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Bouillon cubes are widely consumed and when fortified with iron could contribute in preventing iron deficiency. We report the development (part I) and evaluation (current part II) of a novel ferric phytate compound to be used as iron fortificant in condiments such as bouillon. Ferric pyrophosphate (FePP), is the compound of choice due to its high stability in foods, but has a modest absorption in humans. Our objective was to assess iron bioavailability from a novel iron fortificant consisting of ferric iron complexed with phytic acid and hydrolyzed corn protein (Fe-PA-HCP), used in bouillon with and without an inhibitory food matrix. In a randomised single blind, cross-over study, we measured iron absorption in healthy adult women (n = 22). In vitro iron bioaccessibility was assessed using a Caco-2 cell model. Iron absorption from Fe-PA-HCP was 1.5% and 4.1% in bouillon with and without inhibitory matrix, respectively. Relative iron bioavailability to FeSO 4 was 2.4 times higher than from FePP in bouillon (17% vs 7%) and 5.2 times higher when consumed with the inhibitory meal (41% vs 8%). Similar results were found in vitro . Fe-PA-HCP has a higher relative bioavailability versus FePP, especially when bouillon is served with an inhibitory food matrix.

The postprandial rise in essential amino acid (EAA) concentrations modulates the increase in muscle protein synthesis rates after protein ingestion. The EAA content and AA composition of the dietary protein source contribute to the differential muscle protein synthetic response to the ingestion of different proteins. Lower EAA contents and specific lack of sufficient leucine, lysine, and/or methionine may be responsible for the lower anabolic capacity of plant-based compared with animal-based proteins. We compared EAA contents and AA composition of a large selection of plant-based protein sources with animal-based proteins and human skeletal muscle protein. AA composition of oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, potato, milk, whey, caseinate, casein, egg, and human skeletal muscle protein were assessed using UPLC–MS/MS. EAA contents of plant-based protein isolates such as oat (21%), lupin (21%), and wheat (22%) were lower than animal-based proteins (whey 43%, milk 39%, casein 34%, and egg 32%) and muscle protein (38%). AA profiles largely differed among plant-based proteins with leucine contents ranging from 5.1% for hemp to 13.5% for corn protein, compared to 9.0% for milk, 7.0% for egg, and 7.6% for muscle protein. Methionine and lysine were typically lower in plant-based proteins (1.0 ± 0.3 and 3.6 ± 0.6%) compared with animal-based proteins (2.5 ± 0.1 and 7.0 ± 0.6%) and muscle protein (2.0 and 7.8%, respectively). In conclusion, there are large differences in EAA contents and AA composition between various plant-based protein isolates. Combinations of various plant-based protein isolates or blends of animal and plant-based proteins can provide protein characteristics that closely reflect the typical characteristics of animal-based proteins.

To the Editor: In their review, Heymsfield and Shapses (April 11 issue) 1 err in stating that “plant proteins are usually deficient in 1 or more indispensable amino acids.” Although the consumption of a variety of plant foods ensures better nutrition overall, all plants contain all indispensable amino acids. 2 Heymsfield and Shapses further suggest that persons who adhere to plant-based diets should pay special attention to vitamins B 12 and D, calcium, iron, zinc, and iodine. The same advice applies to everyone, regardless of diet. A low vitamin B 12 level is common in persons older than 50 years of age, particularly in . . .

The purpose of the present study was to determine the effects of acetylation with different doses of acetic anhydride on the chemical composition and chosen functional properties of commercial pumpkin protein concentrate (PPC). The total protein content decreased as compared to unmodified samples. Electrophoretic analysis revealed that in the acetylated pumpkin protein, the content of the heaviest protein (35 kDa) decreased in line with increasing concentrations of modifying reagent. Acetylation of PPC caused a significant increase in water-binding and oil-absorption capacity and for emulsifying properties even at the dose of 0.4 mL/g. Additionally, an increase in foaming capacity was demonstrated for preparations obtained with 2.0 mL/g of acetic anhydride, whereas acetylation with 0.4 and 1.0 mL/g caused a decrease in protein solubility as compared to native PPC.

