bacillus coagulans GBI-30, 6086 (BC30) has been shown to increase protein digestion in an in vitro model of the stomach and small intestine. Once active in the small intestine after germination, BC30 aids the digestion of carbohydrates and proteins. The extent to which BC30 administration may impact protein digestion and amino acid appearance in humans after protein ingestion is currently unknown. This study examined the impact of adding BC30 to a 25-g dose of milk protein concentrate on post-prandial changes in blood amino acids concentrations. Methods 14 males and 16 females (n = 30, 26.4 ± 6.5 years; 172.3 ± 10.8 cm; 78.2 ± 14.8 kg; 22.6 ± 7.2% fat) completed two supplementation protocols that each spanned two weeks separated by a washout period that lasted three weeks. Participants were instructed to track their dietary intake and ingest a daily 25-g dose of milk protein concentrate with (MPCBC30) or without (MPC) the addition of BC30. Body composition and demographics were assessed upon arrival to the laboratory. Upon ingestion of their final assigned supplemental dose, blood samples were taken at 0 (baseline), 30, 60, 90, 120, 180, and 240 min post-consumption and analyzed for amino acid concentrations. Results Arginine (p = 0.03) and Isoleucine (p = 0.05) revealed greater area-under-the curve (AUC) in MPCBC30 group compared to MPC. In addition, Arginine (p = 0.02), Serine (p = 0.01), Ornithine (p = 0.02), Methionine (p = 0.04), Glutamic Acid (p = 0.01), Phenylalanine (p = 0.05), Isoleucine (p = 0.04), Tyrosine (p = 0.02), Essential Amino Acids (p = 0.02), and Total Amino Acids (p < 0.01) all revealed significantly greater concentration maximum (CMax) in MPCBC30 compared to MPC. Finally, time to reach CMax (TMax) was significantly faster for Glutamine (p < 0.01), Citrulline (p < 0.01), Threonine (p = 0.04), Alanine (p = 0.02) in MPCBC30 when compared to MPC. Greater mean differences between groups for AUC and CMax in women when compared to the mean differences in men were found for several amino acids. Conclusion In concert with previous in vitro evidence of improved protein digestion and amino acid appearance, these results reveal that adding BC30 to protein sources such as milk protein concentrate can improve AUC, CMax, and faster TMax. Follow-up research should examine differences between gender and explore how aging can impact these outcomes. Retrospectively registered on June 11, 2020 at ClinicalTrials.gov as NCT04427020.

Interaction of amino acids, peptides and peptidases in the small intestine

1975 ◽  
Vol 190 (1099) ◽  
pp. 149-163 ◽  
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Intestinal Absorption ◽  
Intestinal Lumen ◽  
Effective Inhibitor ◽  
Rat Intestine ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Entry Mechanism ◽  
Stimulation Of

Experiments were carried out with rat intestine to investigate the interaction of various amino acids, peptides and peptidases in intestinal absorption. A number of amino acids reduced the rate of hydrolysis of glycylglycine and glycyl-L-leucine and in both cases L-histidine was the most effective inhibitor. With L-leucyl-glycine the effects were quite different, and most amino acids tested caused some stimulation of hydrolysis, except L-histidine which caused inhibition. There was no evidence of competition between amino acids and dipeptides for an entry mechanism, but there was evidence for competition between different dipeptides. Cobalt caused stimulation of dipeptidases in homogenates but not in intact intestine, and this suggested that the dipeptidase is not accessible to cobalt in the intestinal lumen. The results are discussed in relation to the terminal stages of absorption and digestion of protein.

scholarly journals Diagnosing celiac disease: a review of diagnostic modalities of celiac disease

2018 ◽  
Vol 6 (9) ◽  
pp. 2882
Author(s):  
Arslaan Javaeed
Keyword(s):  
Small Intestine ◽  
Celiac Disease ◽  
Immune System ◽  
Gastrointestinal Tract ◽  
Autoimmune Disorder ◽  
The Body ◽  
Celiac Sprue ◽  
Chronic Disorder ◽  
Gluten Sensitive Enteropathy ◽  
Diagnostic Modalities

Celiac disease is known as gluten-sensitive enteropathy. By enteropathy it simply means it is pathology of the gastrointestinal tract and that is why diarrhea (a common GI symptom) is usually one of the commonest presentations of celiac disease. So, it is safe to define celiac disease as an autoimmune disorder that mainly afflicts the small intestine. By autoimmune authors are referring to a disorder in which the body’s immune system works against the body itself. It is a chronic disorder where the sufferer is not able to tolerate gliadin, which is the alcohol soluble component of gluten. Gluten of course is a protein that is usually found in common foods like barley and wheat. Celiac disease which can also be regarded as celiac sprue has a genetic and immunological aspect to its etiology both of which would need to be considered when screening anyone for celiac disease.

scholarly journals Oxidation of essential amino acids by the ovine gastrointestinal tract

2003 ◽  
Vol 89 (5) ◽  
pp. 617-629 ◽  
Author(s):  
Gerald E. Lobley ◽  
Xiangzhen Shen ◽  
Guowei Le ◽  
David M. Bremner ◽  
Eric Milne ◽  
...  
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Secondary Metabolites ◽  
Large Intestine ◽  
Latin Square ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Ruminant Animal

