Search

Bioactive peptides either present in foods or released from food proteins during digestion have a wide range of physiological effects, including on gut function. Many of the bioactive peptides characterized to date that influence gut motility, secretion, and absorption are opioid agonists or antagonists. The authors review a body of experimental evidence that demonstrates an effect of peptides from food proteins on endogenous (nondietary) protein flow at the terminal ileum of simple-stomached mammals, including adult humans. At least some dietary peptides (1000-5000 Da) significantly enhance the loss of protein from the small intestine, causing an increased amount of protein to enter the colon. Food-derived peptides appear to either stimulate protein secretion into the gut lumen or inhibit amino acid reabsorption or influence both processes simultaneously. The effect of dietary peptides on small-intestine secretory-protein dynamics is discussed in the context of the major components of gut endogenous protein, sloughed cells, enzymatic secretions, mucin, and bacterial protein. [ABSTRACT FROM AUTHOR]

Background: Current systems for assessing protein quality such as the Digestible Indispensable Amino Acid Score correct apparent amino acid (AA) digestibility for basal endogenous protein losses (bEPL), ignoring the potential influence of the diet on these losses. However, the quantification of total endogenous protein losses (tEPL) poses a challenge., Objectives: To evaluate different methods for quantifying tEPL and bEPL, and to assess their potential in discriminating between tEPL originating from bacteria and host., Methods: Using an incomplete Youden square design, 12 ileal cannulated pigs received 10 different protein sources, and a nitrogen-free (NF) diet. Ileal digesta were collected on days 6 and 7 of each 1-wk feeding period, to quantify endogenous protein losses (EPL) and analyze apparent ileal digestibility. Ileal EPL were estimated based on 1) 16S-+18S gene copy quantitative polymerase chain reaction, 2) diaminopimelic acid (DAPA)+18S, 3) differential AA profiles in digesta, EPL, and bacteria, equaling tEPL, and 4) an NF diet and 5) whey protein isolate (WPI), equaling bEPL., Results: Ileal bEPL based on the NF and WPI method correlated moderately to highly (r = 0.69, P < 0.05), but the NF method probably underestimated bEPL. In pigs fed the WPI diet, EPL based on the WPI and AA profile method were highly correlated (r = 0.88, P < 0.01). Overall, tEPL based on the AA profile method were moderately correlated with the 16S+18S method (r = 0.58, P < 0.001), and DAPA+18S (r = 0.57, P < 0.001). Low correlations were observed between bacterial tEPL based on the AA profile method and 16S or DAPA. Host tEPL based on the AA profile method and 18S were weakly correlated (r = 0.39, P < 0.001)., Conclusions: The AA profile method seems the most appropriate method for tEPL quantification, whereas the WPI method is preferred for bEPL quantification. Despite challenges in distinguishing between bacterial and host EPL, it is evident that bacterial proteins substantially (on average 37%-83%, depending on method) contribute to the EPL., Competing Interests: Conflict of interest The authors report no conflict of interest., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

Fermentation of dietary and endogenous protein in the hindgut is generally considered detrimental to the health of pigs. We investigated the in vitro fermentation potential of porcine endogenous protein in ileal digesta and colonic mucus, using a N-free buffer with an excess of fermentable carbohydrates. Urea, whey protein isolate (WPI, positive control), WPI hydrolysate (WPIH), and combinations of the latter two were used to validate the assay. A new biphasic model, including a linear end simulation, fitted to the gas production data over a 48-h period identified the time point when substrate fermentation ended. A higher degree of hydrolysis of WPI resulted in a higher maximum gas production rate (Rmax, P < 0.01). Differences in Rmax and the time required to reach Rmax were observed among ileal digesta samples, with Rmax increasing with the insoluble protein content, and the highest Rmax occurring with colonic mucus samples (P < 0.05). The endogenous proteins entering the large intestine of pigs can ferment more rapidly compared to highly soluble and digestible protein sources, with Rmax positively correlated with decreasing solubility of endogenous nitrogenous components., (© The Author(s) 2024. Published by Oxford University Press on behalf of the American Society of Animal Science.)

Fermentation of protein in the caeca of chickens may lead to the production of potentially detrimental metabolites, which can reduce gut health. A poor precaecal digestion is expected to increase protein fermentation (PF), as more proteins are likely to enter the caeca. It is unknown if the undigested protein that enters the caeca differs in fermentability depending on their ingredient source. In order to predict which feed ingredients increase the risk of PF, an in vitro procedure was developed, which simulates the gastric and enteric digestion, subsequent caecal fermentation. After digestion, amino acids and peptides smaller than 3.5 kD in the soluble fraction were removed by means of dialysis. These amino acids and peptides are assumed to be hydrolysed and absorbed in the small intestine of poultry and therefore not used in the fermentation assay. The remaining soluble and fine digesta fractions were inoculated with caecal microbes. In chicken, the soluble and fine fractions enter the caeca, to be fermented, while insoluble and coarse fractions bypass them. The inoculum was made N-free to ensure bacteria would require the N from the digesta fractions for their growth and activity. The gas production (GP) from the inoculum, therefore, reflected the ability of bacteria to use N from substrates and was an indirect measure for PF. The Maximum GP rate of ingredients averaged 21.3 ± 0.9 ml/h (mean ± SEM) and was in some cases more rapid than the positive control (urea, maximum GP rate = 16.5 ml/h). Only small differences in GP kinetics were found between protein ingredients. Branched-chain fatty acids and ammonia concentrations in the fermentation fluid after 24 hours showed no differences between ingredients. Results indicate that solubilised undigested proteins larger than 3.5 kD are rapidly fermented independent of its source when an equal amount of N is present., (Copyright © 2023 The Author(s). Published by Elsevier B.V. All rights reserved.)

Poorly digestible proteins may lead to increased protein fermentation in the ceca of broilers and hence, the production of potentially harmful metabolites. To evaluate effects of protein fermentation on gut health, an experimental contrast in ileal nitrogen (N) and amino acid (AA) flow is required. Therefore, our objective was to develop a model that creates a contrast in protein fermentation by increasing the prececal flow of protein within ingredients. To this end, we used additional toasting of protein sources and evaluated the effect on prececal N and AA flows. One-day-old Ross 308 male broilers (n = 480) were divided over 6 dietary treatments, with 8 replicate pens with 10 broilers each. Diets contained 20% of a regular soybean meal (SBM), high protein sunflower seed meal (SFM) or a dehulled rapeseed meal (dRSM) as is, or heat damaged by secondary toasting at 136°C for 20 min (tSBM, tSFM, or tdRSM). Ileal and total tract digesta flows of N and AA were determined with 5 birds per pen in their third week of life using an inert marker (TiO 2 ) in the feed. Additional toasting increased the feed conversion ratio (FCR) only in birds fed dRSM (1.39 vs. 1.31), but not SBM and SFM (interaction P = 0.047). In SBM, additional toasting increased the flow of histidine, lysine, and aspartate through the distal ileum and excreted, while in SFM it had no effect on flows of N and AA. Toasting dRSM increased the prececal flows and excretion of N (862 vs 665 and 999 vs 761 mg/d, respectively) and of the AA. Of the ingredients tested, toasting dRSM is a suitable model to increase protein flows into the hind-gut, permitting the assessment of effects of protein fermentation., (Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.)

