scholarly journals Influences of dietary protein sources and crude protein levels on intracellular free amino acid profile in the longissimus dorsi muscle of finishing gilts

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Chunfu Qin ◽  
Ping Huang ◽  
Kai Qiu ◽  
Wenjuan Sun ◽  
Ling Xu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dietary Protein ◽  
Free Amino ◽  
Crude Protein ◽  
Amino Acid Profile ◽  
Longissimus Dorsi ◽  
Protein Sources ◽  
Longissimus Dorsi Muscle ◽  
Protein Levels ◽  
Dorsi Muscle

scholarly journals Influence of dietary protein concentration on the oxidation of phenylalanine by the young pig

1986 ◽  
Vol 55 (3) ◽  
pp. 651-658 ◽  
Author(s):  
Ronald O. Ball ◽  
Henry S. Bayley
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
G Protein ◽  
Dietary Protein ◽  
Free Amino Acids ◽  
Free Amino ◽  
Crude Protein ◽  
Protein Concentration ◽  
Skim Milk ◽  
Intact Protein

1. Piglets were weaned at 3 d of age and reared to 2.5 kg on a liquid diet in which the protein was supplied by dried skim milk and a mixture of free amino acids. The oxidation of L-[l-14C]phenyIalanine was measured as an indication of the partition of amino acids between retention and catabolism in pigs (2.5 kg) offered meals containing vaned concentrations of crude protein (nitrogen x 6.25).2. The dietary protein concentration was varied either by increasing the inclusion of a mixture of free amino acids in a series of diets containing 100 g protein/kg from skim milk, or by increasing the level of inclusion of the skim milk in a series of diets containing the equivalent of 100 g protein/kg from the free amino acid mixture.3. The oxidation of phenylalanine was minimized by dietary protein concentrations of 240 and 258 g/kg for the diets containing increasing concentrations of free amino acids or skim milk respectively.4. These results show that a mixture of free amino acids is used more effectively than intact protein for promoting retention of essential amino acids.5. The recovery of radioactivity in expired carbon dioxide was inversely related to the recovery of radioactivity in liver tissue when the concentration of dietary crude protein was increased from deficient to adequate, demonstrating that the fractional oxidation of the indicator amino acid was inversely related to protein synthesis.

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 Amino acid profile of raw and locally processed seeds of Prosopis africana and Ricinus communis: potential antidotes to protein malnutrition

2012 ◽  
Vol 2 (4) ◽  
pp. 107 ◽  
Author(s):  
Chidi U. Igwe ◽  
Okey A. Ojiako ◽  
Ken C. Anugweje ◽  
Linus A. Nwaogu ◽  
Cosmas O. Ujowundu
Keyword(s):  
Amino Acid ◽  
Essential Amino Acid ◽  
Crude Protein ◽  
Ricinus Communis ◽  
Essential Amino Acids ◽  
Amino Acid Profile ◽  
Protein Sources ◽  
Plant Protein Sources ◽  
Prosopis Africana ◽  
The Individual

Background: Increasing incidence of malnutrition occasioned by high incidence of hunger, worsening food situation in the world, insufficient availability and high cost of animal protein sources, has necessitated extensive research into and use of alternative plant protein sources especially underexploited leguminous seeds.Methods: Flours from raw, boiled and fermented seeds of Prosopis africana and Ricinus communis were evaluated for crude protein and amino acid (AA) profiles, and their protein qualities determined. Results: Fermentation improved the protein contents of raw seeds of P. africana and R. communis by 18.70% and 3.95% respectively. In the raw and fermented P. africana seeds, glutamate at 132.60 ± 1.30 and 182.70 ± 3.02 mg/g crude protein (mg/gcp) was the most abundant amino acid (AA), while leucine (62.80 ± 0.60 and 79.50 ± 2.01 mg/gcp) was the most concentrated essential amino acid (EAA). Aspartate (151.90 ± 2.01 and 170.10 ± 2.00 mg/gcp) and arginine (72.80 ± 2.01 and 78.60 ± 2.00 mg/gcp) were the most concentrated and abundant non-essential amino acid (NEAA) and EAA in the raw and fermented samples of R. communis respectively. The total AA concentrations (mg/gcp) of raw and fermented P. africana were 733.00 and 962.60 respectively, while those of R. communis were 823.50 and 894.10 respectively. The total EAA contents (mg/gcp) for P. africana were 311.00 (raw) and 404.50 (fermented), and for R. communis; 401.10 (raw) and 430.30 (fermented). Threonine was the limiting EAA in raw and fermented P. africana, whereas lysine was the limiting EAA in R. communis raw sample. Fermentation significantly (p<0.05) increased the individual AA compositions of P. africana and R. communis by 94% and 53% respectively, while boiling reduced these parameters significantly (p<0.05) by 47% and 82% respectively.Conclusion: P. africana and R. communis seeds are potentially important plant sources of protein and essential amino acids, and so could be of great importance in combating malnutrition and food security problems generally.Key words: Amino acid score; condiments; crude protein; fermentation; legumes; nutrition

scholarly journals Influence of dietary leucine content on the activities of branched-chain amino acid aminotransferase (EC 2.6.1.42) and branched-chain α-keto acid dehydrogenase (EC 1.2.4.4) complex in tissues of preruminant lambs

1988 ◽  
Vol 59 (3) ◽  
pp. 475-483 ◽  
Author(s):  
Isabelle Papet ◽  
Nadia Lezebot ◽  
Francoise Barre ◽  
Maurice Arnal ◽  
Alfred E. Harper
Keyword(s):  
Amino Acid ◽  
Longissimus Dorsi ◽  
Keto Acid ◽  
Amino Acid Catabolism ◽  
Longissimus Dorsi Muscle ◽  
Acid Dehydrogenase ◽  
Branched Chain Amino Acid ◽  
Dorsi Muscle ◽  
Branched Chain ◽  
Low Rate

1. Branched-chain amino acid aminotransferase (EC 2.6.1.42; BCAAT) and branched-chain α-keto acid dehydrogenase (EC 1.2.4.4; BCKDH) activities were measured in preruminant lamb liver, longissimus dorsi muscle, kidney, jejunum and adipose tissue, 2 h after a meal with or without an excess of leucine.2. Skeletal muscle contained about 70% of the total basal BCAAT activities of the tissues studied whereas liver contained about 60% of the total BCKDH activities of these tissues.3. BCAAT activities were very low in preruminant lamb tissues. BCKDH was more phosphorylated in tissues of preruminant lambs than in rats, especially in liver. These low catalytic potentialities might contribute to a low rate of branched-chain amino acid catabolism in sheep.4. Ingestion of an excess of leucine led to an increase in liver and jejunum BCAAT activities and activation of BCKDH in jejunum.

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