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. 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 profiles largely differed among plant-based proteins with leucine contents ranging from 5. Methionine and lysine were typically lower in plant-based proteins 1.
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.
Dietary protein intake stimulates muscle protein synthesis Rennie et al. The muscle protein synthetic response to protein intake can vary substantially between different dietary protein types or sources. The differential muscle protein synthetic response is largely dependent on the postprandial availability of essential amino acids and leucine in particular to the muscle Atherton et al.
Postprandial essential amino acid availability is regulated by a number of physiological processes including dietary protein digestion, amino acid absorption, splanchnic amino acid retention, and skeletal muscle perfusion Groen et al.
Numerous studies have assessed the postprandial muscle protein synthetic response to the ingestion of dairy Burd et al. The robust postprandial increase in muscle protein synthesis rates after the ingestion of these animal-based proteins is associated with the rapid rise in plasma essential amino acid concentrations, and leucine in particular.
In comparison, the muscle protein synthetic responses to the ingestion of plant-based proteins such as soy Phillips ; Tang et al. All amino acids are required for protein synthesis, and lack of one or more amino acids may compromise the postprandial muscle protein synthetic response. Interestingly, the anabolic properties of plant-based proteins have only been studied for a few protein sources, such as soy Fouillet et al.
The use of plant-based protein isolates in food formulations has recently become of interest due to greater sustainability and lower production costs. The current market offers a wide selection of plant-based proteins, but the lack of studies comparing plant-based proteins makes it difficult to select the most optimal plant-based proteins.
We previously reported substantial differences in dietary protein characteristics between various plant-based protein sources van Vliet et al. However, this report included data from a large number of research studies that used independent analyses and assessed only a single protein source or compared a few plant-based protein sources. In the current study, we applied the same analytical procedures on a large selection of commercially available protein isolates to provide a more comprehensive overview of the dietary protein characteristics of the main plant and animal-based protein isolates that are now widely available on the market.
In the present study, we characterized various plant-based protein isolates oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, and potato , animal-based protein isolates whey, milk, caseinate, casein, and egg , and human skeletal muscle protein. This study provides the basis for the identification of plant-based proteins with a high anabolic potential and for defining new plant-based protein blends that provide a complete spectrum of essential amino acids similar to most animal-based protein sources.
Thirty-five protein samples were selected that are presently commercially available as isolated protein powder suitable for application in human nutrition or animal feeds.
In addition, we included lupin, hemp, and microalgae in the current analyses. Lupin is a native European legume with a protein quality score similar to soy, and has become of interest as an alternative to the import of soy Lucas et al.
Microalgae have received considerable attention due to their high protein content similar to meat, egg, soybean, and milk , presence of other beneficial nutrients, and a production that requires less water and land than other crops or animal foods Bleakley and Hayes Protein samples were transported and stored in unopened packaging in a clean, dry, well-ventilated area at ambient temperature and humidity until further analysis. Human skeletal muscle samples were obtained from the m.
Protein samples were requested, obtained, and analyzed between December and June Approximately 10 mg of protein powder in duplicate or freeze-dried human skeletal muscle tissue was collected in steel crucibles. Protein content was calculated by multiplying the determined nitrogen content by 6. There is an ongoing debate on the preferred use of protein source specific nitrogen-to-protein conversion factors that are known for some but not all of the protein sources included in the current analyses Mariotti et al.
In the present study, we used a single conversion factor 6. HCl was evaporated under nitrogen stream and the dried amino acids were reconstituted in 5 mL water.
Amino acid standards were obtained from Sigma-Aldrich A and diluted to final concentrations of , , , , Amino acid concentrations were determined using ultra-performance liquid chromatography UPLC tandem mass spectrometry Waterval et al. The gradient program used was: initial Run-to-run time was 30 min. The capillary voltage was set at 0. Nitrogen gas was used as desolvation gas and as cone gas.
MRM and daughter-ion scans were performed using argon as the collision gas at a pressure of 3. During acid hydrolysis, the non-essential amino acids asparagine and glutamine are converted into aspartic acid and glutamic acid, respectively, and the essential amino acid tryptophan is decomposed, which precludes the ability to detect these amino acids Fountoulakis and Lahm As tryptophan was not measured, the sum of essential amino acids includes threonine, methionine, phenylalanine, histidine, lysine, valine, isoleucine, and leucine.
The acid hydrolysis was performed in the absence of oxygen and the hydrolyzation process was terminated after 12 h of incubation to minimize the reduction of cysteine and methionine. Although the acid hydrolysis is not optimal for all amino acids, we used this procedure for all protein samples to enable direct comparisons between the various protein sources. White bars represent plant-based protein sources, grey bars represent animal-derived protein sources, and black bar represents human skeletal muscle protein.
Essential amino acid contents are shown in Fig. Thus, the essential amino acid requirement would not be met when one of these proteins would be the only protein source consumed.
Note that the requirement is based on a recommended adult protein intake of 0. Trp was not measured. Amino acid profiles differed substantially among plant-based proteins with leucine contents as low as 5.
Despite the high leucine content of corn and potato, the average leucine content of plant-based proteins was lower 7. Lysine and methionine contents are particularly low in plant-based proteins 3. The lysine content of wheat 1. Methionine contents were low in microalgae 0. Less pronounced variability was observed between plant-based and animal-based proteins in isoleucine, valine, histidine, phenylalanine, and threonine contents. White bars represent plant-based protein sources, grey bars represent animal-derived protein sources, and black bar represents human muscle.