Culling rate in dairy cattle has increased considerably, thereby reducing cowś longevity and raising sustainability concerns worldwide. In the last decades, feeding systems have changed towards larger inclusion of preserved forages and reduced fresh herbage, which may limit vitamin E and beta-carotene dietary supply to dairy cows. Because of higher oxidative stress, engendered by greater milk production of modern genetics, the requirement for these nutrients is increased. Therefore, this study aimed to assess the current status of vitamin E and beta-carotene of commercial dairy cows. Blood vitamin E and beta-carotene concentrations were measured in 2 467 dairy cows from 127 farms in Belgium, Germany, Iberia and The Netherlands, that were visited once. Five cows were randomly selected per lactation stage per farm: Dry (between 30 and 1 day(s) before calving), Very-early (from calving until 15 days in milk (DIM)), Early (between 16 and 119 DIM), and Mid-late (from 120 DIM onwards). In addition, a survey was conducted to retrieve data on vitamin E and beta-carotene supplementation and feeding practices. Vitamin E and beta-carotene blood concentrations dropped considerably around calving. Among all surveyed cows, more than 75 and 44% were deficient in vitamin E and beta-carotene (i.e., blood concentration below 3.0 and 3.5 mg/l, respectively). Of the Very-early group, more than 97 and 78% of the cows were deficient in vitamin E and beta-carotene, respectively, with respective blood concentrations of 1.15 and 2.71 mg/l, which was significantly lower than the other lactation stages. Vitamin E and beta-carotene blood concentrations, as well as their supplementation levels, significantly varied among countries. Vitamin E and beta-carotene blood concentrations were positively related to the total estimated daily intakes of vitamin E and beta-carotene. Therefore, blood concentrations of vitamin E and beta-carotene depend on their respective level of intake, which is generally below recommendations and varies greatly between countries. Supplementation could contribute to provide cows with adequate amounts of vitamin E and beta-carotene all along the lactation, to ensure their lifetime performance and improve their fertility., (Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.)

The amount of dietary protein is associated with intestinal disease in different vertebrate species. In humans, this is exemplified by the association between high-protein intake and fermentation metabolite concentrations in patients with inflammatory bowel disease. In production animals, dietary protein intake is associated with postweaning diarrhea in piglets and with the occurrence of wet litter in poultry. The underlying mechanisms by which dietary protein contributes to intestinal problems remain largely unknown. Fermentation of undigested protein in the hindgut results in formation of fermentation products including short-chain fatty acids, branched-chain fatty acids, ammonia, phenolic and indolic compounds, biogenic amines, hydrogen sulfide, and nitric oxide. Here, we review the mechanisms by which these metabolites may cause intestinal disease. Studies addressing how different metabolites induce epithelial damage rely mainly on cell culture studies and occasionally on mice or rat models. Often, contrasting results were reported. The direct relevance of such studies for human, pig, and poultry gut health is therefore questionable and does not suffice for the development of interventions to improve gut health. We discuss a roadmap to improve our understanding of gut metabolites and microbial species associated with intestinal health in humans and production animals and to determine whether these metabolite/bacterial networks cause epithelial damage. The outcomes of these studies will dictate proof-of-principle studies to eliminate specific metabolites and or bacterial strains and will provide the basis for interventions aiming to improve gut health.

Background/objectives: To assess the prevalence of vitamin D deficiency in Dutch athletes and to define the required dosage of vitamin D3 supplementation to prevent vitamin D deficiency over the course of a year., Subjects/methods: Blood samples were collected from 128 highly trained athletes to assess total 25(OH)D concentration. Of these 128 athletes, 54 male and 48 female athletes (18-32 years) were included in a randomized, double blind, dose-response study. Athletes with either a deficient (<50 nmol/l) or an insufficient (50-75 nmol/l) 25(OH)D concentration were randomly assigned to take 400, 1100 or 2200 IU vitamin D3 per day orally for 1 year. Athletes who had a total 25(OH)D concentration above 75 nmol/l at baseline continued with the study protocol without receiving vitamin D supplements. Serum total 25(OH)D concentration was assessed every 3 months, as well as dietary vitamin D intake and sunlight exposure., Results: Nearly 70% of all athletes showed an insufficient (50-75 nmol/l) or a deficient (<50 nmol/l) 25(OH)D concentration at baseline. After 12 months, serum 25(OH)D concentration had increased more in the 2200 IU/day group (+50±27 nmol/l) than the sufficient group receiving no supplements (+4±17 nmol/l; P<0.01) and the 1100 IU/day group (+25±23 nmol/l; P<0.05). Supplementation with 2200 IU/day vitamin D resulted in a sufficient 25(OH)D concentration in 80% of the athletes after 12 months., Conclusions: Vitamin D deficiency is highly prevalent in athletes. Athletes with a deficient or an insufficient 25(OH)D concentration can achieve a sufficient 25(OH)D concentration within 3 months by taking 2200 IU/day.

Context: Monitoring mood state is a useful tool for avoiding nonfunctional overreaching. Brain-derived neurotrophic factor (BDNF) is implicated in stress-related mood disorders., Purpose: To investigate the impact of intensified training-induced mood disturbance on plasma BDNF concentrations at rest and in response to exercise., Methods: Eight cyclists performed 1 wk of normal (NT), 1 wk of intensified (INT), and 1 wk of recovery (REC) training. Fasted blood samples were collected before and after exercise on day 7 of each training week and analyzed for plasma BDNF and cortisol concentrations. A 24-item Profile of Mood State questionnaire was administered on day 7 of each training week, and global mood score (GMS) was calculated., Results: Time-trial performance was impaired during INT (P = .01) and REC (P = .02) compared with NT. Basal plasma cortisol (NT = 153 ± 16 ng/mL, INT = 130 ± 11 ng/mL, REC = 150 ± 14 ng/ml) and BDNF (NT = 484 ± 122 pg/mL, INT = 488 ± 122 pg/mL, REC = 383 ± 56 pg/mL) concentrations were similar between training conditions. Likewise, similar exercise-induced increases in cortisol and BDNF concentrations were observed between training conditions. GMS was 32% greater during INT vs NT (P < .001)., Conclusions: Consistent with a state of functional overreaching (FOR), impairments in performance and mood state with INT were restored after 1 wk of REC. These results support evidence for mood changes before plasma BDNF concentrations as a biochemical marker of FOR and that cortisol is not a useful marker for predicting FOR.

