scholarly journals Ingestion of Insect Protein Isolate Enhances Blood Amino Acid Concentrations Similar to Soy Protein in A Human Trial

Nutrients ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1357 ◽  
Author(s):  
Mathias Vangsoe ◽  
Rebekka Thogersen ◽  
Hanne Bertram ◽  
Lars-Henrik Heckmann ◽  
Mette Hansen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Muscle Mass ◽  
Soy Protein ◽  
Muscle Protein ◽  
Protein Isolate ◽  
Blood Concentrations ◽  
Blood Samples ◽  
Protein Sources ◽  
Amino Acid Availability

Background: Increased amino acid availability stimulates muscle protein synthesis (MPS), which is critical for maintaining or increasing muscle mass when combined with training. Previous research suggests that whey protein is superior to soy protein in regard to stimulating MPS and muscle mass. Nevertheless, with respect to a future lack of dietary protein and an increasing need for using eco-friendly protein sources it is of great interest to investigate the quality of alternative protein sources, like insect protein. Objective: Our aim was to compare the postprandial amino acid (AA) availability and AA profile in the blood after ingestion of protein isolate from the lesser mealworm, whey isolate, and soy isolate. Design: Six healthy young men participated in a randomized cross-over study and received three different protein supplementations (25 g of crude protein from whey, soy, insect or placebo (water)) on four separate days. Blood samples were collected at pre, 0 min, 20 min, 40 min, 60 min, 90 min, and 120 min. Physical activity and dietary intake were standardized before each trial, and participants were instructed to be fasting from the night before. AA concentrations in blood samples were determined using 1H NMR spectroscopy. Results: A significant rise in blood concentration of essential amino acids (EAA), branched-chain amino acids (BCAA) and leucine was detected over the 120 min period for all protein supplements. Nevertheless, the change in AA profile was significantly greater after ingestion of whey than soy and insect protein (p < 0.05). Area under the curve (AUC) analysis and AA profile revealed comparable AA concentrations for soy and insect protein, whereas whey promoted a ~97% and ~140% greater AUC value than soy and insect protein, respectively. A tendency towards higher AA concentrations beyond the 120 min period was observed for insect protein. Conclusion: We report that ingestion of whey, soy, and insect protein isolate increases blood concentrations of EAA, BCAA, and leucine over a 120 min period (whey > insect = soy). Insect protein induced blood AA concentrations similar to soy protein. However, a tendency towards higher blood AA concentrations at the end of the 120 min period post ingestion was observed for insect protein, which indicates that it can be considered a “slow” digestible protein source.

Control of Muscle Protein Synthesis as a Result of Contractile Activity and Amino Acid Availability: Implications for Protein Requirements

2001 ◽  
Vol 11 (s1) ◽  
pp. S170-S176 ◽  
Author(s):  
Michael J. Rennie
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Contractile Activity ◽  
Muscle Protein Synthesis ◽  
Protein Requirements ◽  
Amino Acid Availability ◽  
Separate Pathway

The major anabolic influences on muscle are feeding and contractile activity. As a result of feeding, anabolism occurs chiefly by increases in protein synthesis with minor changes in protein breakdown. Insulin has a permissive role in increasing synthesis, but the availability of amino acids is crucial for net anabolism. We have investigated the role of amino acids in stimulating muscle protein synthesis, the synergy between exercise and amino acid availability, and some of the signaling elements involved. The results suggest that muscle is acutely sensitive to amino acids, that exercise probably increases the anabolic effects of amino acids by a separate pathway, and that for this reason it is unlikely that accustomed physical exercise increases protein requirements.

scholarly journals The Role of the Anabolic Properties of Plant- versus Animal-Based Protein Sources in Supporting Muscle Mass Maintenance: A Critical Review

Nutrients ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 1825 ◽  
Author(s):  
Insaf Berrazaga ◽  
Valérie Micard ◽  
Marine Gueugneau ◽  
Stéphane Walrand
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Intake ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Essential Amino Acids ◽  
Protein Sources ◽  
Nutritional Strategies

