scholarly journals Meat protein quality of Dormitator latifrons (Pisces: Eleotridae): arguments for use by rural communities

2019 ◽  
Vol 7 (1) ◽  
Author(s):  
Mao Ernesto Rafael Basto-Rosales ◽  
Olimpia Carrillo-Farnés ◽  
Cynthia Eugenia Montoya-Martínez ◽  
Daniel Badillo-Zapata ◽  
Gustavo Gustavo Rodríguez-Montes de Oca ◽  
...  

The objective of this study was to evaluate the quality of meat protein of Dormitator latifrons for humans based on its Protein Digestibility Corrected Amino Acid Score (PDCAAS). Wild and cultured specimens were evaluated for amino acid content using HPLC equipment. The calculation of PDCAAS was performed as follows: milligrams of essential amino acid in 1 g of test protein per milligram of the same amino acid in 1 g of reference protein per true digestibility. To evaluate the protein of D. latifrons in relation to that of other fish, PDCAAS was calculated from the proteins of eight fish usually used in human nutrition. D. latifrons has a good essential amino acid profile, providing the same nutritional quality as those of other fish. Although the meat of wild D. latifrons contributes only 73% of human lysine requirements, it can be complemented with other lysine sources.

Author(s):  
Bidyut Kumar Sarmah ◽  
Rubi Gupta ◽  
Sumita Acharjee

Background: Evaluation of the nutritional composition of genetically modified (GM) crops is mandatory for their deregulation. Chickpea is known for its high-quality protein and demonstrating that the seed protein quality of transgenic chickpea remains unaltered is important for its acceptance. Amino acid content, seed storage protein profile and the digestibility of chickpea protein are important determinants of seed protein quality. Thus, in the present study, we assessed the effect of Bt (Cry2Aa) gene expression on the Bt chickpea seed protein quality. Methods: We assessed the amino acid profile, in vitro protein digestibility and factors affecting protein digestibility like trypsin inhibitor, tannins and phytic acid contents of the transgenic Bt chickpea expressing a codon modified Cry2Aa gene and its non-transgenic counterpart. Furthermore, the seed storage proteins were also fractionated and separated on SDS-PAGE followed by mass spectroscopy of the major peptides. Result: Amino acid profile and factors affecting protein digestibility revealed no significant variations between transgenic and non-transgenic chickpeas. Seed storage protein profile confirmed the presence of legumin, vicilin and albumin. No potential change in the digestibility pattern of seed proteins was revealed. Our findings suggest no potential unintended changes in chickpea seed protein quality due to the expression of Cry2Aa gene.


2005 ◽  
Vol 88 (3) ◽  
pp. 988-994 ◽  
Author(s):  
Gertjan Schaafsma

Abstract Protein Digestibility-Corrected Amino Score (PDCAAS) is discussed. PDCAAS is now widely used as a routine assay for protein quality evaluation, replacing the more traditional biological methods [e.g., measurement of the Protein Efficiency Ratio (PER) in rats]. PDCAAS is based on comparison of the essential amino acid content of a test protein with that of a reference essential amino acid pattern and a correction for differences in protein digestibility as determined using a rat assay. Although PDCAAS is a rapid and useful method, it often shows discrepancies when compared to PER values. These discrepancies relate to the following issues: uncertainty about the validity of reference patterns, invalidity of correction for fecal (versus ileal) digestibility, truncation of PDCAAS values to 100%, failure to obtain full biological response after supplementation of the limiting essential amino acid, discrepancies between protein and amino acid digestibility, effects of processing on protein quality, and effects of the presence of antinutritional factors in the matrix containing the protein. Part of the discrepancy between PDCAAS and PER can be overcome by modifications of PDCAAS. This article describes some proposed modifications and puts forward the suggestion that the rat protein fecal digestibility assay be replaced by an in vitro ileal amino acid digestibility assay based on a computer-controlled gastrointestinal model.


2001 ◽  
Vol 47 ◽  
pp. 21-26
Author(s):  
Biljana Bauer Petrovska

The nutritional quality of mushroom protein varies and is strongly affected by the relative proportion of each amino acid. Thus, the purpose of this study was to estimate the concentration of the amino acids present in mushroom proteins in order to evaluate the protein nutritional value. In this investigation fifteen field-collected mushroom samples of the Boletaceae family from various parts of Macedonia were included. After acid hydrolysis and pre-column derivatisation with phenyl isothiocyanate (PITC) determination of seventeen amino acids was carried out by the HPLC method. Tryptophan was determined spectophotometrically in the alkaline hydrolysates. The dietary protein quality of the investigated mushrooms was evaluated by comparison of the essential amino acid content with the reference FAO/WHO pattern. Essential amino acids made up 47-75 % of all determined amino acids depending on the origin and the species of the fruit body. Lysine was the most often found limiting amino acid in the investigated mushrooms samples. The nutritional value of proteins calculated by biological value, protein ratio, chemical score and essential amino acid index was very high in the majority of mushrooms studied. The biological value of the mushroom protein varied from 51.3 to 78.9 %. Protein amino acids accounted for about 66.7 % of the total nitrogen, suggesting that a practical nitrogen to protein conversion factor for this Macedonian edible Boletaceae mushroom may be considered to be about 4.17 on average.


