scholarly journals Techno-Functional, Nutritional and Environmental Performance of Protein Isolates from Blue Lupin and White Lupin

Foods ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 230 ◽  
Author(s):  
Martin Vogelsang-O’Dwyer ◽  
Juergen Bez ◽  
Iben Lykke Petersen ◽  
Marcel Skejovic Joehnke ◽  
Andreas Detzel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Environmental Impacts ◽  
Milk Powder ◽  
Protein Isolate ◽  
White Lupin ◽  
Trypsin Inhibitor Activity ◽  
Foaming Properties ◽  
Protein Isolates ◽  
Lupin Protein

Similarly prepared protein isolates from blue lupin (Lupinus angustifolius) and white lupin (L. albus) were assessed in relation to their composition, functional properties, nutritional attributes and environmental impacts. Blue lupin protein isolate (BLPI) and white lupin protein isolate (WLPI) were found to be quite similar in composition, although differences in the electrophoretic protein profiles were apparent. Both lupin protein isolates (LPIs) had good protein solubility (76.9% for BLPI and 69.8% for WLPI at pH 7) and foaming properties. However, a remarkable difference in heat gelation performance was observed between BLPI and WLPI. WLPI had a minimum gelling concentration of 7% protein, whereas BLPI required 23% protein in order to form a gel. WLPI also resulted in stronger gels over a range of concentrations compared to BLPI. Nutritional properties of both LPIs were similar, with no significant differences in in vitro protein digestibility (IVPD), and both had very low trypsin inhibitor activity (TIA) and fermentable oligo-, di- and monosaccharides, and polyols (FODMAP) content. The amino acid profiles of both LPIs were also similar, with sulfur-containing amino acids (SAAs) being the limiting amino acid in each case. Environmental impacts revealed by the life cycle assessment (LCA) were almost identical for BLPI and WLPI, and in most categories the LPIs demonstrated considerably better performance per kg protein when compared to cow’s whole milk powder.

scholarly journals Functional properties of protein isolates from camelina (Camelina sativa (L.) Crantz) and flixweed (sophia, Descurainis sophia L.) seed meals

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Na Thi Ty Ngo ◽  
Fereidoon Shahidi
Keyword(s):  
Functional Properties ◽  
Protein Extraction ◽  
Protein Profile ◽  
Protein Solubility ◽  
Protein Isolate ◽  
Absorption Capacity ◽  
Foaming Properties ◽  
Oil Absorption ◽  
Protein Isolates ◽  
Water Holding

AbstractCamelina and flixweed (sophia) seed protein isolates were prepared using both the conventional extraction and ultrasonic-assisted extraction methods at 40 kHz for 20 min, and their functional properties investigated. SDS-PAGE showed that both ultrasound-assisted and conventional extractions resulted in a similar protein profile of the extract. The application of ultrasound significantly improved protein extraction/content and functional properties (water holding capacity, oil absorption capacity, emulsifying foaming properties, and protein solubility) of camelina protein isolate and sophia protein isolate. The water-holding and oil absorption capacities of sophia protein isolate were markedly higher than those of camelina protein isolate. These results suggest that camelina protein isolate and sophia protein isolate may serve as natural functional ingredients in the food industry. Graphical Abstract

scholarly journals Nutritional quality evaluation of Whitemouth croaker (Micropogonias furnieri) protein isolate

2014 ◽  
Vol 44 (2) ◽  
pp. 134-143
Author(s):  
William Renzo Cortez-Vega ◽  
Irene Rodrigues Freitas ◽  
Sandriane Pizato ◽  
Carlos Prentice
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nutritional Quality ◽  
Troponin I ◽  
Essential Amino Acids ◽  
Protein Isolate ◽  
Content Type ◽  
Sds Page ◽  
Apparent Bioavailability

Purpose – The purpose of this study was to isolate Whitemouth croaker protein by alkaline solubilization process and evaluate their nutritional quality to evaluate the bioavailability of essential amino acids. Design/methodology/approach – The proximate composition, essential amino acid composition, in vitro digestibility, apparent bioavailability, chemical score of amino acids and SDS-PAGE were determined for the isolated croaker proteins. Findings – The isolated protein showed a high level of protein 92.21 percent and low amount of lipids 0.57 percent. The protein is rich in lysine and leucine, 108.73 and 96.75 mg/g protein, respectively. The protein isolate had high digestibility, 94.32 percent, which indicates proper utilization of this protein source, while the tryptophan had lower bioavailability (12.58 mg amino acid/mg protein). The high chemical scores were found for the amino acids lysine, methionine+cysteine (6.79 and 5.14). SDS-PAGE of proteins extracted showed appearance of the heavy chain of myosin (220 kDa), actin (50 kDa) and other fractions, with molecular weight between 20 and 50 kDa, such as troponin I, C and T. Originality/value – The products obtained from croaker muscle can be incorporated as a high value supplements in human diets. The isolated protein exhibited a high content of essential amino acids and digestibility, indicating that the protein has a high nutritional quality.

