In-vitro protein and sulphur amino acid availability as a measure of bean protein quality

1992 ◽  
Vol 59 (4) ◽  
pp. 497-504 ◽  
Author(s):  
Luisa Marletta ◽  
Marina Carbonaro ◽  
Emilia Carnovale
Author(s):  
Samy Fangus Sharobeem ◽  
Radomir Lásztity ◽  
Máté Hidvégi ◽  
András Salgó ◽  
Livia Simon-Sarkadi

Foods ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1531
Author(s):  
Yanwen Wang ◽  
Sean M. Tibbetts ◽  
Fabrice Berrue ◽  
Patrick J. McGinn ◽  
Scott P. MacQuarrie ◽  
...  

The present study was conducted to evaluate the protein quality of microalgae species Chlorella vulgaris (CV), Chlorella sorokiniana (CS), and Acutodesmus obliquus (AO) and assess the impact of mechanical cell wall disruption. Male Sprague–Dawley rats, around 156 g after adaptation, were placed in metabolic cages and fed experimental diets that were either protein-free or contained 10% protein solely from one of the undisrupted or disrupted CV, CS, and AO. After 3 days, feces were collected for a period of 5 days and analyzed together with diet samples for crude protein contents. Apparent protein digestibility, true protein digestibility, amino acid score, and protein digestibility-corrected amino acid score were calculated. In vitro protein digestibility was measured using the pepsin–pancreatin method and the in vitro protein digestibility-corrected amino acid score was calculated. The crude protein contents of CV, CS, and AO were 53.5, 50.2, and 40.3%, respectively. The amino acid score of the first limiting amino acid was 1.10, 1.27, and 0.86, true protein digestibility was 64.7, 59.3, and 37.9% and protein digestibility-corrected amino acid score was 0.63, 0.64, and 0.29, respectively, for CV, CS, and AO. Mechanical cell disruption significantly improved protein digestibility without a substantial impact on the amino acid profile and score, resulting in the increase of protein digestibility-corrected amino acid score to 0.77, 0.81, and 0.46, respectively, for disrupted CV, CS, and AO. There was a strong correlation between in vitro protein digestibility and apparent protein digestibility (r = 0.986), and also between in vitro protein digestibility-corrected amino acid score and in vivo protein digestibility-corrected amino acid score (r = 0.994). The results suggest that the CV and CS are acceptable sources of protein for humans and animals and quality can be markedly improved by mechanical cell wall disruption. Additionally, in vitro protein digestibility measured using the pepsin–pancreatin method may be used to screen protein product candidates, save animals, reduce cost, and accelerate product development.


2021 ◽  
Vol 51 (3) ◽  
pp. 203-210
Author(s):  
Mustafa Yaman ◽  
Hafsa Sena Sargın ◽  
Ömer Faruk Mızrak ◽  
Halime Uğur ◽  
Jale Çatak ◽  
...  

The aim of this study was to determine the amino acid content and in vitro protein digestibility of breakfast cereals and evaluate their protein quality using in vitro protein digestibility-corrected amino acid score (PDCAAS) methods. Statistically big differences were found in the proportions of essential amino acids between breakfast cereals. Higher protein digestibility was found in samples containing rice and corn than those containing oats. The first limiting amino acid score (AAS) in 6 out of 12 samples was methionine + cysteine, in 4 out of 12 samples was lysine, and in 2 out of 12 samples was tryptophan. According to the first limiting AAS, the in vitro PDCAAS ranged from 0.19±0.01 to 0.86±0.02 in breakfast cereals. When we evaluated the first limiting AAS, lysine, methionine+cysteine and tryptophan predominantly determined PDCAAS. As a result, the PDCAAS, which is an indicator of protein quality, was generally low in breakfast cereal products.


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.