Aim: Muscle fibre hypertrophy is accompanied by an increase in myonuclear number, an increase in myonuclear domain size or both. It has been suggested that increases in myonuclear domain size precede myonuclear accretion and subsequent muscle fibre hypertrophy during prolonged exercise training. In this study, we assessed the changes in muscle fibre size, myonuclear and satellite cell content throughout 12 weeks of resistance-type exercise training in young men., Methods: Twenty-two young men (23 ± 1 year) were assigned to a progressive, 12-weeks resistance-type exercise training programme (3 sessions per week). Muscle biopsies from the vastus lateralis muscle were taken before and after 2, 4, 8 and 12 weeks of exercise training. Muscle fibre size, myonuclear content, myonuclear domain size and satellite cell content were assessed by immunohistochemistry., Results: Type I and type II muscle fibre size increased gradually throughout the 12 weeks of training (type I: 18 ± 5%, type II: 41 ± 6%, P < 0.01). Myonuclear content increased significantly over time in both the type I (P < 0.01) and type II (P < 0.001) muscle fibres. No changes in type I and type II myonuclear domain size were observed at any time point throughout the intervention. Satellite cell content increased significantly over time in both type I and type II muscle fibres (P < 0.001)., Conclusion: Increases in myonuclear domain size do not appear to drive myonuclear accretion and muscle fibre hypertrophy during prolonged resistance-type exercise training in vivo in humans., (© 2015 Scandinavian Physiological Society. Published by John Wiley & Sons Ltd.)

Some food-derived peptides possess bioactive properties, and may affect health positively. For example, the C-terminal lacto-tri-peptides Ile-Pro-Pro (IPP), Leu-Pro-Pro (LPP) and Val-Pro-Pro (VPP) (together named here XPP) are described to lower blood pressure. The bioactivity depends on their availability at the site of action. Quantitative trans-organ availability/kinetic measurements will provide more insight in C-terminal tri-peptides behavior in the body. We hypothesize that the composition of the meal will modify their systemic availability. We studied trans-organ XPP fluxes in catheterized pigs (25 kg; n=10) to determine systemic and portal availability, as well as renal and hepatic uptake of a water-based single dose of synthetic XPP and a XPP containing protein matrix (casein hydrolyte, CasH). In a second experiment (n=10), we compared the CasH-containing protein matrix with a CasH-containing meal matrix and the modifying effects of macronutrients in a meal on the availability (high carbohydrates, low quality protein, high fat, and fiber). Portal availability of synthetic XPP was 0.08 ± 0.01% of intake and increased when a protein matrix was present (respectively 3.1, 1.8 and 83 times for IPP, LPP and VPP). Difference between individual XPP was probably due to release from longer peptides. CasH prolonged portal bioavailability with 18 min (absorption half-life, synthetic XPP: 15 ± 2 min, CasH: 33 ± 3 min, p<0.0001) and increased systemic elimination with 20 min (synthetic XPP: 12 ± 2 min; CasH: 32 ± 3 min, p<0.0001). Subsequent renal and hepatic uptake is about 75% of the portal release. A meal containing CasH, increased portal 1.8 and systemic bioavailability 1.2 times. Low protein quality and fiber increased XPP systemic bioavailability further (respectively 1.5 and 1.4 times). We conclude that the amount and quality of the protein, and the presence of fiber in a meal, are the main factors that increase the systemic bioavailability of food-derived XPP.

Background: It has been demonstrated that protein ingestion before sleep increases muscle protein synthesis rates during overnight recovery from an exercise bout. However, it remains to be established whether dietary protein ingestion before sleep can effectively augment the muscle adaptive response to resistance-type exercise training., Objective: Here we assessed the impact of dietary protein supplementation before sleep on muscle mass and strength gains during resistance-type exercise training., Methods: Forty-four young men (22 ± 1 y) were randomly assigned to a progressive, 12-wk resistance exercise training program. One group consumed a protein supplement containing 27.5 g of protein, 15 g of carbohydrate, and 0.1 g of fat every night before sleep. The other group received a noncaloric placebo. Muscle hypertrophy was assessed on a whole-body (dual-energy X-ray absorptiometry), limb (computed tomography scan), and muscle fiber (muscle biopsy specimen) level before and after exercise training. Strength was assessed regularly by 1-repetition maximum strength testing., Results: Muscle strength increased after resistance exercise training to a significantly greater extent in the protein-supplemented (PRO) group than in the placebo-supplemented (PLA) group (+164 ± 11 kg and +130 ± 9 kg, respectively; P < 0.001). In addition, quadriceps muscle cross-sectional area increased in both groups over time (P < 0.001), with a greater increase in the PRO group than in the PLA group (+8.4 ± 1.1 cm(2) vs. +4.8 ± 0.8 cm(2), respectively; P < 0.05). Both type I and type II muscle fiber size increased after exercise training (P < 0.001), with a greater increase in type II muscle fiber size in the PRO group (+2319 ± 368 μm(2)) than in the PLA group (+1017 ± 353 μm(2); P < 0.05)., Conclusion: Protein ingestion before sleep represents an effective dietary strategy to augment muscle mass and strength gains during resistance exercise training in young men. This trial was registered at clinicaltrials.gov as NCT02222415., (© 2015 American Society for Nutrition.)

The present study examined whether a high protein diet prevents the impaired leukocyte redistribution in response to acute exercise caused by a large volume of high-intensity exercise training. Eight cyclists (VO2max: 64.2±6.5mLkg(-1)min(-1)) undertook two separate weeks of high-intensity training while consuming either a high protein diet (3gkg(-1)proteinBM(-1)day(-1)) or an energy and carbohydrate-matched control diet (1.5gkg(-1)proteinBM(-1)day(-1)). High-intensity training weeks were preceded by a week of normal-intensity training under the control diet. Leukocyte and lymphocyte sub-population responses to acute exercise were determined at the end of each training week. Self-reported symptoms of upper-respiratory tract infections (URTI) were monitored daily by questionnaire. Undertaking high-intensity training with a high protein diet restored leukocyte kinetics to similar levels observed during normal-intensity training: CD8(+) TL mobilization (normal-intensity: 29,319±13,130cells/μL×∼165min vs. high-intensity with protein: 26,031±17,474cells/μL×∼165min, P>0.05), CD8(+) TL egress (normal-intensity: 624±264cells/μL vs. high-intensity with protein: 597±478cells/μL, P>0.05). This pattern was driven by effector-memory populations mobilizing (normal-intensity: 6,145±6,227cells/μL×∼165min vs. high-intensity with protein: 6,783±8,203cells/μL×∼165min, P>0.05) and extravastating from blood (normal-intensity: 147±129cells/μL vs. high-intensity with protein: 165±192cells/μL, P>0.05). High-intensity training while consuming a high protein diet was associated with fewer symptoms of URTI compared to performing high-intensity training with a normal diet (P<0.05). To conclude, a high protein diet might reduce the incidence of URTI in athletes potentially mediated by preventing training-induced impairments in immune-surveillance., (Copyright © 2013 Elsevier Inc. All rights reserved.)