White lupin protein isolate as a foaming agent

1998 ◽  
Vol 207 (2) ◽  
pp. 91-96 ◽  
Author(s):  
A. Raymundo ◽  
J. Empis ◽  
I. Sousa
Keyword(s):  
Protein Isolate ◽  
White Lupin ◽  
Foaming Agent ◽  
Lupin Protein

scholarly journals Detection of Genistein in Soy Protein Isolate and Soymilk Powder by Spectrophotometric and Chromatographic Method

2019 ◽  
Vol 11 ◽  
pp. 69-73
Author(s):  
Md. Anisur Rahman Mazumder ◽  
Parichat Hongsprabhas
Keyword(s):  
Soy Protein ◽  
Cultured Cells ◽  
Soy Protein Isolate ◽  
Milk Powder ◽  
Density Lipoprotein ◽  
Inhibitory Effect ◽  
Protein Isolate ◽  
Hplc Method ◽  
Spectrophotometric Methods

Genistein proposed as a treatment for osteoporosis for postmenopausal women, elderly men, lowering cardiovascular disease and reduces hormone dependent cancers. Genistein also exerted inhibitory effect on lipid peroxidation induced in vitro by pro-oxidant agents on model and natural membranes on cultured cells and on low density lipoprotein. Genistein detection in soy products is very much important for Food Scientist. Gensitein can be detected by UV-Visible spectrophotometric and HPLC method. This study focused on the detection of genistein by HPLC and spectrophotometric methods. Genistein content of both soy protein isolate (SPI) and spray dried soy milk powder (SMP) was determined by spectrophotometry (93.12±1.15 and 74.78±0.75 mg/100g, respectively) were slightly higher but not significantly differ than HPLC analysis (89.67±5.16 and 72.34±0.27 mg/100g, respectively). This study suggested that genistein and its glycoside could be detected by spectrophotometric methods with high accuracy.

scholarly journals Differences in Amino Acid Digestibility and Protein Quality Among Various Protein Isolates and Concentrates Derived from Cereal Grains, Plant and Dairy Proteins

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 681-681 ◽  
Author(s):  
Hannah Bailey ◽  
Hans Stein
Keyword(s):  
Amino Acid ◽  
Protein Quality ◽  
Soy Protein Isolate ◽  
Brown Rice ◽  
Latin Square ◽  
Protein Isolate ◽  
Plant Protein ◽  
Cereal Grains ◽  
Experimental Unit ◽  
Protein Isolates

Abstract Objectives The objectives of this research were to use the growing pig as a model to determine the amino acid (AA) digestibility and protein quality by the digestible indispensable amino acid score (DIAAS) for brown rice concentrate (BRPC), pea protein concentrate (PPC), two rapeseed protein isolates (RSP-1 and RSP-2), soy protein isolate (SPI), and whey protein isolate (WPI). Methods Seven ileal cannulated barrows (36.5 ± 1.6 kg) were randomly allotted to a 7 × 7 Latin square design with 7 diets and seven 7-d periods, with ileal digesta collected on d 6 and 7. Each protein ingredient was included in a diet as the only AA containing source, and a nitrogen-free diet was used to measure basal endogenous losses of AA. The DIAAS were calculated for children from 6 months to 3 years and for persons > 3 years according to the Food and Agriculture Organization. Data were analyzed using the PROC MIXED of SAS in a completely randomized design with the pig as the experimental unit. Results The standardized ileal digestibility (SID) of Arg, His, Ile, Leu, and Phe was greater (P < 0.05) for WPI compared with the other proteins, and the SID of Thr and Trp did not differ among WPI, SPI, and RSP-2. The SID of all indispensable AA (IAA), expect Arg and Lys, was greater (P < 0.05) for RSP-2 than for PPC and BRPC, and PPC and BRPC had a greater (P < 0.05) SID of most IAA, expect His, Lys, and Met, than RSP-1. For DIAAS, RSP-2 had a DIAAS greater than 100 for children 6 months to 3 years, whereas, for persons > 3 years, RSP-2 and WPI had DIAAS greater than 100, i.e., 110 and 117, respectively. For both reference patterns, the DIAAS for RSP-2 and WPI was greater (P < 0.05) than for SPI, and the DIAAS for RSP-1 was less (P < 0.05) than the DIAAS for SPI but greater (P < 0.05) than for PPC, and PPC had a DIAAS greater (P < 0.05) than BRPC. Conclusions Results of this research illustrate that WPI is an excellent dairy protein for persons >3 years, and RSP-2 is an excellent quality plant protein for children from 6 months to 3 years and persons >3 years. In contrast, protein concentrates from cereal grains and some plant proteins, i.e., BRPC and PPC, respectively, are lower quality proteins, but soy based plant protein isolates, i.e., SPI, may be considered good quality proteins for children from 6 months to 3 years and persons >3 years. Funding Sources DSM animal nutrition and health.