It is not known if the ruminant animal gastrointestinal tract (GIT) can oxidise essential amino acids (AA) other than leucine. Therefore, the oxidation of four essential AA (leucine, lysine, methionine and phenylalanine), supplied systemically as labelled 1-13C forms, was monitored across the mesenteric-drained viscera (MDV; small intestine) and portal-drained viscera (PDV; total GIT), as part of a 4×4 Latin square design, in four wether sheep (35–45 kg) fed at 1·4 × maintenance. Oxidation was assessed primarily by appearance of13CO2,corrected for sequestration of [13C]bicarbonate. The GIT contributed 25 % (P<0·001) and 10 % (P<0·05) towards whole-body AA oxidation for leucine and methionine respectively. This reduced net appearance across the PDV by 23 and 11 % respectively. The contribution of MDV metabolism to total PDV oxidation was 40 % for leucine and 60 % for methionine. There was no catabolism of systemic lysine or phenylalanine across the GIT. Production and exchange of secondary metabolites (e.g. 4-methyl-2-oxo-pentanoate, homocysteine, 2-aminoadipate) across the GIT was also limited. Less AA appeared across the PDV than MDV (P<0·001), indicative of use by tissues such as the forestomach, large intestine, spleen and pancreas. The PDV: MDV net appearance ratios varied (P<0·001) between AA, e.g. phenylalanine (0·81), lysine (0·71), methionine (0·67), leucine (0·56), histidine (0·71), threonine (0·63) and tryptophan (0·48). These differences probably reflect incomplete re-absorption of endogenous secretions and, together with the varied oxidative losses measured, will alter the pattern of AA net supply to the rest of the animal.

Sites of Maximal Absorption and Hydrolysis of Two Dipeptides by Rat Small Intestine in Vivo

1973 ◽  
Vol 44 (6) ◽  
pp. 583-594 ◽  
Author(s):  
R. F. Crampton ◽  
Maria T. Lis ◽  
D. M. Matthews
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Intestinal Lumen ◽  
Proximal Half ◽  
Proximal Small Intestine ◽  
Significant Difference ◽  
Maximal Absorption ◽  
Hydrolysis Of ◽  
Mucosal Uptake

1. Though mucosal uptake of peptides plays an important part in protein absorption, little is known about the site of maximal absorption of peptides in the small intestine. This paper reports an investigation of the characteristics of absorption and hydrolysis of l-methionyl-l-methionine (Met-Met) and glycylglycine (Gly-Gly) by tied loops along the length of the small intestine of the rat, and those of absorption of the equivalent l-methionine (Met) and glycine (Gly). 2. Absorption of Met-Met, or a mixture of Met-Met and Met, was maximal in the proximal half of the small intestine, whereas absorption of Met was maximal in the distal half. Absorption of Met-Met was greater than that of the equivalent Met, especially in the proximal small intestine. In most sites, absorption of a mixture of Met-Met and Met was not significantly different from that of the equivalent Met-Met. Absorption of Met was not increased by raising its concentration from 100 to 200 μmol/ml, but addition of Met-Met (50 μmol/ml) produced a large increase in absorption, indicating that absorption of Met from Met-Met is independent of that from free Met. During absorption of Met-Met, large amounts of free Met appeared in the intestinal lumen. Most of this resulted from intralumen hydrolysis. The hydrolytic ability of mucosal homogenates was several times greater than that required to hydrolyse the Met-Met disappearing from the lumen during absorption. 3. The sites of maximal absorption of Gly-Gly, Gly and a mixture of Gly-Gly and Gly, were all in the proximal half of the intestine near the mid-point. Absorption of Gly-Gly was greater than that of the equivalent Gly, especially in the proximal sites. In several sites, there was no significant difference between absorption of a mixture of Gly-Gly and Gly and that of the equivalent Gly-Gly. During absorption of Gly-Gly, the amounts of free Gly appearing in the lumen were small except in the two most distal sites. Most of the free Gly resulted from back-diffusion from the mucosa. The hydrolytic ability of mucosal homogenates was barely adequate to hydrolyse the Gly-Gly disappearing from the lumen during absorption. 4. The results suggest that there is no real discrepancy between the site of maximal absorption of protein digestion products from tied loops of small intestine and that of their absorption in the intact animal. They indicate that absorption of Met and Met-Met involves independent mechanisms, and confirm previous evidence that the capacity of the intestine to absorb mixtures of peptides and amino acids is greater than its capacity to absorb amino acids alone.

Structure and function of the gut

2010 ◽  
pp. 2201-2204
Author(s):  
D.G. Thompson
Keyword(s):  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Oral Cavity ◽  
Anal Sphincter ◽  
Structure And Function ◽  
The Body ◽  
Major Site ◽  
Colon And Rectum ◽  
Small Intestinal ◽  
And Function

The gastrointestinal tract is a hollow tube stretching from the oral cavity through the oesophagus, stomach, small intestine, colon, and rectum to the anal sphincter. Its function is the transport, digestion, and elimination of ingested material to supply nutrients, vitamins, minerals, and electrolytes that are essential for life, together with the protection of the rest of the body from injurious or allergenic material. The stomach acts as a storage, sterilizing, and digestive tank; the small intestine is the major site of digestion and absorption; the colon’s function is to salvage water and electrolyte from the small intestinal effluent; and the rectum provides a storage function, enabling the elimination of colonic residue (defecation) to be restricted to times of personal convenience....

Sign in / Sign up

Export Citation Format

Share Document