Effect of barrel temperature and feed moisture on protein quality in pre-cooked Kabuli chickpea, sorghum, and maize flours

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.

2020 ◽  
pp. 34-42
Author(s):  
V. C. Wabali ◽  
S. Y. Giami ◽  
D. B. Kiin- Kabari ◽  
O. M. Akusu

The objective of this work was to evaluate the Amino Acid profile/score and In-vitro protein digestibility of composite biscuits produced from blends of Wheat flour (WHF), African breadfruit flour (ABF)and Moringa seed flour(MSF) at the following ratios (Sample A: WHF 100%: ABF 0; MSF 0, B= WHF 77.5%:ABF 20%: MSF 2.5%, C=WHF 75%: ABF 20%: MSF 5.0%, D= WHF 72.5%: ABF 20%: MSF 7.5%. E = WHF 70%: ABF 20%: MSF 10%, F = WHF 90%: ABF 0: MSF 10%, G = WHF 80%: ABF 20%: MSF 0). The most predominant Amino Acid in ABF was glutamic (12.27 g/100 g) followed by Aspartic and lysine, with values of 8.96 g/100 g and 6.55 g/100 g, respectively. Glutamic Acid content of the biscuits ranged from 10.96 g/100 g – 12.96 g/100 g, with sample B giving significantly higher value. Substitution with MSF resulted in decreasing glutamic acid content levels in the formulated biscuits, while lysine, phenylalanine and Isoleucine improved with the addition of 10% Moringa seed flour. Amino acid Scores of the biscuits using Hen egg as standard showed that whole egg had a higher amino acid score except glycine (1.04 – 1.25). Percentage In-vitro protein digestibility ranged from 10.64% - 47.33%, showing that addition of moringa seed flour and African breadfruit flour improved digestibility values from 10.64% to 47.33% for sample E with the control sample (wheat flour biscuit) being significantly lower. Substitution with ABF and MSF improved protein digestibility of the produced biscuits. Also, the Amino acid scores of the formulated biscuits were higher than the FAO recommended daily dietary requirements for Amino acids.


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.


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

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.


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