Plant-sourced proteins offer environmental and health benefits, and research increasingly includes them in study formulas. However, plant-based proteins have less of an anabolic effect than animal proteins due to their lower digestibility, lower essential amino acid content (especially leucine), and deficiency in other essential amino acids, such as sulfur amino acids or lysine. Thus, plant amino acids are directed toward oxidation rather than used for muscle protein synthesis. In this review, we evaluate the ability of plant- versus animal-based proteins to help maintain skeletal muscle mass in healthy and especially older people and examine different nutritional strategies for improving the anabolic properties of plant-based proteins. Among these strategies, increasing protein intake has led to a positive acute postprandial muscle protein synthesis response and even positive long-term improvement in lean mass. Increasing the quality of protein intake by improving amino acid composition could also compensate for the lower anabolic potential of plant-based proteins. We evaluated and discussed four nutritional strategies for improving the amino acid composition of plant-based proteins: fortifying plant-based proteins with specific essential amino acids, selective breeding, blending several plant protein sources, and blending plant with animal-based protein sources. These nutritional approaches need to be profoundly examined in older individuals in order to optimize protein intake for this population who require a high-quality food protein intake to mitigate age-related muscle loss.

scholarly journals Postprandial Plasma Amino Acid Responses Between Standard Whey Protein Isolate and Whey Protein Isolate Plus Novel Technology

2019 ◽  
Vol 12 ◽  
pp. 117863881982797 ◽  
Author(s):  
Matthew H Sharp ◽  
Matthew W Stefan ◽  
Ryan P Lowery ◽  
Jacob M Wilson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Whey Protein ◽  
Plasma Levels ◽  
Muscle Protein ◽  
Plasma Concentrations ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Plasma Amino Acid ◽  
Whole Body

Background: Muscle mass is an important determinant of metabolic health and physical function. It has previously been demonstrated that the postprandial rise in circulating essential amino acids (EAA) acts as the main stimulus for muscle protein synthesis (MPS). This study investigated postprandial plasma amino acid (AA) responses of 2 different forms of whey protein isolate (WPI) with iso-caloric and iso-nitrogenous profiles to investigate plasma concentrations of EAA. Methods: In all, 12 healthy men (n = 12) between 19 and 32 years of age were recruited for a randomized, cross-over design, which involved consumption of protein supplements on 2 testing days separated by a 6-day washout period between conditions. On each testing day, subjects consumed either 29.6 g of WPI or WPI + io (whey protein isolate plus Ingredient Optimized Protein®) mixed with 236 mL of water. Plasma EAA and branch chain amino acid (BCAA) concentrations were assessed from whole body donated by subjects at pre-consumption and 30, 60, 90, 120, and 180 minutes post consumption. Results: Plasma levels of total EAA concentration was significantly greater in WPI + io at 30, 60, 90, and 120 minutes post consumption ( P < .01, P < .001, P < .01, and P < .01, respectively). Plasma levels of total BCAA concentration was significantly greater in WPI + io at 30, 60, 90, and 120 minutes post consumption ( P < .01, P < .001, P < .01, and P < .05, respectively) compared with WPI. For leucine, only WPI + io had elevated levels compared with pre-test at 90 minutes post consumption ( P < .001). Discussion: Both conditions significantly elevated EAA, BCAA, and leucine from basal levels. However, we conclude that the consumption of the treated WPI significantly raises plasma EAA, BCAA, and leucine to a greater extent compared with WPI with no treatment. Thus, supplementation with WPI that has undergone Ingredient Optimized® technology may be highly beneficial for those who partake in regular exercise, elderly individuals, or those affected by a reduced sensitivity to amino acids.

scholarly journals Characterising the muscle anabolic potential of dairy, meat and plant-based protein sources in older adults

2017 ◽  
Vol 77 (1) ◽  
pp. 20-31 ◽  
Author(s):  
Stefan H. M. Gorissen ◽  
Oliver C. Witard
Keyword(s):  
Older Adults ◽  
Skeletal Muscle ◽  
Amino Acid ◽  
Muscle Mass ◽  
Dietary Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Amino Acid Profile ◽  
Protein Sources ◽  
Age Related

