Countercurrent extraction-isoelectric precipitation of sunflower seed protein isolates

1981 ◽  
Vol 32 (2) ◽  
pp. 166-174 ◽  
Author(s):  
Fakhriya S. Taha ◽  
Mehassen Abbasy ◽  
Ahmed S. El-Nockrashy ◽  
Zein E. Shoeb
Keyword(s):  
Sunflower Seed ◽  
Seed Protein ◽  
Countercurrent Extraction ◽  
Isoelectric Precipitation ◽  
Protein Isolates

Rapeseed protein isolates by countercurrent extraction and isoelectric precipitation

1977 ◽  
Vol 25 (1) ◽  
pp. 193-197 ◽  
Author(s):  
Ahmad S. El Nockrashy ◽  
Kumar D. Mukherjee ◽  
Helmut K. Mangold
Keyword(s):  
Countercurrent Extraction ◽  
Isoelectric Precipitation ◽  
Protein Isolates ◽  
Rapeseed Protein

scholarly journals Effect of free amino acids and peptide hydrolysates from sunflower seed protein on the formation of pyrazines under different heating conditions

RSC Advances ◽  
2021 ◽  
Vol 11 (45) ◽  
pp. 27772-27781
Author(s):  
Furong Wang ◽  
Hailiang Shen ◽  
Xi Yang ◽  
Ting Liu ◽  
Yali Yang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Maillard Reaction ◽  
Free Amino Acids ◽  
Free Amino ◽  
Sunflower Seed ◽  
Seed Protein ◽  
Heating Temperature ◽  
Reaction Model

Exploring the effect of heating temperature and time on the formation of pyrazines; revealing the potential roles of FAAs and hydrolyzed sunflower seed peptides in the Maillard reaction model.

scholarly journals Functional Properties of Alstonia scholaris Seed Protein Isolates

2014 ◽  
Vol 26 (7) ◽  
pp. 1969-1973
Author(s):  
Mita Dutta ◽  
Subrata Laskar ◽  
Pinak Dutta
Keyword(s):  
Functional Properties ◽  
Seed Protein ◽  
Protein Isolates ◽  
Alstonia Scholaris

scholarly journals Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 703
Author(s):  
Hristo Kalaydzhiev ◽  
Radoslav Georgiev ◽  
Petya Ivanova ◽  
Magdalena Stoyanova ◽  
Cristina L. M. Silva ◽  
...  
Keyword(s):  
Protein Solubility ◽  
Rapeseed Meal ◽  
Protein Isolate ◽  
Protein Fractions ◽  
Isoelectric Precipitation ◽  
Protein Isolates ◽  
Sds Page ◽  
Enhanced Solubility ◽  
Meal Protein ◽  
Biochemical Analyses

The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5–8.5 contained a higher amount of crude protein (72.84%) than PI10.5–2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5–2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5–2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5–8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5–2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5–8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5–8.5, while the solubility of PI10.5–2.5 was increased. The supplementation of PI10.5–2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates.

Low phytate, low chlorogenic acid sunflower seed protein concentrate

Nahrung/Food ◽  
1981 ◽  
Vol 25 (8) ◽  
pp. 759-764 ◽  
Author(s):  
F. S. Taha ◽  
A. S. Elnockrashy
Keyword(s):  
Chlorogenic Acid ◽  
Sunflower Seed ◽  
Seed Protein ◽  
Protein Concentrate
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