Unlabelled: On September 29, 2011, acknowledged experts in the field of vitamin D, mainly European, were brought together in order to discuss the recent scientific advances in relation to vitamin D: the current requirements and associations with various health outcomes. In this article, the discussions resulting from the meeting are summarized., Introduction: Several groups at risk for developing vitamin D insufficiency have been identified. Accordingly, reviews indicate that a significant percentage of the population worldwide have serum 25-hydroxyvitamin D levels below 50 nmol/l. In addition to the role of vitamin D in bone health, recent studies suggest that it may play a pivotal role in other systems, e.g., the cardiovascular system, pancreas, muscle, immune system and brain. Most evidence, however, is obtained from observational studies and yet inconclusive., Methods: To exchange and broaden knowledge on the requirements for vitamin D and its effect on various health outcomes, a workshop entitled "Vitamin D Expert Meeting: Do we get enough?", was organized., Results: Despite low vitamin D levels worldwide, consensus on the definition of deficiency is not yet reached. In order to define cut-off points for vitamin D whilst taking into account extraskeletal health effects, randomized controlled trials in these fields are warranted. The experts do emphasize that there is evidence to suggest an important role for vitamin D in the maintenance of optimal bone health at all ages and that vitamin D supplementation, in most studies co-administered with calcium, reduces fracture risk in the senior population., Conclusion: To reach a serum 25-hydroxyvitamin D level of 50 nmol/l older adults aged ≥65 years are therefore recommended to meet a mean daily vitamin D intake of 20 μg (800 IU), which is best achieved with a supplement.

Purpose: We examined whether exercise-induced lymphocytosis and lymphocytopenia are impaired with high-intensity training., Methods: Eight trained cyclists (VO(2max) = 64.2 ± 6.5 mL · kg(-1) · min(-1)) undertook 1 wk of normal-intensity training and a second week of high-intensity training. On day 7 of each week, participants performed a cycling task, consisting of 120 min of submaximal exercise followed by a 45-min time trial. Blood was collected before, during, and after exercise. CD8(+) T lymphocytes (CD8(+)TLs) were identified, as well as CD8(+)TL subpopulations on the basis of CD45RA and CD27 expression., Results: High-intensity training (18,577 ± 10,984 cells per microliter × ~165 min) was associated with a smaller exercise-induced mobilization of CD8(+)TLs compared with normal-intensity training (28,473 ± 16,163 cells per microliter × ~165 min, P = 0.09). The response of highly cytotoxic CD8(+)TLs (CD45RA(+)CD27(-)) to exercise was smaller after 1 wk of high-intensity training (3144 ± 924 cells per microliter × ~165 min) compared with normal-intensity training (6417 ± 2143 cells per microliter × ~165 min, P < 0.05). High-intensity training reduced postexercise CD8(+)TL lymphocytopenia (-436 ± 234 cells per microliter) compared with normal-intensity training (-630 ± 320 cells per microliter, P < 0.05). This was driven by a reduced egress of naive CD8(+)TLs (CD27(+)CD45RA(+)). High-intensity training was associated with reduced plasma epinephrine (-37%) and cortisol (-15%) responses (P < 0.05)., Conclusions: High-intensity training impaired CD8(+)TL mobilization and egress in response to exercise. Highly cytotoxic CD8(+)TLs were primarily responsible for the reduced mobilization of CD8(+)TLs, which occurred in parallel with smaller neuroendocrine responses. The reduced capacity for CD8(+)TLs to leave blood after exercise with high-intensity training was accounted for primarily by naive, and also, highly cytotoxic CD8(+)TLs. This impaired CD8(+)TL redistribution in athletes undertaking intensified training may imply reduced immune surveillance.

Background: Ingestion of high doses of casein hydrolysate stimulates insulin secretion in healthy subjects and patients with type 2 diabetes. The effects of low doses have not been studied. The aim of this study was to assess the effect of lower doses of a casein hydrolysate on the glucose and insulin responses to an oral glucose tolerance test in patients with type 2 diabetes., Methods: In this randomized, placebo-controlled, double-blind study, thirteen patients with type 2 diabetes (age: 58±1 years) were studied. Glucose, insulin and C-peptide responses were determined after the oral administration of 0 (control), 6 or 12 g protein hydrolysate in combination with 50 g carbohydrate., Results: Twelve grams of casein hydrolysate, but not 6g, elevated insulin levels and decreased glucose levels post-challenge. These changes over time were not large enough to also affect the total area under the curve of glucose and insulin. C-peptide levels did not change after both treatments., Conclusion: Ingestion of six grams of casein hydrolysate did not affect glucose or insulin responses. Intake of 12 g of casein hydrolysate has a small positive effect on post-challenge insulin and glucose levels in patients with type 2 diabetes., (Copyright © 2010 European Federation of Internal Medicine. Published by Elsevier B.V. All rights reserved.)

Purpose: The purpose of the present study was to examine the effect of increased protein intake on short-term decrements in endurance performance during a block of high-intensity training., Methods: Trained male cyclists (VO(2max) = 64.2 ± 6.5 mL·kg(-1)·min(-1)) completed two 3-wk trials both divided equally into normal (NOR), intensified (INT), and recovery (REC) training. In a counterbalanced crossover experimental design, cyclists received either a high-protein (PRO; 3 g protein·kg(-1) body mass (BM)·d(-1)) or a normal diet (CON; 1.5 g protein·kg(-1) BM·d(-1)) during INT and REC. Dietary carbohydrate content remained constant at 6 g·kg(-1) BM·d(-1). Energy balance was maintained during each training week. Endurance performance was assessed with a VO(2max) test and a preloaded time trial. Alterations in blood metabolite responses to exercise were measured at rest, during, and after exercise. Cyclists completed the Daily Analysis of Life Demands for Athletes (DALDA) questionnaire each day., Results: Increased dietary protein intake led to a possible attenuation (4.3%; 90% confidence limits ×/÷5.4%) in the decrement in time trial performance after a block of high-intensity training compared with NOR (PRO = 2639 ± 350 s; CON = 2555 ± 313 s). Restoration of endurance performance during recovery training possibly benefited (2.0%; ×/÷4.9%) from additional protein intake. Frequency of symptoms of stress described as "worse than normal" reported after a block of high-intensity training was very likely (97%) attenuated (17; ±11 AUC of "a" scores part B, DALDA for INT + REC) by increasing the protein content of the diet. No discernable changes in blood metabolite concentrations were observed in PRO., Conclusions: Additional protein intake reduced symptoms of psychological stress and may result in a worthwhile amelioration of the performance decline experienced during a block of high-intensity training.

