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      Sesame meal as the first protein source in piglet starter diets and advantages of a phytase: a digestive study

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          Abstract

          Soybean meal (SBM) is the protein source that is used most in feeding piglets, but its high price has prompted a search for alternatives. One option is sesame meal (SM), a by-product of sesame oil. This study evaluated the effects of SM and phytase on the intestinal morphology, total trypsin activity (TTA) and specific trypsin activity (STA), apparent ileal digestibility (AID) of amino acids (AAs), and apparent total tract digestibility (ATTD) of phosphorus (P), calcium (Ca), and energy (E) in weaned piglets. Twenty piglets weaned at 17 days old were placed in metabolic cages in a temperature-controlled room. When the piglets were 21 days old, cannulas were fitted at the terminal ileum. From the fourth day after surgery, piglets received the experimental treatments for nine days, namely an SM or SBM diet, each with or without phytase. The protein source or phytase did not affect villus height, crypt depth, or TTA. However, phytase increased STA. The AID of dry matter (DM), E, crude protein (CP), and AA was similar among treatments, except for arginine, which was more digestible in the SM diets (85.8) than in the SBM ones (81.6). The ATTD of DM and E was higher in the SM than in the SBM diets. Phytase increased the ATTD of Ca (22.7 %) and P (27.9 %). The findings showed that SM can be used as a protein source for piglets and that its consumption increases arginine intake. The addition of phytase to the diet increases the ATTD of P and Ca.

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          Technical note: a procedure for the preparation and quantitative analysis of samples for titanium dioxide.

          A procedure was developed for the rapid analysis of titanium dioxide (TiO2) concentrations in feed and fecal samples. Samples were digested in concentrated H2SO4 for 2 h, followed by addition of 30% H2O2, and absorbance was measured at 410 nm. Standards were prepared by spiking blanks with increasing amounts of TiO2, resulting in a linear standard curve. Complete analysis using this procedure can typically be accomplished within 4.5 h. This procedure was compared to a previously published dry-ash procedure for the analysis of TiO2 in bovine fecal samples. Three sources of OM devoid of TiO2 (a forage sample, a bovine fecal sample without Cr2O3, and a bovine fecal sample containing Cr2O3) were spiked with graded amounts (0, 2, 4, 6, 8, or 10 mg) of TiO2. With our procedure, TiO2 recoveries averaged 96.7, 97.5, and 98.5%, for the three OM sources, respectively, vs. 74.3, 83.8, and 53.1% for the same samples analyzed using the dry-ash method. These results suggest that our procedure is a rapid and accurate alternative to dry-ash procedures for the determination of TiO2.
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            Protein-phytate interactions in pig and poultry nutrition: a reappraisal.

            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 protein isoelectric points are exceeded binary complexes dissociate; however, the isoelectric point of proteins in cereal grains may be 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 (HPO(4)(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 component of mucin remains largely undigested. Phytate promotes the transition of Na(+) into the small-intestinal lumen and this suggests that phytate may interfere with glucose and amino acid absorption by compromising Na(+)-dependent transport systems and the activity of the Na pump (Na(+)-K(+)-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.
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              Total and phytate phosphorus contents of various foods and feedstuffs of plant origin

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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                sajas
                South African Journal of Animal Science
                S. Afr. j. anim. sci.
                The South African Society for Animal Science (SASAS) (Pretoria, Gauteng, South Africa )
                0375-1589
                2221-4062
                2017
                : 47
                : 5
                : 606-615
                Affiliations
                [01] Querétaro orgnameUniversidad Autónoma de Querétaro orgdiv1Facultad de Ciencias Naturales México
                [02] Querétaro orgnameInstituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias orgdiv1Centro Nacional de Investigación en Fisiología Animal México
                Article
                S0375-15892017000500003
                10.4314/sajas.v47i5.3
                37449a5b-071a-4390-bb3f-252f82ed80bc

                This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

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                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 37, Pages: 10
                Product

                SciELO South Africa


                phosphorus digestibility,arginine,piglets weaning,Amino acids digestibility

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