scholarly journals Proteins and Amino Acids Treated with Atmospheric Plasma Show Significantly Increased Bioavailability in Humans

2020 ◽  
Vol 13 ◽  
pp. 117863882094923
Author(s):  
Matthew H Sharp ◽  
Matthew W Stefan ◽  
Raad H Gheith ◽  
Dallen D Reber ◽  
Charlie R Ottinger ◽  
...  

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 acts as the main stimulus for muscle protein synthesis (MPS). The current study investigated the postprandial plasma essential amino acid (EAA) and branched-chain amino acid (BCAA) responses of (1) Hydrolyzed whey protein isolate (HWPI) compared to plasma treated non-hydrolyzed whey protein isolate (PT-NHWPI), (2) standard branch-chain amino acids (S-BCAA) compared to plasma treated branch-chained amino acids (PT-BCAA), (3) standard pea protein (S-PP), compared to plasma treated pea protein (PT-PP), and (4) HWPI compared to PT-PP. Methods: Ten subjects (24.6 ± 5.3 years; 178.8 ± 8.1 cm; 78.6 ± 10.1 kg) participated in a double-blind, randomized, crossover trial comparing four separate protein conditions (HWPI, PT-NHWPI, S-PP, PT-PP). A separate cohort of ten subjects (26.4 ± 7.4 years; 178.8 ± 5.9 cm; 85 ± 12.3 kg) participated in a double-blind randomized, crossover trial comparing two branch-chain amino acid conditions: S-BCAA and PT-BCAA. All conditions were administered following a 7-day washout. Plasma EAA and BCAA concentrations were assessed from blood donated by subjects at pre-consumption, 30-, 60-, 90-, 120-, and 180 minutes post-consumption. Results: Blood plasma levels of total EAA and BCAA concentration were significantly greater in all treated conditions at 30-, 60-, 90-, and 120 minutes post consumption ( P < .05). There were no differences between PT-PP and HWPI. Discussion: All proteins significantly elevated EAAs, and BCAAs from basal levels. However, we conclude that the consumption of the treated proteins significantly raises blood levels of EAAs, and BCAAs to a greater extent across multiple dairy, vegan, and isolated BCAA conditions. Moreover, atmospheric plasma treatment of a vegan protein source makes its amino acid response similar to whey. Thus, protein supplementation with that has undergone Ingredient Optimized® atmospheric plasma treatment technology may be highly beneficial for improving the blood plasma amino acid response.

1983 ◽  
Vol 106 (6) ◽  
pp. 1297-1306 ◽  
Author(s):  
Michael J Bowles ◽  
V.Bala Subramanian ◽  
Anthony B Davies ◽  
Edward B Raftery

1969 ◽  
Vol 47 (3) ◽  
pp. 323-327 ◽  
Author(s):  
J. E. Knipfel ◽  
H. G. Botting ◽  
F. J. Noel ◽  
J. M. McLaughlan

Changes in plasma amino acid (PAA) concentrations effected by force-feeding glucose to rats were studied in two experiments. Attempts were made to relate PAA concentration changes to amino acid requirements, previous diet, time after feeding glucose, and composition of several body proteins. Distribution of 14C-lysine between blood and tissues was examined in an additional rat experiment. Previous diet did not affect the relative quantities of amino acids removed from plasma (PAA removal pattern) after glucose force-feeding. Minimal PAA concentrations occurred by 40 min after glucose administration. The PAA removal pattern was not distinctly related to either amino acid requirements or to any particular body protein composition. Results of administering 14C-lysine simultaneously with glucose indicated that decreased plasma 14C-lysine levels were caused by increased tissue uptake of 14C, likely mediated by insulin. Muscle acted as the major recipient of 14C from plasma, with liver a lesser and more dynamic reservoir of 14C accumulation. Work is continuing to further clarify the significance of the PAA removal pattern, caused by the force-feeding of glucose.


2014 ◽  
Vol 44 (2) ◽  
pp. 134-143
Author(s):  
William Renzo Cortez-Vega ◽  
Irene Rodrigues Freitas ◽  
Sandriane Pizato ◽  
Carlos Prentice

Purpose – The purpose of this study was to isolate Whitemouth croaker protein by alkaline solubilization process and evaluate their nutritional quality to evaluate the bioavailability of essential amino acids. Design/methodology/approach – The proximate composition, essential amino acid composition, in vitro digestibility, apparent bioavailability, chemical score of amino acids and SDS-PAGE were determined for the isolated croaker proteins. Findings – The isolated protein showed a high level of protein 92.21 percent and low amount of lipids 0.57 percent. The protein is rich in lysine and leucine, 108.73 and 96.75 mg/g protein, respectively. The protein isolate had high digestibility, 94.32 percent, which indicates proper utilization of this protein source, while the tryptophan had lower bioavailability (12.58 mg amino acid/mg protein). The high chemical scores were found for the amino acids lysine, methionine+cysteine (6.79 and 5.14). SDS-PAGE of proteins extracted showed appearance of the heavy chain of myosin (220 kDa), actin (50 kDa) and other fractions, with molecular weight between 20 and 50 kDa, such as troponin I, C and T. Originality/value – The products obtained from croaker muscle can be incorporated as a high value supplements in human diets. The isolated protein exhibited a high content of essential amino acids and digestibility, indicating that the protein has a high nutritional quality.


2020 ◽  
Vol 12 (4) ◽  
pp. 1330-1339 ◽  
Author(s):  
Ralf Jäger ◽  
Javier Zaragoza ◽  
Martin Purpura ◽  
Stefania Iametti ◽  
Mauro Marengo ◽  
...  

Abstract The fate of dietary protein in the gut is determined by microbial and host digestion and utilization. Fermentation of proteins generates bioactive molecules that have wide-ranging health effects on the host. The type of protein can affect amino acid absorption, with animal proteins generally being more efficiently absorbed compared with plant proteins. In contrast to animal proteins, most plant proteins, such as pea protein, are incomplete proteins. Pea protein is low in methionine and contains lower amounts of branched-chain amino acids (BCAAs), which play a crucial role in muscle health. We hypothesized that probiotic supplementation results in favorable changes in the gut microbiota, aiding the absorption of amino acids from plant proteins by the host. Fifteen physically active men (24.2 ± 5.0 years; 85.3 ± 12.9 kg; 178.0 ± 7.6 cm; 16.7 ± 5.8% body fat) co-ingested 20 g of pea protein with either AminoAlta™, a multi-strain probiotic (5 billion CFU L. paracasei LP-DG® (CNCM I-1572) plus 5 billion CFU L. paracasei LPC-S01 (DSM 26760), SOFAR S.p.A., Italy) or a placebo for 2 weeks in a randomized, double-blind, crossover design, separated by a 4-week washout period. Blood samples were taken at baseline and at 30-, 60-, 120-, and 180-min post-ingestion and analyzed for amino acid content. Probiotic administration significantly increased methionine, histidine, valine, leucine, isoleucine, tyrosine, total BCAA, and total EAA maximum concentrations (Cmax) and AUC without significantly changing the time to reach maximum concentrations. Probiotic supplementation can be an important nutritional strategy to improve post-prandial changes in blood amino acids and to overcome compositional shortcomings of plant proteins. ClinicalTrials.gov Identifier: ISRCTN38903788


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