scholarly journals Functional Properties of Defatted Roselle (Hibiscus sabdariffa L.) Seeds Protein and Its Hydrolysates

Author(s):  
Fatoumata Tounkara ◽  
Issiaka Togola ◽  
Lassana Sissoko ◽  
Mah Moutaga Fane ◽  
Nouhoum Diarra ◽  
...  

Aim: The purpose of this study was to evaluate the functional properties of Roselle seed protein isolates and its hydrolysates. Place and Duration of Study: The Roselle seeds were collected in Koutiala (Mali), in November 2018. All analysis were conducted in the Faculty of Sciences and Technics, particularly in the Laboratory of Plant and Food Biochemistry and Biotechnology from January to June 2019.   Methodology: The effect of enzymatic hydrolysis on the functional properties of Roselle seed protein (RSP) was investigated. Defatted Roselle seed flour was used to extract the protein isolates. The protein was digested for 2 hours and 3 hours using pepsin followed by pancreatin. Results: The 2 hours and 3 hours Roselle seed protein hydrolysates (RSPH2, RSPH3) compare to RSPI, exhibited a good foaming capacity of 300, 315 and 165% respectively. The water holding capacity (WHC) of the RSPI, RSPH2 and the RSPH3 were 2, 2.5 and 2.2 ml/g respectively. The oil holding capacity ranged from 5.75 to 5.32 ml/g, the emulsifying capacity of the RSPH2 was higher than that of the RSPH3 and the RSPI, 105, 97 and 82 ml/g respectively. Conclusion: The ability of pepsin and pancreatin hydrolysates to be functional is primarily due to their soluble peptide content. The samples have good functional properties. These results proposed that pepsin and pancreatin hydrolysates could be useful as whole or partial replacement of high-price materials such as egg albumen and casein.

2012 ◽  
Vol 443-444 ◽  
pp. 660-665 ◽  
Author(s):  
Zhi Dong Liu ◽  
Ben Heng Guo ◽  
Mi Ya Su ◽  
Yin Yu Wang

The effect of ultrasonic treatment on some functional properties whey protein isolates (WPIs) was investigated. The water holding capacity of WPIs treated by ultrasound was not significantly changed. The oil holding capacity of WPIs treated by ultrasonic was significantly higher than that by untreated by ultrasonic, especially the power of 50 %. The foaming capacity of WPIs treated by ultrasonic was higher than that by untreated by ultrasonic, while the foaming stability of WPIs treated by ultrasonic was higher than that by untreated by ultrasonic.The emulsifying capacity is almost unchanged. These results showed that ultrasonic treatment could effectively affected some functional properties of WPIs be associated with the sonication time and power density. Therefore, some functional properties of WPIs can be modified by ultrasonic treatment.


2014 ◽  
Vol 26 (7) ◽  
pp. 1969-1973
Author(s):  
Mita Dutta ◽  
Subrata Laskar ◽  
Pinak Dutta

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Na Thi Ty Ngo ◽  
Fereidoon Shahidi

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


2013 ◽  
Vol 10 (1) ◽  
pp. 65
Author(s):  
Normah Ismail ◽  
Najihah Shukor ◽  
Zainal Samicho

Silver catfish (Pangasius sutchi) skin gelatin was extracted to determine the effects of extraction time on the functional properties of the gelatin in terms of solubility, protein solubility as a function of pH and sodium chloride concentration, emulsifying capacity and stability, water holding capacity, fat binding capacities and foaming properties. Silver catfish skins were washed in sodium chloride (NaCl) solution prior to pre-treatment in sodium hydroxide (NaOH) and acetic acid solution. Gelatin was extracted at 50ºC for 6, 8, 10 and 12 hours extraction time followed by freeze drying. The extraction of silver catfish skin gelatin at 50 ºC for 12 hours was more effective than extraction at 6, 8 and 10 hours where the gelatin was characterized by higher emulsifying capacity (52.63%), emulsifying stability (47.83%), water holding capacity (31.78 mL/g), fat binding capacities (54.76%), foaming capacity (41.47 mL) and foaming stability (56.42%) than gelatins extracted at other extraction time. The longer the extraction time, the better the functional properties of the gelatin. Based on its good functional properties, silver catfish skin gelatin may be useful in various food applications such as soups, sauces and gravies.