The age-related loss of skeletal muscle mass and function is caused, at least in part, by a reduced muscle protein synthetic response to protein ingestion. The magnitude and duration of the postprandial muscle protein synthetic response to ingested protein is dependent on the quantity and quality of the protein consumed. This review characterises the anabolic properties of animal-derived and plant-based dietary protein sources in older adults. While approximately 60 % of dietary protein consumed worldwide is derived from plant sources, plant-based proteins generally exhibit lower digestibility, lower leucine content and deficiencies in certain essential amino acids such as lysine and methionine, which compromise the availability of a complete amino acid profile required for muscle protein synthesis. Based on currently available scientific evidence, animal-derived proteins may be considered more anabolic than plant-based protein sources. However, the production and consumption of animal-derived protein sources is associated with higher greenhouse gas emissions, while plant-based protein sources may be considered more environmentally sustainable. Theoretically, the lower anabolic capacity of plant-based proteins can be compensated for by ingesting a greater dose of protein or by combining various plant-based proteins to provide a more favourable amino acid profile. In addition, leucine co-ingestion can further augment the postprandial muscle protein synthetic response. Finally, prior exercise or n-3 fatty acid supplementation have been shown to sensitise skeletal muscle to the anabolic properties of dietary protein. Applying one or more of these strategies may support the maintenance of muscle mass with ageing when diets rich in plant-based protein are consumed.

scholarly journals How to Overcome Anabolic Resistance in Dialysis-Treated Patients?

2021 ◽  
Vol 8 ◽  
Author(s):  
Giacomo Garibotto ◽  
Michela Saio ◽  
Francesca Aimasso ◽  
Elisa Russo ◽  
Daniela Picciotto ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Muscle Mass ◽  
Healthy Subjects ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Optimal Dose ◽  
Dialysis Patients ◽  
Protein Amino Acid ◽  
Anabolic Resistance

A current hypothesis is that dialysis-treated patients are “anabolic resistant” i. e., their muscle protein synthesis (MPS) response to anabolic stimuli is blunted, an effect which leads to muscle wasting and poor physical performance in aging and in several chronic diseases. The importance of maintaining muscle mass and MPS is often neglected in dialysis-treated patients; better than to describe mechanisms leading to energy-protein wasting, the aim of this narrative review is to suggest possible strategies to overcome anabolic resistance in this patient's category. Food intake, in particular dietary protein, and physical activity, are the two major anabolic stimuli. Unfortunately, dialysis patients are often aged and have a sedentary behavior, all conditions which per se may induce a state of “anabolic resistance.” In addition, patients on dialysis are exposed to amino acid or protein deprivation during the dialysis sessions. Unfortunately, the optimal amount and formula of protein/amino acid composition in supplements to maximixe MPS is still unknown in dialysis patients. In young healthy subjects, 20 g whey protein maximally stimulate MPS. However, recent observations suggest that dialysis patients need greater amounts of proteins than healthy subjects to maximally stimulate MPS. Since unneccesary amounts of amino acids could stimulate ureagenesis, toxins and acid production, it is urgent to obtain information on the optimal dose of proteins or amino acids/ketoacids to maximize MPS in this patients' population. In the meantime, the issue of maintaining muscle mass and function in dialysis-treated CKD patients needs not to be overlooked by the kidney community.

scholarly journals Assessment of the nutritional quality of proteins: the use of ‘ileal’ digestibilities of amino acids as measures of their availabilities

1979 ◽  
Vol 41 (3) ◽  
pp. 559-571 ◽  
Author(s):  
S. C. Achinewhu ◽  
D. Hewitt
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nutritional Value ◽  
Protein Quality ◽  
Protein Isolate ◽  
Soya Bean ◽  
Amino Acid Availability ◽  
Analysis Technique ◽  
Bean Protein

1. A comparative study was made of two biological techniques for assessing protein quality in wheat and barley, and in a soya-bean-protein isolate both as received, and after being heat damaged by autoclaving. Amino acid digestibility was determined by the ‘ileal’ analysis technique while amino acid availability was measured in growth assays. Some chemical and microbiological tests were also done.2. Heat treatment of the soya-bean-protein isolate caused little change in amino acid composition but the digestibility of all amino acids and the availability of lysine and methionine were severely reduced, lysine being most affected. The reduced availability of lysine was not entirely attributable to impaired digestibility.3. The amino acids in wheat and barley were highly digestible. The availability of methionine and lysine in barley and of methionine in wheat was high, whereas the availability of lysine in wheat was apparently much lower.4. The results showed that for methionine, digestibility values are a fair measure of the availability. In heat-damaged soya-bean-protein isolate however, digestibility of lysine over-estimated the availability, indicating that amino acid digestibility may sometimes provide a misleading indication of nutritional value.