Oral or intravenous administration of labeled, free amino acids does not allow the direct assessment of protein digestion and absorption kinetics following dietary protein intake. Consequently, dietary protein sources with labeled amino acids incorporated within the protein are required. The aim of this study was to produce milk proteins intrinsically labeled with l-[1-(13)C]phenylalanine that would allow the assessment of protein digestion and absorption kinetics and the subsequent muscle protein synthetic response to dietary protein intake in vivo in humans. Two Holstein cows (body weight of 726 +/- 38 kg) were continuously infused with l-[1-(13)C]phenylalanine at 402 micromol/min for 44 to 48 h, during and after which plasma samples and milk were collected. After milk protein separation, casein was used in a subsequent human proof-of-principle experiment. Two healthy males (aged 61 +/- 1 yr; body mass index of 22.4 +/- 0.1 kg/m(2)) ingested 35 g of casein highly enriched with [1-(13)C] phenylalanine. Plasma samples were collected at regular intervals, and skeletal muscle biopsies were collected before and 6 h after casein ingestion. In the initial experiment, a total of 5.83 kg of l-[1-(13)C]phenylalanine-enriched milk protein (casein enrichment was 29.4 molar percent excess) was collected during stable isotope infusion in the cows. In the proof-of-principle study, ingestion of 35 g of intrinsically labeled casein resulted in peak plasma l-[1-(13)C]phenylalanine enrichments within 90 min after protein ingestion (9.75 +/- 1.47 molar percent excess). Skeletal muscle protein synthesis rates calculated over the entire 6-h period averaged 0.058 +/- 0.012%/h. The production of intrinsically labeled milk protein is feasible and provides dietary protein that can be used to investigate protein digestion and absorption and the subsequent muscle protein synthetic response in vivo in humans.

Impaired digestion and/or absorption of dietary protein lowers postprandial plasma amino acid availability and, as such, could reduce the postprandial muscle protein synthetic response in the elderly. We aimed to compare in vivo dietary protein digestion and absorption and the subsequent postprandial muscle protein synthetic response between young and elderly men. Ten elderly (64 +/- 1 y) and 10 young (23 +/- 1 y) healthy males consumed a single bolus of 35 g specifically produced, intrinsically l-[1-(13)C]phenylalanine-labeled micellar casein (CAS) protein. Furthermore, primed continuous infusions with l-[ring-(2)H(5)]phenylalanine, l-[1-(13)C]leucine, and l-[ring-(2)H(2)]tyrosine were applied and blood and muscle tissue samples were collected to assess the appearance rate of dietary protein-derived phenylalanine in the circulation and the subsequent muscle protein fractional synthetic rate over a 6-h postprandial period. Protein ingestion resulted in a rapid increase in exogenous phenylalanine appearance in both the young and elderly men. Total exogenous phenylalanine appearance rates (expressed as area under the curve) were 39 +/- 3 mumol.6 h.kg(-1) in the young men and 38 +/- 2 mumol.6 h.kg(-1) in the elderly men (P = 0.73). In accordance, splanchnic amino acid extraction did not differ between young (72 +/- 2%) and elderly (73 +/- 1%) volunteers (P = 0.74). Muscle protein synthesis rates, calculated from the oral tracer, were 0.063 +/- 0.006 and 0.054 +/- 0.004%/h in the young and elderly men, respectively, and did not differ between groups (P = 0.27). We conclude that protein digestion and absorption kinetics and the subsequent muscle protein synthetic response following the ingestion of a large bolus of intact CAS are not substantially impaired in healthy, elderly men.

Background: It has been suggested that a protein hydrolysate, as opposed to its intact protein, is more easily digested and absorbed from the gut, which results in greater plasma amino acid availability and a greater muscle protein synthetic response., Objective: We aimed to compare dietary protein digestion and absorption kinetics and the subsequent muscle protein synthetic response to the ingestion of a single bolus of protein hydrolysate compared with its intact protein in vivo in humans., Design: Ten elderly men (mean +/- SEM age: 64 +/- 1 y) were randomly assigned to a crossover experiment that involved 2 treatments in which the subjects consumed a 35-g bolus of specifically produced L-[1-(13)C]phenylalanine-labeled intact casein (CAS) or hydrolyzed casein (CASH). Blood and muscle-tissue samples were collected to assess the appearance rate of dietary protein-derived phenylalanine in the circulation and subsequent muscle protein fractional synthetic rate over a 6-h postprandial period., Results: The mean (+/-SEM) exogenous phenylalanine appearance rate was 27 +/- 6% higher after ingestion of CASH than after ingestion of CAS (P < 0.001). Splanchnic extraction was significantly lower in CASH compared with CAS treatment (P < 0.01). Plasma amino acid concentrations increased to a greater extent (25-50%) after the ingestion of CASH than after the ingestion of CAS (P < 0.01). Muscle protein synthesis rates averaged 0.054 +/- 0.004% and 0.068 +/- 0.006%/h in the CAS and CASH treatments, respectively (P = 0.10)., Conclusions: Ingestion of a protein hydrolysate, as opposed to its intact protein, accelerates protein digestion and absorption from the gut, augments postprandial amino acid availability, and tends to increase the incorporation rate of dietary amino acids into skeletal muscle protein.