Values are presented in g per g raw material. Tryptophan, aspartic acid, asparagine, and glutamine were not measured. Table 2 shows representative amounts of protein or raw material that need to be consumed to allow 2. Between 20 and 54 g of plant-based protein needs to be consumed to ingest 2. This again highlights the variability among plant-based protein sources.
Amount of a certain protein source that needs to be consumed to provide 2. This study measures and compares amino acid composition of various plant-based protein isolates including oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, and potato with animal-derived proteins and human skeletal muscle protein. We observed that plant-based proteins have relatively low essential amino acid and leucine contents when compared with animal-based proteins and human skeletal muscle protein.
As there is a large variability in amino acid composition among the various plant-based protein sources, a balanced combination of different plant-based proteins may provide a high er quality protein blend. World population growth in combination with increasingly limited resources arable land and fresh water has resulted in the need for alternative protein sources to meet global protein requirements.
The production of plant-based foods requires less land and water and is associated with lower greenhouse gas emissions compared with animal-based foods. However, studies suggest that plant-based proteins are of lesser quality with respect to their ability to increase postprandial muscle protein synthesis rates.
This belief is mainly based on the very few studies that assessed the muscle protein synthetic response to the ingestion of soy protein Phillips ; Tang et al.
However, there is a large variability in amino acid composition among different plant-based protein sources. In a recent literature review, we compared data on essential amino acid, leucine, lysine, and methionine contents between various plant and animal-based protein sources van Vliet et al. This review used data obtained from a large selection of publications that applied many different analytical procedures to assess protein characteristics such as nitrogen content and amino acid composition.
Figure 1. Figure 2. Closing Remarks The global or local amino acid composition of nucleic acid-binding proteins is often overlooked and an unjustly underestimated parameter. Author Contributions Conceptualization, M. Institutional Review Board Statement Not applicable. Informed Consent Statement Not applicable. Data Availability Statement No new data were created or analyzed in this study. Conflicts of Interest The authors declare no conflict of interest.
References 1. Ghani N. In: Ranganathan S. Encyclopedia of Bioinformatics and Computational Biology. Academic Press; Oxford, UK: Jutras B. Wang I. Genome Res. Ouwerkerk P. Plant Reverse Genetics. Springer; Basel, Switzerland: Yeast one-hybrid screens for detection of transcription factor DNA interactions; pp. Gaudinier A. In: Busch W. Plant Genomics: Methods and Protocols. Springer; New York, NY: Methods in Molecular Biology. Hellman L. Seo M.
Nucleic Acid Chem. Carey M. Haronikova L. Liu B. Fang Y. Amino Acids. Wei L. Choi S. BMC Bioinform. Helma R. Lyons S. Nucleic Acids Res. Oyoshi T. Bartas M. Tateishi-Karimata H. Cer R. Non-B DB v2. Brazda V. G-Quadruplexes in the Archaea Domain. Rhodes D. Zeraati M. Chedin F. Fleming A. Bevilacqua P. Shin S. DNA Res. Spiegel J. Trends Chem. Varshney D. Cell Biol. Kaushik M. Masai H. Herbert A. Yuan W. Cell Biochem. Bacolla A. Cammas A. Kharel P. Wiley Interdiscip.
Consortium G. Expansion of the Gene Ontology Knowledgebase and Resources. Gene Ontology Consortium: Going Forward. Carbon S. Mishra S. Moccia F. Riccardi C.
BMC Mol. Kim C. BMB Rep. Iwai K. Jukes T. Aukerman M. Genes Dev. Protein molecules are abundant in mammals and are a significant and vital part of the mammalian diet as well as a vital part of their metabolism.
Since proteins and various amino acids are needed in the human diet to help the body repair cells and synthesize new cells, amino acid quantification may be used to monitor or detect the metabolic states by analyzing the content of free amino acids in biological fluids such as urine, blood or plasma. Bio-Synthesis follows GLP guidelines, offering comprehensive amino acid analysis and amino acid quantification services on biological compounds, foods, tissue, biological fluids, and drug samples.
Using UV spectrophotometry, Bio-Synthesis can obtain accurate data on proteins, peptides, and amino acids of a particular sample. Protein characterization, concentration, content, molar ratio, and extinction coefficients can all be determined by using our amino acid analysis services. For additional information, please contact us or send an email to info biosyn. This is a standard analysis that recovers amino acids released from proteins. It should be noted that cysteine and trytophan have low probability of recovery by this method low amounts of trytophan may be recovered.
A buffer blank will be analyzed to determine if background content such as trace proteins, peptides, and amino acids are present. Bio-Synthesis accepts raw amino acid data for thorough analysis. The analysis results will be sent back to the customer with informative comments and suggestions. Bio-Synthesis offers an option for amino acid hydrolysis. The resulting hydrolysate is dried off the acid and sent back to the customer. This system performs reverse-phase chromatography by fluorescence detection.
Prior to chromatography, pre-column derivatization of the amino groups is performed using AccQTag 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate chemistry under aqueous conditions. Amino acids are derivatized with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate AQC. Following the pre-column derivatization of the analytes, separation and detection is achieved using a reversed-phase column and a TUV detector.
The analysis allows for the identification and quantification of up to 42 amino acids and related compounds. These samples are automatically analyzed with assured performance methods and reports are generated using pre-defined software templates.
It is advisable to contact Bio-Synthesis prior to sample submission to discuss the required analysis.
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