Background Large (48-g), isonitrogenous doses of rice and whey protein have previously been shown to stimulate similar adaptations to resistance training, but the impact of consuming smaller doses has yet to be compared. We evaluated the ability of 24-g doses of rice or whey protein concentrate to augment adaptations following 8 weeks of resistance training. Methods Healthy resistance-trained males ( n  = 24, 32.8 ± 6.7 years, 179.3 ± 8.5 cm, 87.4 ± 8.5 kg, 27.2 ± 1.9 kg/m 2 , 27.8 ± 6.0% fat) were randomly assigned and matched according to fat-free mass to consume 24-g doses of rice ( n  = 12, Growing Naturals, LLC) or whey (n = 12, NutraBio Labs, Inc.) protein concentrate for 8 weeks while completing a standardized resistance training program. Body composition (DXA), muscular strength (one-repetition maximum [1RM]) and endurance (repetitions to fatigue [RTF] at 80% 1RM) using bench press (BP) and leg press (LP) exercises along with anaerobic capacity (Wingate) were assessed before and after the intervention. Subjects were asked to maintain regular dietary habits and record dietary intake every 2 weeks. Outcomes were assessed using 2 × 2 mixed (group x time) factorial ANOVA with repeated measures on time and independent samples t-tests using the change scores from baseline. A p -value of 0.05 and 95% confidence intervals on the changes between groups were used to determine outcomes. Results No baseline differences ( p  > 0.05) were found for key body composition and performance outcomes. No changes ( p  > 0.05) in dietary status occurred within or between groups (34 ± 4 kcal/kg/day, 3.7 ± 0.77 g/kg/day, 1.31 ± 0.28 g/kg/day, 1.87 ± 0.23 g/kg/day) throughout the study for daily relative energy (34 ± 4 kcals/kg/day), carbohydrate (3.7 ± 0.77 g/kg/day), fat (1.31 ± 0.28 g/kg/day), and protein (1.87 ± 0.23 g/kg/day) intake. Significant main effects for time were revealed for body mass ( p  = 0.02), total body water ( p  = 0.01), lean mass ( p  = 0.008), fat-free mass ( p  = 0.007), BP 1RM ( p  = 0.02), BP volume ( p  = 0.04), and LP 1RM ( p  = 0.01). Changes between groups were similar for body mass (− 0.88, 2.03 kg, p  = 0.42), fat-free mass (− 0.68, 1.99 kg, p  = 0.32), lean mass (− 0.73, 1.91 kg, p  = 0.37), fat mass (− 0.48, 1.02 kg, p  = 0.46), and % fat (− 0.63, 0.71%, p  = 0.90). No significant between group differences were seen for BP 1RM (− 13.8, 7.1 kg, p  = 0.51), LP 1RM (− 38.8, 49.6 kg, p  = 0.80), BP RTF (− 2.02, 0.35 reps, p  = 0.16), LP RTF (− 1.7, 3.3 reps, p  = 0.50), and Wingate peak power (− 72.5, 53.4 watts, p  = 0.76) following the eight-week supplementation period. Conclusions Eight weeks of daily isonitrogenous 24-g doses of rice or whey protein in combination with an eight-week resistance training program led to similar changes in body composition and performance outcomes. Retroactively registered on as NCT04411173 .

Background The potential for alternative plant protein sources to replace limited marine ingredients in fish feeds is important for the future of the fish farming industry. However, plant ingredients in fish feeds contain antinutritional factors (ANFs) that can promote gut inflammation (enteritis) and compromise fish health. It is unknown whether enteritis induced by plant materials with notable differences in secondary metabolism is characterised by common or distinct gene expression patterns, and how using feeds with single vs mixed plant proteins may affect the gut transcriptome and fish performance. We used Atlantic salmon parr to investigate the transcriptome responses of distal gut to varying dietary levels (0–45 %) of soy protein concentrate (SPC) and faba bean ( Vicia faba ) protein concentrate (BPC) following an 8-week feeding trial. Soybean meal (SBM) and fish meal (FM) were used as positive and negative controls for enteritis, respectively. Gene expression profiling was performed using a microarray platform developed and validated for Atlantic salmon. Results Different plant protein materials (SPC, BPC and SBM) generated substantially different gut gene expression profiles, with relatively few transcriptomic alterations (genes, pathways and GO terms) common for all plant proteins used. When SPC and BPC were simultaneously included in the diet, they induced less extensive alterations of gut transcriptome than diets with either SPC or BPC singly, probably due to reduced levels of individual ANFs. The mixed plant protein diets were also associated with improved body composition of fish relative to the single plant protein diets, which may provide evidence for a link between the magnitude of changes in gut transcriptome and whole-animal performance. Conclusions Our results indicate that gut transcriptomic profiling provides a useful tool for testing the applicability of alternative protein sources for aquaculture feeds and designing diets with reduced impact of ANFs on fish health. Ultimately, understanding diet-gut interactions and intestinal homeostasis in farmed fish is important to maximise performance and to ensure that aquaculture continues to be a sustainable source of food for a growing world population.