2019 ◽  
Vol 26 (3) ◽  
pp. 265-274 ◽  
Author(s):  
Shuyang Wang ◽  
Matthew G Nosworthy ◽  
James D House ◽  
Shannon-Hood Niefer ◽  
Michael T Nickerson

The effect of barrel temperature (120 and 150 ℃, held constant in zones 4–6) and feed moisture (20 and 24%) on the protein quality of Kabuli chickpea, sorghum, and maize flours were examined, which included amino acid profile, in vitro protein digestibility and in vitro protein digestibility-corrected amino acid score (IV-PDCAAS). It was found that the limiting amino acid of chickpea changed from threonine to valine after extrusion, whereas both sorghum and maize were limiting in lysine before and after extrusion. The in vitro protein digestibility increased from 77 to 81% for chickpea and 73 to 76% for maize; values for sorghum remained at 74% after extrusion. However, the IV-PDCAAS for the extruded flours generally remained at the same level, 69% for chickpea, 22% for sorghum, and ∼35% for maize. The effect of extrusion temperature, moisture and their interaction was significant on protein quality of sorghum and maize, but in the case of chickpea, only the extrusion temperature was significant. Only chickpea extruded at 150 ℃ (regardless of the moisture) met the protein quality (PDCAAS > 70%) requirement to be used in food assistance products.


2018 ◽  
Vol 2018 ◽  
pp. 1-8 ◽  
Author(s):  
Renata Pyz-Łukasik ◽  
Waldemar Paszkiewicz

This study determined the proximate composition, energy value, amino acid profile, and protein quality of the muscle tissue of four food fish species. The fish analyzed contained 78.90–69.89% water, 18.25–15.69% protein, and 2.28–12.57% fat. The energy value of the muscle tissue ranged from 93.50 to 175.83 kcal/100 g. The contents of amino acids in 100 g of protein were 47.64–45.86 g for total essential amino acids (TEAA), 52.36–54.14 g for total neutral amino acids (TNAA), 3.14–2.25 g for total sulphur amino acids (TSAA), and 7.23–7.81 g for total aromatic amino acids (TArAA). The essential amino acid (EAA) composition of the fish was compared with the standard protein, and Chemical Score (CS), Protein Digestibility-Corrected Amino Acid Score (PDCAAS), and Essential Amino Acid Index (EAAI) were calculated. The quality of the muscle tissue proteins of all four fish species was high. These fish can constitute a healthy addition to the human diet.


Author(s):  
Samy Fangus Sharobeem ◽  
Radomir Lásztity ◽  
Máté Hidvégi ◽  
András Salgó ◽  
Livia Simon-Sarkadi

Foods ◽  
2019 ◽  
Vol 8 (6) ◽  
pp. 199 ◽  
Author(s):  
Iris Joye

Protein digestibility is currently a hot research topic and is of big interest to the food industry. Different scoring methods have been developed to describe protein quality. Cereal protein scores are typically low due to a suboptimal amino acid profile and low protein digestibility. Protein digestibility is a result of both external and internal factors. Examples of external factors are physical inaccessibility due to entrapment in e.g., intact cell structures and the presence of antinutritional factors. The main internal factors are the amino acid sequence of the proteins and protein folding and crosslinking. Processing of food is generally designed to increase the overall digestibility through affecting these external and internal factors. However, with proteins, processing may eventually also lead to a decrease in digestibility. In this review, protein digestion and digestibility are discussed with emphasis on the proteins of (pseudo)cereals.


2015 ◽  
Vol 68 (1) ◽  
pp. 7487-7496 ◽  
Author(s):  
Piedad Margarita Montero Castillo ◽  
Yesid Alejandro Marrugo Ligardo ◽  
Lesbia Cristina Julio González

The future of nutrition in Colombia, and perhaps in other developing countries, will depend in large part on the ability of food technology to take full advantage of the food sources available in the country and to adapt and develop new products that will vary and complement the diets of the majority of the population at a low cost. The objective of this study was to evaluate the protein quality of rice-based drinks fortified with bovine and porcine blood plasma. Six treatments were prepared with different levels of fortification (14.5%, 18.5% and 29%). The effects of the plasma type and the addition levels on the protein content, the amino acid profile, and the in vitro digestibility of the drinks were observed. The AOAC method was employed for the determination of the protein content; the amino acid profile was created using HPLC. The protein digestibility was determined by subjecting a dispersion of the drink to the action of a multi-enzymatic solution. The protein content increased with the level of fortification. The drinks fortified with bovine plasma (104%) and porcine plasma (89%) presented a better protein quality index than the unfortified drink. The digestibility of the fortified drinks did not demonstrate significant improvements in comparison with the unfortified drink. The chemical score of the drinks fortified with porcine plasma (71.6) and bovine plasma (78.5) showed that the latter had the best nutritional quality.


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