2021 ◽  
Author(s):  
Fengzhang Wang ◽  
Yan Ma ◽  
Yongtao Wang ◽  
Liang Zhao ◽  
Xiaojun Liao

Abstract: Pepper seed is one by-product in pepper processing, rich in protein, fat, and fiber, which is a new plant-based protein source. In this paper, the physicochemical and functional properties...


2014 ◽  
Vol 55 ◽  
pp. 173-179 ◽  
Author(s):  
Mila P. Hojilla-Evangelista ◽  
Gordon W. Selling ◽  
Mark A. Berhow ◽  
Roque L. Evangelista

2011 ◽  
Vol 236-238 ◽  
pp. 2647-2650
Author(s):  
Guo Qin Liu ◽  
Xiao Jun Liu ◽  
Lin Li ◽  
Bing Li

The effects of frozen storage time on the functional properties of frozen wheat gluten were evaluated. The frozen wheat gluten was subjected to frozen storage in refrigerator at-18°C for 0–120days. The samples were obtained by the process of freeze-drying. The main functional properties of frozen wheat gluten were determined to confirm the effects of frozen storage time on functional properties of frozen wheat gluten. Results showed that solubility, water-holding capacity, emulsifying capacity, foamability and foam stability of frozen wheat gluten decreased and that oil-holding capacity, emulsion stability of frozen wheat gluten were improved with prolonged frozen storage time.


2011 ◽  
Vol 17 (2) ◽  
pp. 119-126 ◽  
Author(s):  
L. Chel-Guerrero ◽  
S. Gallegos-Tintoré ◽  
A. Martínez-Ayala ◽  
A. Castellanos-Ruelas ◽  
D. Betancur-Ancona

Functional properties were identified for the total globulin (TG), 7S and 11S fractions of Lima bean ( Phaseolus lunatus L.) seeds. The 11S component accounted for 58.3% of TGs and the 7S for 41.7%. Solubility was higher in the 7S fraction, especially at alkaline pHs. Water-holding capacity was similar (3 g water/g sample) in both globulin fractions. Oil-holding capacity was higher in the 11S fraction, which also exhibited better foaming capacity and foam stability than the 7S and TG fractions at alkaline pHs. The TG and 7S fractions exhibited low emulsifying capacity and emulsion stability at different pHs (5, 7 and 9), but the 11S fraction had relatively higher values. In suspension at low concentrations, all fractions exhibited shear-thinning (pseudoplastic) behavior. The studied Lima bean globulin fractions exhibit functional properties which make them potentially apt for use in some industrial food systems.


Foods ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 678 ◽  
Author(s):  
Katharina Schlegel ◽  
Anika Leidigkeit ◽  
Peter Eisner ◽  
Ute Schweiggert-Weisz

Lupin protein isolate was fermented with eight different microorganisms to evaluate the influence on sensory profile, techno-functional properties and protein integrity. All investigated microorganisms were able to grow in lupin protein isolate. The results showed that the foaming activity in the range of 1646–1703% and the emulsifying capacity in the range of 347–595 mL of the fermented lupin protein isolates were similar to those of the unfermented ones. Protein solubility at pH 4 showed no significant changes compared to unfermented lupin protein isolate, whereas the solubility at pH 7 decreased significantly from 63.59% for lupin protein isolate to solubilities lower than 42.35% for fermented lupin protein isolate. Fermentation with all microorganisms showed the tendency to decrease bitterness from 2.3 for lupin protein isolate (LPI) to 1.0–2.0 for the fermented ones. The most promising microorganisms for the improvement of the sensory properties of lupin protein isolates were Lactobacillus brevis as it reduced the intensity of characteristic aroma impression (pea-like, green bell pepper-like) from 4.5 to 1.0. The SDS-PAGE results showed the fermentation treatment appeared not to be sufficiently effective to destruct the protein integrity and thus, deplete the allergen potential of lupin proteins. Fermentation allows the development of food ingredients with good functional properties in foam formation and emulsifying capacity, with a well-balanced aroma and taste profile.


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