Costs of compounded diets containing fish meal as a primary protein source can be expected to rise as fish meal prices increase in response to static supply and growing demand. Alternatives to fish meal are needed to reduce production costs in many aquaculture enterprises. Some plant proteins are potential replacements for fish meal because of their amino acid composition, lower cost and wide availability. In this study, we measured utilization of soybean meal (SBM) and soy protein concentrate (SPC) by Florida pompano fed compounded diets, to determine the efficacy of these products as fish meal replacements. We also calculated apparent digestibility coefficients (ADCs) for canola meal (CM), corn gluten meal (CGM), and distillers dried grains with solubles (DDGS), following typical methods for digestibility trials. Juvenile Florida pompano were fed fish-meal-free diets containing graded levels of SBM and SPC, and weight gain was compared to a control diet that contained SBM, SPC, and fish meal. Fish fed diets that contained 25-30 percent SBM in combination with 43-39 percent SPC had weight gain equivalent to fish fed the control diet with fish meal, while weight gain of fish fed other soy combinations was significantly less than that of the control group. Apparent crude protein digestibility of CGM was significantly higher than that of DDGS but not significantly different from CM. Apparent energy digestibility of DDGS was significantly lower than CGM but significantly higher than CM. Findings suggested that composition of the reference diet used in a digestibility trial affects the values of calculated ADCs, in addition to the chemical and physical attributes of the test ingredient.

Almond is consumed worldwide and renowned as a valuable healthy food. Despite this, it is also a potent source of allergenic proteins that can trigger several mild to life-threatening immunoreactions. Food processing proved to alter biochemical characteristics of proteins, thus affecting the respective allergenicity. In this paper, we investigated the effect of autoclaving, preceded or not by a hydration step, on the biochemical and immunological properties of almond proteins. Any variation in the stability and immunoreactivity of almond proteins extracted from the treated materials were evaluated by total protein quantification, Enzyme Linked Immunosorbent Assay (ELISA), and protein profiling by electrophoresis-based separation (SDS-PAGE). The sole autoclaving applied was found to weakly affect almond protein stability, despite what was observed when hydration preceded autoclaving, which resulted in a loss of approximately 70% of total protein content compared to untreated samples, and a remarkable reduction of the final immunoreactivity. The final SDS-PAGE protein pattern recorded for hydrated and autoclaved almonds disclosed significant changes. In addition, the same samples were further submitted to human-simulated gastro-intestinal (GI) digestion to evaluate potential changes induced by these processing methods on allergen digestibility. Digestion products were identified by High Pressure Liquid Chromatography-High Resolution Tandem Mass Spectrometry (HPLC-HRMS/MS) analysis followed by software-based data mining, and complementary information was provided by analyzing the proteolytic fragments lower than 6 kDa in size. The autoclave-based treatment was found not to alter the allergen digestibility, whereas an increased susceptibility to proteolytic action of digestive enzymes was observed in almonds subjected to autoclaving of prehydrated almond kernels. Finally, the residual immunoreactivity of the GI-resistant peptides was in-silico investigated by bioinformatic tools. Results obtained confirm that by adopting both approaches, no epitopes associated with known allergens survived, thus demonstrating the potential effectiveness of these treatments to reduce almond allergenicity.

Plant cell enlargement is regulated by wall relaxation and yielding, which is thought to be catalyzed by elusive \"wall-loosening\" enzymes. By employing a reconstitution approach, we found that a crude protein extract from the cell walls of growing cucumber seedlings possessed the ability to induce the extension of isolated cell walls. This activity was restricted to the growing region of the stem and could induce the extension of isolated cell walls from various dicot stems and the leaves of amaryllidaceous monocots, but was less effective on grass coleoptile walls. Endogenous and reconstituted wall extension activities showed similar sensitivities to pH, metal ions, thiol reducing agents, proteases, and boiling in methanol or water. Sequential HPLC fractionation of the active wall extract revealed two proteins with molecular masses of 29 and 30 kD associated with the activity. Each protein, by itself, could induce wall extension without detectable hydrolytic breakdown of the wall. These proteins appear to mediate \"acid growth\" responses of isolated walls and may catalyze plant cell wall extension by a novel biochemical mechanism.

The assembly of 11S globulin seed storage proteins in plants is regulated in part by the activity of a protease that cleaves between asparagine and glycine residues. Post-translational cleavage of subunit precursors into acidic and basic polypeptides is associated with the ability of subunits in trimers to aggregate into hexamers in vitro. An activity is present in extracts from immature soybean seeds that specifically cleaves immature 11S seed storage proteins of soybean and Vicia faba into the polypeptides of the mature proteins. Sequence microanalysis has been used to demonstrate that proglycinin and prolegumin are cut at the legitimate site when proteins synthesized in vitro are used as substrates. A single amino acid change in the cleavage site renders the substrate uncleavable. The protease responsible for this activity also hydrolyzes a synthetic octapeptide whose sequence reproduces four amino acids on either side of the glycinin subunit G4 cleavage site. This assay permitted the purification and characterization of the protease. It is a glycosylated enzyme with an acidic pH optimum and a molecular mass of about 45 kDa in solution.