1979 ◽  
Vol 41 (3) ◽  
pp. 559-571 ◽  
Author(s):  
S. C. Achinewhu ◽  
D. Hewitt

1. A comparative study was made of two biological techniques for assessing protein quality in wheat and barley, and in a soya-bean-protein isolate both as received, and after being heat damaged by autoclaving. Amino acid digestibility was determined by the ‘ileal’ analysis technique while amino acid availability was measured in growth assays. Some chemical and microbiological tests were also done.2. Heat treatment of the soya-bean-protein isolate caused little change in amino acid composition but the digestibility of all amino acids and the availability of lysine and methionine were severely reduced, lysine being most affected. The reduced availability of lysine was not entirely attributable to impaired digestibility.3. The amino acids in wheat and barley were highly digestible. The availability of methionine and lysine in barley and of methionine in wheat was high, whereas the availability of lysine in wheat was apparently much lower.4. The results showed that for methionine, digestibility values are a fair measure of the availability. In heat-damaged soya-bean-protein isolate however, digestibility of lysine over-estimated the availability, indicating that amino acid digestibility may sometimes provide a misleading indication of nutritional value.


1999 ◽  
Vol 50 (5) ◽  
pp. 889 ◽  
Author(s):  
V. Ravindran ◽  
Wayne L. Bryden

Methodology to evaluate the protein quality or amino acid availability in feed ingredients for poultry using in vitro (enzymic, chemical, or microbiological assays), indirect in vivo (plasma amino acid assays), or direct in vivo (growth or digestibility assays) measurements has been reviewed. The specific applications and limitations of these methods are examined. In vitro assays are useful in providing information on heat damage in selected protein sources under defined conditions, and on relative ranking of different samples, but they cannot form the basis of practical feed formulations. While growth assays remain the only direct means of confirming nutritional relevance of values obtained by other procedures, in vivo digestibility assays appear to be most useful, at present, to estimate amino acid availability. Amino acid digestibility assays in poultry should be based on the analysis of digesta from the terminal ileum rather than excreta, because of the variable and modifying effects of hindgut microflora. Techniques used to estimate endogenous amino acid losses in poultry are discussed. The needs for correction of endogenous losses in amino acid digestibility calculations and the relative merits of apparent and true digestible amino acid systems are still being debated. It is, however, clear that both digestible amino systems are superior to the total amino acid system currently employed to formulate practical diets. Digestible amino acid values are likely to form the basis of poultry feed formulations in the future. In particular, there is an urgent need for more precise information on the variation in digestible amino acid contents of locally grown ingredients and on the factors causing this variation (e.g. variety, location, season, agronomic practices, processing, etc.).


1991 ◽  
Vol 58 (4) ◽  
pp. 431-441 ◽  
Author(s):  
Thérèse Desrosiers ◽  
Laurent Savoie

SummaryThe effect of heat treatments, at various water activities (αw), on digestibility and on the availabilities of amino acids of whey protein samples in the presence of lactose was estimated by an in vitro digestion method with continuons dialysis. Four αw (0·3, 0·5, 0·7 and 0·97), three temperatures (75, 100 and 121 °C) and three heating periods (50, 500 and 5000 s) were selected. The initial lysine: lactose molar ratio was 1:1. Amino acid profiles showed that excessive heating of whey (121 °C, 5000 s) destroyed a significant proportion of cystine at all αw, lysine at αw 0·3, 0·5 and 0·7, and arginine at αw 0·5 and 0·7. At αw 0·3, 0·5 and 0·7, protein digestibility decreased (P < 0·05) as the temperature increased from 75 to 121 °C for a heating period of 5000 s, and as the heating time was prolonged from 500 to 5000 s at 121 °C. Excessive heating also decreased (P < 0·05) the availabilities of ail amino acids at αw 0·3, 0·5 and 0·7. The availabilities of lysine, proline, aspartic acid, glutamic acid, threonine, alanine, glycine and serine were particularly affected. Severe heating at αw 0·97 did not seem to favour the Maillard reaction, but the availabilities of cystine, tyrosine and arginine were decreased, probably as a result of structural modifications of the protein upon heating. Heating whey protein concentrates in the presence of lactose not only affected lysine, but also impaired enzymic liberation of other amino acids, according to the severity of heat treatments and αw.


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