204 Awardee Talk: Recent Advances in Protein Nutrition in Horses

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 109-109
Author(s):  
Kristine Urschel
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Protein Digestibility ◽  
Future Research ◽  
Amino Acid Supplementation ◽  
Protein Nutrition ◽  
Active Research

Abstract Protein has been recognized as an essential nutrient for animals for well over 100 years. Protein plays many important structural and metabolic roles, and some of its component amino acids have additional functions, including as regulatory molecules, as energy substrates and in the synthesis of other non-protein molecules. Skeletal muscle makes up approximately 50% of body weight in horses, with protein being the major non-water component. As an athletic species, the development and maintenance of muscle mass is of the utmost importance in horses. Because muscle mass is largely determined by the balance of rates of muscle protein synthesis and breakdown, understanding how these pathways are regulated and influenced by dietary protein and amino acid provision is essential. Historically, much research regarding protein nutrition in horses has focused on the protein digestibility of different feed ingredients, and the adequacy of different protein sources in supporting the growth and maintenance of horses. This presentation will focus on some of the current areas of active research relating to protein nutrition in horses: the activation of the signaling pathways that regulate muscle protein synthesis, amino acid supplementation in athletic horses, protein metabolism in aged and horses and those with insulin dysregulation, and amino acid and protein nutrition in predominantly forage-fed horses. There are many exciting opportunities for future research in the area of protein and amino acid nutrition in horses across the lifespan.

scholarly journals Stimulation of Muscle Protein Synthesis by Prolonged Parenteral Infusion of Leucine Is Dependent on Amino Acid Availability in Neonatal Pigs

2009 ◽  
Vol 140 (2) ◽  
pp. 264-270 ◽  
Author(s):  
Fiona A. Wilson ◽  
Agus Suryawan ◽  
Maria C. Gazzaneo ◽  
Renán A. Orellana ◽  
Hanh V. Nguyen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Neonatal Pigs ◽  
Amino Acid Availability ◽  
Stimulation Of

Extent of damage to amino acid availability of whey protein heated with sugar

1991 ◽  
Vol 58 (4) ◽  
pp. 431-441 ◽  
Author(s):  
Thérèse Desrosiers ◽  
Laurent Savoie
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Whey Protein ◽  
Significant Proportion ◽  
Protein Digestibility ◽  
Heating Time ◽  
Heat Treatments ◽  
Molar Ratio ◽  
Amino Acid Availability

SummaryThe effect of heat treatments, at various water activities (αw), on digestibility and on the availabilities of amino acids of whey protein samples in the presence of lactose was estimated by an in vitro digestion method with continuons dialysis. Four αw (0·3, 0·5, 0·7 and 0·97), three temperatures (75, 100 and 121 °C) and three heating periods (50, 500 and 5000 s) were selected. The initial lysine: lactose molar ratio was 1:1. Amino acid profiles showed that excessive heating of whey (121 °C, 5000 s) destroyed a significant proportion of cystine at all αw, lysine at αw 0·3, 0·5 and 0·7, and arginine at αw 0·5 and 0·7. At αw 0·3, 0·5 and 0·7, protein digestibility decreased (P < 0·05) as the temperature increased from 75 to 121 °C for a heating period of 5000 s, and as the heating time was prolonged from 500 to 5000 s at 121 °C. Excessive heating also decreased (P < 0·05) the availabilities of ail amino acids at αw 0·3, 0·5 and 0·7. The availabilities of lysine, proline, aspartic acid, glutamic acid, threonine, alanine, glycine and serine were particularly affected. Severe heating at αw 0·97 did not seem to favour the Maillard reaction, but the availabilities of cystine, tyrosine and arginine were decreased, probably as a result of structural modifications of the protein upon heating. Heating whey protein concentrates in the presence of lactose not only affected lysine, but also impaired enzymic liberation of other amino acids, according to the severity of heat treatments and αw.

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