This study examined whether a carbohydrate + casein hydrolysate (CHO+ProH) beverage improved time-trial performance vs. a CHO beverage delivering approximately 60 g CHO/hr. Markers of muscle disruption and recovery were also assessed. Thirteen male cyclists (VO2peak = 60.8 +/- 1.6 ml . kg-1 . min-1) completed 2 computer-simulated 60-km time trials consisting of 3 laps of a 20-km course concluding with a 5-km climb (approximately 5% grade). Participants consumed 200 ml of CHO (6%) or CHO+ProH beverage (6% + 1.8% protein hydrolysate) every 5 km and 500 ml of beverage immediately postexercise. Beverage treatments were administered using a randomly counterbalanced, double-blind design. Plasma creatine phosphokinase (CK) and muscle-soreness ratings were assessed immediately before and 24 hr after cycling. Mean 60-km times were 134.4 +/- 4.6 and 135.0 +/- 4.0 min for CHO+ProH and CHO beverages, respectively. All time differences between treatments occurred during the final lap, with protein hydrolysate ingestion explaining a significant (p < .05) proportion of between-trials differences over the final 20 km (44.3 +/- 1.6, 45.0 +/- 1.6 min) and final 5 km (16.5 +/- 0.6, 16.9 +/- 0.6 min). Plasma CK levels and muscle-soreness ratings increased significantly after the CHO trial (161 +/- 53, 399 +/- 175 U/L; 15.8 +/- 5.1, 37.6 +/- 5.7 mm) but not the CHO+ProH trial (115 +/- 21, 262 +/- 88 U/L; 20.9 +/- 5.3, 32.2 +/- 7.1 mm). Late-exercise time-trial performance was enhanced with CHO+ProH beverage ingestion compared with a beverage containing CHO provided at maximal exogenous oxidation rates during exercise. CHO+ProH ingestion also prevented increases in plasma CK and muscle soreness after exercise.

Tripeptides may possess bioactive properties. For instance, blood pressure lowering is attributed to the proline-rich tripeptides Ile-Pro-Pro (IPP), Leu-Pro-Pro (LPP), and Val-Pro-Pro (VPP). However, little is known about their absorption, distribution, and elimination characteristics. The aim of this study was to characterize the pharmacokinetic behavior of IPP, LPP, and VPP in a conscious pig model. Synthetic IPP, LPP, and VPP were administered intravenously or intragastrically (4.0 mg kg(-1) BW in saline) to 10 piglets (approximately 25 kg body weight) in the postabsorptive state. After intravenous dosing, the elimination half-life for IPP was significantly higher (P<0.001) than for LPP and VPP (2.5+/-0.1, 1.9+/-0.1, and 2.0+/-0.1 min, respectively). After intragastric dosing, however, the elimination half-lives were not significantly different between the peptides (9+/-1, 15+/-4, and 12+/-6 min, respectively). Maximum plasma concentrations were about 10 nmol l(-1) for the three tripeptides. The fraction dose absorbed was 0.077+/-0.010, 0.059+/-0.009, and 0.073+/-0.015%, for IPP, LPP, and VPP, respectively. Proline-rich tripeptides reach the blood circulation intact, with an absolute bioavailability of about 0.1% when administered via a saline solution. Because half-lives of absorption and elimination were maximally about 5 and 15 min, respectively, this suggests that under these conditions a bioactive effect of these tripeptides would be rather acute.

We investigated the effect of carbohydrate and protein hydrolysate ingestion on whole-body and muscle protein synthesis during a combined endurance and resistance exercise session and subsequent overnight recovery. Twenty healthy men were studied in the evening after consuming a standardized diet throughout the day. Subjects participated in a 2-h exercise session during which beverages containing both carbohydrate (0.15 g x kg(-1) x h(-1)) and a protein hydrolysate (0.15 g x kg(-1) x h(-1)) (C+P, n = 10) or water only (W, n = 10) were ingested. Participants consumed 2 additional beverages during early recovery and remained overnight at the hospital. Continuous i.v. infusions with L-[ring-(13)C(6)]-phenylalanine and L-[ring-(2)H(2)]-tyrosine were applied and blood and muscle samples were collected to assess whole-body and muscle protein synthesis rates. During exercise, whole-body and muscle protein synthesis rates increased by 29 and 48% with protein and carbohydrate coingestion (P < 0.05). Fractional synthetic rates during exercise were 0.083 +/- 0.011%/h in the C+P group and 0.056 +/- 0.003%/h in the W group, (P < 0.05). During subsequent overnight recovery, whole-body protein synthesis was 19% greater in the C+P group than in the W group (P < 0.05). However, mean muscle protein synthesis rates during 9 h of overnight recovery did not differ between groups and were 0.056 +/- 0.004%/h in the C+P group and 0.057 +/- 0.004%/h in the W group (P = 0.89). We conclude that, even in a fed state, protein and carbohydrate supplementation stimulates muscle protein synthesis during exercise. Ingestion of protein with carbohydrate during and immediately after exercise improves whole-body protein synthesis but does not further augment muscle protein synthesis rates during 9 h of subsequent overnight recovery.

In contrast to the effect of nutritional intervention on postexercise muscle protein synthesis, little is known about the potential to modulate protein synthesis during exercise. This study investigates the effect of protein coingestion with carbohydrate on muscle protein synthesis during resistance-type exercise. Ten healthy males were studied in the evening after they consumed a standardized diet throughout the day. Subjects participated in two experiments in which they ingested either carbohydrate or carbohydrate with protein during a 2-h resistance exercise session. Subjects received a bolus of test drink before and every 15 min during exercise, providing 0.15 g x kg(-1) x h(-1) carbohydrate with (CHO + PRO) or without (CHO) 0.15 g x kg(-1) x h(-1) protein hydrolysate. Continuous intravenous infusions with l-[ring-(13)C(6)]phenylalanine and l-[ring-(2)H(2)]tyrosine were applied, and blood and muscle biopsies were collected to assess whole body and muscle protein synthesis rates during exercise. Protein coingestion lowered whole body protein breakdown rates by 8.4 +/- 3.6% (P = 0.066), compared with the ingestion of carbohydrate only, and augmented protein oxidation and synthesis rates by 77 +/- 17 and 33 +/- 3%, respectively (P < 0.01). As a consequence, whole body net protein balance was negative in CHO, whereas a positive net balance was achieved after the CHO + PRO treatment (-4.4 +/- 0.3 vs. 16.3 +/- 0.4 micromol phenylalanine x kg(-1) x h(-1), respectively; P < 0.01). In accordance, mixed muscle protein fractional synthetic rate was 49 +/- 22% higher after protein coingestion (0.088 +/- 0.012 and 0.060 +/- 0.004%/h in CHO + PRO vs. CHO treatment, respectively; P < 0.05). We conclude that, even in a fed state, protein coingestion stimulates whole body and muscle protein synthesis rates during resistance-type exercise.

