Protein-phytate interactions in pig and poultry nutrition: a reappraisal (Record no. 48028)

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control field MX-MdCICY
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control field 20250625153930.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-13831
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245 10 - TITLE STATEMENT
Title Protein-phytate interactions in pig and poultry nutrition: a reappraisal
490 0# - SERIES STATEMENT
Volume/sequential designation Nutrition Research Reviews, 6, p.1-17, 2012
520 3# - SUMMARY, ETC.
Summary, etc. Protein-phytate interactions are fundamental to the detrimental impact of phytate on protein/amino acid availability. The inclusion of exogenous phytase in pig and poultry diets degrades phytate to more innocuous esters and attenuates these negative influences. The objective of the present review is to reappraise the underlying mechanisms of these interactions and reassess their implications in pig and poultry nutrition. Protein digestion appears to be impeded by phytate in the following manner. Binary protein-phytate complexes are formed at pH levels less than the isoelectric point of proteins and complexed proteins are refractory to pepsin digestion. Once the sufficiently high to permit these complexes to persist in the small intestine. Ternary protein-phytate complexes are formed at pH levels above the isoelectric point of proteins where a cationic bridge links the protein and phytate moieties. The molecular weights of protein and polypeptides in small-intestinal digesta may be sufficient to allow phytate to bind nutritionally important amounts of protein in ternary complexes. Thus binary and ternary complexes may impede protein digestion and amino acid absorption in the small intestine. Alternatively, phytate may interact with protein indirectly. Myo-inositol hexaphosphate possesses six phosphate anionic moieties (HPO4 2-)that have strong kosmotropic effects and can stabilise proteins by interacting with the surrounding water medium. Phytate increases mucin secretions into the gut, which increases endogenous amino acid flows as the protein omponent of mucin remains largely undigested. Phytate promotes the transition of Naþ into the small-intestinal lumen and this suggests that phytate may interfere with glucose and amino acid absorption by compromising Naþ-dependent transport systems and the activity of the Na pump (Naþ-Kþ-ATPase). Starch digestion may be depressed by phytate interacting with proteins that are closely associated with starch in the endosperm of cereal grains. While elucidation is required, the impacts of dietary phytate and exogenous phytase on the site, rate and synchrony of glucose and amino acid intestinal uptakes may be of importance to efficient protein deposition. Somewhat paradoxically, the responses to phytase in the majority of amino acid digestibility assays in pigs and poultry are equivocal. A brief consideration of the probable reasons for these inconclusive outcomes is included in this reappraisal.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHYTATE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PROTEIN
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PIGS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element POULTRY
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHYTASE
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Selle, Peter H.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Cowieson, Aaron J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Cowieson, Nathan P.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Ravindran, V.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1KPHRI_8uqNXp_4nUS1WZHfL9Gt1dlT9S/view?usp=drivesdk">https://drive.google.com/file/d/1KPHRI_8uqNXp_4nUS1WZHfL9Gt1dlT9S/view?usp=drivesdk</a>
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-13831 25.06.2025 25.06.2025 Documentos solicitados