scholarly journals PSIX-2 Amino acid digestibility and digestible indispensable amino acid scores of a few protein isolates and concentrates derived from cereal grains, plant proteins, or dairy proteins

2020 ◽  
Vol 98 (Supplement_3) ◽  
pp. 186-187
Author(s):  
Hannah M Bailey ◽  
Hans H Stein
Keyword(s):  
Amino Acid ◽  
Block Design ◽  
Brown Rice ◽  
Latin Square ◽  
Protein Isolate ◽  
Experimental Unit ◽  
Protein Concentrate ◽  
Protein Isolates ◽  
Excellent Quality ◽  
Indispensable Amino Acid

Abstract The objective of this experiment was to determine standardized ileal digestibility (SID) of amino acid (AA) and digestible indispensable amino acid scores (DIAAS) for brown rice protein concentrate (BRPC), pea protein concentrate (PPC), two rapeseed protein isolates (RSP-1 and RSP-2), soy protein isolate (SPI), and whey protein isolate (WPI). Seven cannulated barrows (36.51 ± 1.61 kg) were randomly allotted to a 7 × 7 Latin square design and fed a diet containing each protein as the sole source of AA. A nitrogen-free diet was also used. The DIAAS was calculated for children from 6-mo to 3-yr and persons >3-yr. Data were analyzed using PROC MIXED of SAS in a randomized complete block design with pigs as the experimental unit. Among proteins, WPI had the greatest (P < 0.05) SID of all indispensable AA (IAA), except Lys and Thr, and RSP-1 had the least (P < 0.05) SID of most IAA. The SID of all AA, except Leu and Met, did not differ between RSP-2 and SPI, and the SID of all IAA, except Arg and Lys, was greater (P < 0.05) for RSP-2 than for PPC and BRPC. For DIAAS (Table 1), RSP-2 was the only protein with a DIAAS greater than 100 for children 6-mo to 3-yr, and both RSP-2 and WPI had a DIAAS greater than 100 for persons >3-yr. For both reference patterns, the DIAAS for RSP-2 and WPI was greater (P < 0.05) than for SPI. The DIAAS for RSP-1 was less (P < 0.05) than for SPI and greater (P < 0.05) than for PPC, which had a DIAAS greater (P < 0.05) than BRPC. In conclusion, RSP-2 resulted in an excellent quality protein for persons >6-mo, and WPI is an excellent quality protein for persons >3-yr.

scholarly journals Characterization of okra seed flours, protein concentrate, protein isolate and enzymatic hydrolysates

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Anastasia Amaka Nnamezie ◽  
Akinsola Albert Famuwagun ◽  
Saka Olasunkanmi Gbadamosi
Keyword(s):  
Protein Hydrolysate ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Protein Isolate ◽  
Foaming Properties ◽  
World Population ◽  
Protein Concentrate ◽  
Post Harvest ◽  
Seed Flours

Abstract The need to feed the increasing world population with high quality protein and the enormous post-harvest losses of okra fruits necessitated the research on okra seeds in this study. Whole flour (WF) of matured okra seed was processed to obtain defatted flour (DF), protein concentrate (PC) and protein isolate (PI), followed by hydrolysis of the protein isolate by three different proteases; pepsin (PHp), pancreatin (PHc) and trypsin (PHT) to produce hydrolysates. The okra seed flours, proteins and the hydrolysates were analyzed for changes in the functional groups using Fourier, Transform Infrared (FTIR), amino acid composition, solubility profile and some functional properties. The FTIR results showed the presence of N-H stretching, C=O stretching, C=N stretching N-H bending and C-N stretching in the samples. Protein hydrolysate had higher essential amino acids (51.32–53.01%) than unhydrolysed samples (36.31–37.99%). PI and WF had the highest water absorption and swelling capacities respectively. The solubility profiles of the samples were minimal at pH 2–4 and then increased after the isoelectric point. The PC was more soluble than PI between pH 2–8. The foaming properties of the samples was least in the absence of salt but high in the presence of 0.5 M sodium chloride. The emulsion capacity of the samples was least in the presence of 1.0 M NaCl. The in-vitro protein digestibility results showed that okra seed protein hydrolysates were more digestible (83.26–86.08%) than unhydrolyzed proteins (36.48–80.90%). The results of the antioxidant properties showed that PHp and PHT exhibited better radical scavenging and metal chelating activities respectively than the other samples. The study concluded that okra seed proteins and hydrolysates demonstrated potentials as ingredients in functional food preparation and this may be considered as a strategy to reducing the post-harvest losses of okra fruit and subsequently feeding the world with quality proteins. Graphical abstract

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