Policosanol is a mixture of long-chain primary aliphatic saturated alcohols. Previous studies in humans and animals have shown that these compounds improved lipoprotein profiles. However, more-recent placebo-controlled studies could not confirm these promising effects. Octacosanol (C28), the main component of sugarcane-derived policosanol, is assumed to be the bioactive component. This has, however, never been tested in an in vivo study that compared individual policosanol components side by side. Here we present that neither the individual policosanol components (C24, C26, C28, or C30) nor the natural policosanol mixture (all 30 mg/100 g diet) lowered serum cholesterol concentrations in LDL receptor knock-out (LDLr(+/-)) mice. Moreover, there was no effect on gene expression profiles of LDLr, ABCA1, HMG-CoA synthase 1, and apolipoprotein A-I (apoA-I) in hepatic and small intestinal tissue of female LDLr(+/-) mice after the 7 week intervention period. Finally, none of the individual policosanols or their respective long-chain fatty acids or aldehydes affected de novo apoA-I protein production in vitro in HepG2 and CaCo-2 cells. Therefore, we conclude that the evaluated individual policosanols, as well as the natural policosanol mixture, have no potential for reducing coronary heart disease risk through effects on serum lipoprotein concentrations.

The present study was designed to assess the impact of coingestion of various amounts of carbohydrate combined with an ample amount of protein intake on postexercise muscle protein synthesis rates. Ten healthy, fit men (20 +/- 0.3 yr) were randomly assigned to three crossover experiments. After 60 min of resistance exercise, subjects consumed 0.3 g x kg(-1) x h(-1) protein hydrolysate with 0, 0.15, or 0.6 g x kg(-1) x h(-1) carbohydrate during a 6-h recovery period (PRO, PRO + LCHO, and PRO + HCHO, respectively). Primed, continuous infusions with L-[ring-(13)C(6)]phenylalanine, L-[ring-(2)H(2)]tyrosine, and [6,6-(2)H(2)]glucose were applied, and blood and muscle samples were collected to assess whole body protein turnover and glucose kinetics as well as protein fractional synthesis rate (FSR) in the vastus lateralis muscle over 6 h of postexercise recovery. Plasma insulin responses were significantly greater in PRO + HCHO compared with PRO + LCHO and PRO (18.4 +/- 2.9 vs. 3.7 +/- 0.5 and 1.5 +/- 0.2 U.6 h(-1) x l(-1), respectively, P < 0.001). Plasma glucose rate of appearance (R(a)) and disappearance (R(d)) increased over time in PRO + HCHO and PRO + LCHO, but not in PRO. Plasma glucose R(a) and R(d) were substantially greater in PRO + HCHO vs. both PRO and PRO + LCHO (P < 0.01). Whole body protein breakdown, synthesis, and oxidation rates, as well as whole body protein balance, did not differ between experiments. Mixed muscle protein FSR did not differ between treatments and averaged 0.10 +/- 0.01, 0.10 +/- 0.01, and 0.11 +/- 0.01%/h in the PRO, PRO + LCHO, and PRO + HCHO experiments, respectively. In conclusion, coingestion of carbohydrate during recovery does not further stimulate postexercise muscle protein synthesis when ample protein is ingested.

An experiment with 224 weaner pigs (initial BW of 7.8 kg) was conducted to determine the effect of dose of dietary phytase supplementation on apparent fecal digestibility of minerals (P, Ca, Mg, Na, K, and Cu) and on performance. Four blocks, each with 8 pens of 7 pigs, were formed. Eight dietary treatments were applied to each block in the 43-d experiment: supplementation of 0 (basal diet), 100, 250, 500, 750, 1,500, or 15,000 phytase units (FTU) or of 1.5 g of digestible P (dP; monocalcium phosphate; positive control) per kilogram of feed. The basal diet, with corn, barley, soybean meal, and sunflower seed meal as the main components, contained 1.2 g of dP per kilogram of feed. Fresh fecal grab samples were collected in wk 4 and 5 of the experiment. Average daily feed intake, ADG, G:F, and digestibility of all of the minerals increased (P < 0.001) with increasing phytase dose. Digestibility of P increased from 34% in the basal diet to a maximum of 84% in the diet supplemented with 15,000 FTU, generating 1.76 g of dP per kilogram of feed. At this level, 85% of the phytate phosphorus was digested, compared with 15% in the basal diet. Compared with the basal diet, digestibility of the monovalent minerals increased maximally at 15,000 FTU, from 81 to 92% (Na) and from 76 to 86% (K). In conclusion, phytase supplementation up to a level of 15,000 FTU/kg of a dP-deficient diet improved performance of weaner pigs and digestibility of minerals, including monovalent minerals. Up to 85% of the phytate-P was digested. Thus, dietary phytase supplementation beyond present day standards (500 FTU/kg) could further improve mineral use and consequently reduce mineral output to the environment.

The interaction between protein and phytate was investigated in vitro using proteins extracted from five common feedstuffs and from casein. The appearance of naturally present soluble protein-phytate complexes in the feedstuffs, the formation of complexes at different pHs, and the degradation of these complexes by pepsin and/or phytase were studied. Complexes of soluble proteins and phytate in the extracts appeared in small amounts only, with the possible exception of rice pollards. Most proteins dissolved almost completely at pH 2, but not after addition of phytate. Phytase prevented precipitation of protein with phytate. Pepsin could release protein from a precipitate, but the rate of release was increased by phytase. Protein was released faster from a protein-phytate complex when phytase was added, but phytase did not hydrolyze protein. Protein was released from the complex and degraded when both pepsin and phytase were added. It appears that protein-phytate complexes are mainly formed at low pH, as occurs in the stomach of animals. Phytase prevented the formation of the complexes and aided in dissolving them at a faster rate. This might positively affect protein digestibility in animals.

Supplementation of microbial phytase usually improves the digestibility and utilization of phosphorus in feedstuffs of plant origin. The effect of phytase supplementation on the digestibilities of AA also has been examined, but the results have been inconsistent. This study was carried out to determine the effect of phytase (Natuphos) supplementation, at a rate of 2,000 phytase units/kg, to two basal diets on the apparent ileal digestibilities (AID) of GE, CP, and AA, and on the apparent total-tract digestibilities (ATTD) of CP and GE. The basal diets contained 18% CP and were formulated (as-fed basis) to contain either a low (0.22%) or high content (0.48%) of phytate P. The high-phytate diet contained 20% rice bran, which is a rich source of phytate and has low intrinsic phytase activity. Eight barrows (average initial BW = 40.6 kg), fitted with a simple T-cannula at the distal ileum, were fed the four diets according to a replicated 4 x 4 Latin square design. The pigs were fed twice daily at 0800 and 2000, equal amounts each meal, at a rate of 2.4 times the daily maintenance requirement for ME. Each experimental period comprised 14 d. Ileal digesta were collected from 0800 to 2000 on d 12, 13, and 14. Feces were collected from 0800 on d 8 until 0800 on d 12. Chromic oxide was used as the digestibility marker. The AID of GE, CP, and AA and the ATTD of CP and GE were less in the high- than in the low-phytate diet (P < 0.01). With the exception of glutamic acid, phytase supplementation did not affect (P > 0.10) the AID of CP and AA. There was no effect (P > 0.05) of phytase on the ATTD of CP and GE. These results show that if a response occurs to phytase supplementation, it is independent of the dietary phytate content.

