Plant seeds as protein sources of food or feed. Evaluation based on amino acid composition of 379 species

1967 ◽  
Vol 15 (6) ◽  
pp. 1077-1089 ◽  
Author(s):  
Cecil H. Van Etten ◽  
William F. Kwolek ◽  
John E. Peters ◽  
Arthur S. Barclay
1959 ◽  
Vol 13 (2) ◽  
pp. 132-150 ◽  
Author(s):  
C. R. Smith ◽  
M. C. Shekleton ◽  
I. A. Wolff ◽  
Quentin Jones

1991 ◽  
Vol 121 (suppl_11) ◽  
pp. S64-S65 ◽  
Author(s):  
Karin Neirinck ◽  
Louis Istasse ◽  
Annick Gabriel ◽  
Christian Van Eenaeme ◽  
Jean-Marie Bienfait

2021 ◽  
Author(s):  
Philippe J. M. Pinckaers ◽  
Jorn Trommelen ◽  
Tim Snijders ◽  
Luc J. C. van Loon

AbstractThere is a global trend of an increased interest in plant-based diets. This includes an increase in the consumption of plant-based proteins at the expense of animal-based proteins. Plant-derived proteins are now also frequently applied in sports nutrition. So far, we have learned that the ingestion of plant-derived proteins, such as soy and wheat protein, result in lower post-prandial muscle protein synthesis responses when compared with the ingestion of an equivalent amount of animal-based protein. The lesser anabolic properties of plant-based versus animal-derived proteins may be attributed to differences in their protein digestion and amino acid absorption kinetics, as well as to differences in amino acid composition between these protein sources. Most plant-based proteins have a low essential amino acid content and are often deficient in one or more specific amino acids, such as lysine and methionine. However, there are large differences in amino acid composition between various plant-derived proteins or plant-based protein sources. So far, only a few studies have directly compared the muscle protein synthetic response following the ingestion of a plant-derived protein versus a high(er) quality animal-derived protein. The proposed lower anabolic properties of plant- versus animal-derived proteins may be compensated for by (i) consuming a greater amount of the plant-derived protein or plant-based protein source to compensate for the lesser quality; (ii) using specific blends of plant-based proteins to create a more balanced amino acid profile; (iii) fortifying the plant-based protein (source) with the specific free amino acid(s) that is (are) deficient. Clinical studies are warranted to assess the anabolic properties of the various plant-derived proteins and their protein sources in vivo in humans and to identify the factors that may or may not compromise the capacity to stimulate post-prandial muscle protein synthesis rates. Such work is needed to determine whether the transition towards a more plant-based diet is accompanied by a transition towards greater dietary protein intake requirements.


2021 ◽  
Vol 37 (2) ◽  
pp. 157-164
Author(s):  
A.N Agbo

The high cost of animal protein sources has made it necessary to evaluate the use of alternative plant protein sources especially unconventional plant proteins. Leucaena leucocephala (white lead tree) is a leguminous plant, the leaves of which have the potential of being used as a plant protein source. Leucaena leaf has been analysed to have a crude protein value of 15.2-34.3%. The plant leaves were collected from the forage section of the College of Agriculture and Animal Sciences (CAAS) Mando, Kaduna. The first group of the leaves was divided into three and sun-dried for 24 hours, 48 hours and 72 hours respectively. The second group was further divided into three subgroups which were soaked in water for 24 hours, 48 hours and 72 hours then sun-dried. The two groups of the leaves were ground into leaf powder. The effects of sun-drying and soaking on amino acid composition of L. leucocephala leaves was investigated. The amino acid analysis was done by ion-exchange chromatography (IEC) using the Technicon Sequential Multisample Amino Acid Analyser (TSM) Technicon Instruments Corporation, New York. The essential amino acids detected in L. leucocephala leaf were arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine and valine. Alanine, cysteine, tyrosine, aspartic acid, glutamic acid, glycine, serine and proline were the non-essential amino acids detected. Sun-drying and soaking led to significant (P≤0.05) losses in the concentration of all the amino acids in the leaf samples (Sundried for 24 hours - SD1, Sundried for 48 hours - SD2, Sundried for 72 hours - SD3, soaked in water for 24 hours – SW1, soaked in water for 48 hours - SW2, soaked in water for 72 hours - SW3) when compared with the raw leaf samples (SU). Soaking caused higher reduction in the amino acid levels when compared to sun-drying in the test leaf meals which was significant at P≤0.05. The amino acid scores revealed that lysine and methionine were the limiting amino acids in L. leucocephala leaves relative to WHO/FAO/UNU standard for preschool aged children. Therefore, processed L. leucocephala leaves should be supplemented with other feed ingredients rich in these amino acids for animal feed production. Keywords: Leucaena leucocephala leaf, sun-drying, soaking, amino acid composition.


PEDIATRICS ◽  
1951 ◽  
Vol 8 (4) ◽  
pp. 455-462
Author(s):  
ANTHONY A. ALBANESE

Evidence has been presented which supports the view that the nutritional inadequacy of unsupplemented breast feeding of infants beyond the third month of life arises primarily from quantitative rather than qualitative limitations of certain amino acids. On the basis of amino acid composition data and the biologic value of a number of proteins tested in infants, it appears that to overcome the defects of this feeding practice which still prevails in larger areas of the world the necessary diet supplements should be derived principally from animal protein sources, milk and meat, rather than cereal proteins. In the lack of animal foods, soybean milk may be employed to advantage.


2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton

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