Enzymes of the small intestine of the calf: effect of dietary protein source on the activities of some enzymes in the small intestinal mucosa and digesta

Montagné, Lucile; Salgado, Paulo; Toullec, R.; Lallès, Jean Paul

doi:10.1002/jsfa.1260

Cited by 8 publications

(6 citation statements)

References 33 publications

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“…At the duodenum, fraction M r > 20,000 probably contained endogenous proteins from digestive secretions, including enzymes and mucus, and proteins sloughedoff in the lumen from the lining of anterior segments of the gut, as suggested by Montagne et al (2000) and Montagne et al (2002). Endogenous proteins flowing at the duodenum are hydrolyzed and absorbed proximodistally by the same mechanisms as dietary proteins.…”

Section: Effect Of Dietary Cp Level On Digestion Of Cp Along the Smalmentioning

confidence: 82%

Influence of Dietary Protein Level and Source on the Course of Protein Digestion Along the Small Intestine of the Veal Calf

Montagné¹,

Crévieu-Gabriel²,

Toullec³

et al. 2003

Journal of Dairy Science

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The objective of this study was to examine the effect of the dietary crude protein (CP) content and source on the distribution of digesta proteins and peptides according to their molecular mass along the small intestine of veal calves. Diets contained 14, 104, 205, and 279 g/kg of CP supplied by skim milk powder (SMP) in experiment 1. Diets contained only SMP or SMP plus proteins (1:1 on digestible CP basis) from either a soybean protein concentrate (SPC), an isolated soy protein partially hydrolyzed (HSPI), or a potato protein concentrate (PPC) in experiment 2. Duodenal, jejunal, and ileal digesta were collected from calves fitted with simple cannulae and continuously infused the milk replacers into the abomasum. The distribution of molecular mass (Mr) of proteins and peptides was studied by gel filtration chromatography. Increasing the dietary CP level of milk replacers increased the flow of oligopeptides and free amino acids in ileal digesta. Incorporating plant protein increased the flow of proteins with Mr > 20,000 in the duodenum and that of proteins and peptides with Mr < 10,000 in the ileum. Hydrolysis of oligopeptides and absorption may be a limiting step in the digestion of plant protein in the veal calf.

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Section: Effect Of Dietary Cp Level On Digestion Of Cp Along the Smalmentioning

confidence: 82%

Influence of Dietary Protein Level and Source on the Course of Protein Digestion Along the Small Intestine of the Veal Calf

Montagné¹,

Crévieu-Gabriel²,

Toullec³

et al. 2003

Journal of Dairy Science

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“…The specific activity of aminopeptidase N (EC 3.4.11.2) was determined according to Sangild et al (1995). The specific activity of alkaline phosphatase (EC 3.1.3.1) was determined according to Martins et al (2000) Alkaline phosphatase and aminopeptidase N were retained because the former is considered to be a biomarker of intestinal maturation and the latter, which contributes to peptide digestion, was found to vary similarly to other peptidases (aminopeptidase A and dipeptidylpeptidase IV) in piglets and calves fed various legume protein sources (Salgado et al 2001;Montagne et al 2002). Protein was measured by the method of Lowry et al (1951) and specific enzyme activities were calculated.…”

Section: Discussionmentioning

confidence: 99%

Influence of thePhaseolus vulgarisphaseolin level of incorporation, type and thermal treatment on gut characteristics in rats

et al. 2006

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Phaseolus vulgaris phaseolin has been shown to stimulate faecal losses of endogenous N in rats. Experiments with purified phaseolin were carried out in rats to test the hypothesis that these losses reflect intestinal disorders. Phaseolin composition varies depending on its constitutive subunits. Therefore, three phaseolin types (S, T, I) were tested. Phaseolin T was incorporated in varying levels (0, 33, 67 or 100 % of the dietary protein) as raw material in experiment 1. In experiment 2, the three phaseolin types were incorporated at 50 %, with or without previous thermic treatment. Raw casein was the basal protein source and was also heated in experiment 2. Faecal digestibility of phaseolin and gut integrity were evaluated in both experiments. The incorporation level or type of phaseolin had little effect on gross anatomy of gut segments but these factors influenced the weight and pH of fresh contents of the stomach and caecum (P, 0·05). Raw phaseolin T incorporated at various levels led to an enlargement of duodenal villi together with a tendency for increased crypt depth in the jejunum (P¼ 0·06). Activities of both alkaline phosphatase in the duodenum and aminopeptidase N in the ileum decreased (P, 0·05) after thermal treatment of casein while they increased (P,0·05) for heat-treated phaseolin S and T, respectively. In conclusion, raw phaseolin had no effect on the tissue weight of gut segments and induced limited alterations in the small intestine. Differences due to phaseolin level or type were limited too.

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“…Of relevance is that Montagne et al ( 60 ) reported that the partial substitution of soya protein concentrate for skimmed milk powder increased alkaline phosphatase activity in the duodenum and jejunum by approximately 33%, which was more pronounced with soya protein isolate. Phytate was probably present in both soya preparations ( 57 ) and may have triggered these increases in alkaline phosphatase activity.…”

Section: Protein–phytate Interactionsmentioning

confidence: 99%

Protein–phytate interactions in pig and poultry nutrition: a reappraisal

et al. 2012

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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 (HPO42–) 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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Enzymes of the small intestine of the calf: effect of dietary protein source on the activities of some enzymes in the small intestinal mucosa and digesta

Cited by 8 publications

References 33 publications

Influence of Dietary Protein Level and Source on the Course of Protein Digestion Along the Small Intestine of the Veal Calf

Influence of Dietary Protein Level and Source on the Course of Protein Digestion Along the Small Intestine of the Veal Calf

Influence of thePhaseolus vulgarisphaseolin level of incorporation, type and thermal treatment on gut characteristics in rats

Protein–phytate interactions in pig and poultry nutrition: a reappraisal

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