Positive effects of dietary phytase supplementation on pig performance are observed not only when phosphorus is limiting. Improved energy utilization might be one explanation. Using indirect calorimetry, phytase-induced changes in energy metabolism were evaluated in young piglets with adequate phosphorus intake. Eight replicates of 8 group-housed barrows each were assigned to either a control or a phytase-supplemented diet [1500 phytase units (FTU)/kg feed]. Piglets were fed a restricted amount of the control or phytase diet. The diets were made limiting in energy content by formulating them to a high digestible lysine:DE ratio. Fecal nutrient digestibility, portal blood variables, organ weights, and apparent absorption and urinary excretion of ash, Ca, P, Na, K, Mg, Cu, and Fe, were also measured. A model was developed to estimate energy required for absorption and excretion, which are partly active processes. Phytase tended to improve energy digestibility (P = 0.10), but not its metabolizability. Energy retention and heat production were not affected. At the end of the 3-wk period, pancreas weight (P < 0.05) and blood pH were lower (P < 0.01), and CO(2) pressure was higher (P < 0.01) due to phytase. This suggests that phytase reduced energy expenditure of the digestive tract, and increased metabolic activity in visceral organs. The potential increases in energy retention due to phytase were counterbalanced by increased energy expenditures for processes such as increased mineral absorption (for most P < 0.05), and their subsequent urinary excretion. Energy costs of increased absorption of nutrients, and deposition and excretion of minerals was estimated as 4.6 kJ/(kg(0.75) . d), which is 1% of the energy required for maintenance. The simultaneous existence of both increases and decreases in heat production processes resulted in the absence of a net effect on energy retention.

Four experiments were conducted with weanling pigs fitted with a simple T-cannula at the distal ileum, to determine the effect of phytase supplementation to four diets on the apparent ileal digestibilities (AID) of CP and AA, and the apparent total-tract digestibilities (ATTD) of CP and DE. Phytase (Natuphos, DSM Food Specialties, Delft, The Netherlands) was supplemented at rates of 0, 500 or 1,000 FTU/kg to the four diets. A 20% CP (as-fed basis) corn-soybean meal diet was used in Exp. 1; a 20% CP wheat-soybean meal diet in Exp. 2; a 20% CP wheat-soybean meal-canola meal diet in Exp. 3; and a 19% CP barley-peas-canola meal diet in Exp. 4. In each experiment, six barrows, fitted with a simple T-cannula at the distal ileum, were fed the basal plus phytase-supplemented diets according to a repeated 3 x 3 Latin square design. Each experimental period comprised 14 d. The piglets were at fed 0800 and 2000 daily, equal amounts for each meal, at a daily rate of at least 2.4 times the maintenance requirement for ME. Feces were collected from 0800 on d 8 until 0800 on d 12 of each experimental period. Ileal digesta were collected from 0800 to 2000 on d 12, 13, and 14. Chromic oxide was used as the digestibility marker. The average initial and final BW (average of all experiments) were 7.9 and 16.5 kg, respectively. Phytase supplementation did not improve the AID of CP and AA in Exp. 1, 2, and 4; however, there were improvements (P < 0.05) or tendencies (P < 0.10) toward improvements in the AID of CP and AA or the ATTD of CP and the content of DE with phytase supplementation in Exp. 3. These results suggest that the AA response factor to microbial phytase supplementation depends on diet composition.

An experiment was conducted to examine the effects of adding microbial phytase (Natuphos) on the performance in broilers fed a phosphorus-adequate, lysine-deficient diet. A wheat-soybean meal-sorghum-based diet, containing 1.00% lysine and 0.45% nonphytate phosphorus, was supplemented with L-lysine monochloride to provide 1.06, 1.12, or 1.18% lysine or with 125, 250, 375, 500, 750, or 1,000 phytase units (FTU)/kg diet. Each diet was fed to six pens of 10 chicks each from Day 7 to 28 posthatching. Addition of lysine to the lysine-deficient diet linearly increased (P < 0.001) weight gain and gain per feed of broilers. The response in weight gain to added phytase reached a plateau at 500 FTU/kg diet (quadratic effect, P < 0.001). Phytase had no effect on gain per feed to 250 FTU/kg diet and then increased (quadratic effect, P < 0.05) with further additions. Assuming that the observed responses in weight gain and gain per feed to added phytase were due to the release of lysine alone and by solving linear or nonlinear response equations of lysine and phytase levels, the lysine equivalency value was calculated to be 500 FTU phytase/kg diet = 0.074% lysine. Addition of increasing levels of supplemental phytase to the lysine-deficient diet improved (P < 0.001) the digestibilities of nitrogen and all amino acids. Phytase also increased the AME, and the response reached a plateau at 750 FTU/kg diet (quadratic effect, P < 0.001). These results showed that amino acid and energy responses are responsible for the performance improvements observed when phytase was added to a wheat-soybean meal-sorghum-based diet.

1. A study with growing chicks investigated the effects of an inclusion of an endo-xylanase preparation (LYXASAN) to a wheat- and rye-based diet on performance and nutrient digestibility in relation to the fat source. 2. The basal diet contained 500 g wheat and 100 g rye/kg of diet. The basal diet was supplemented with either 65 g soya oil/kg or 60 g blended animal fat and 5 g soya oil/kg. 3. Endo-xylanase added to the soya oil diet did not affect weight gain, but there was a numerical improvement in food conversion efficiency which was not statistically significant. When the endo-xylanase preparation was added to the blended animal fat diet, both weight gain and food utilisation were improved by 9.5% and 6.0%, respectively (P < 0.05). 4. Digestibilities of organic matter, crude fat, crude fibre and NFE were not significantly affected by adding endo-xylanase to the soya oil diet. However, when endo-xylanase was included in the blended animal fat diet, digestibility of organic matter, crude fat, crude fibre and NFE were improved (P < 0.05). The improvement in fat digestibility was the most pronounced, amounting to 9.4%. Nitrogen retention and metabolisable energy content were improved significantly by the addition of an endo-xylanase to the animal fat diet (P < 0.05), by 6.6% and 6.5% respectively. 5. From the results of this study, it can be concluded that the effects on chick performance and nutrient digestibility of a dietary endo-xylanase in a wheat- and rye-based diet are influenced to a considerable degree by the type of fat in the diet.