Effects of combined treatment with ultrasound and pH shifting on foaming properties of chickpea protein isolate

2021 ◽  
pp. 107351
Author(s):  
Yuntao Wang ◽  
Shasha Wang ◽  
Rui Li ◽  
Yingjuan Wang ◽  
Qisen Xiang ◽  
...  
2015 ◽  
Vol 26 ◽  
pp. 48-55 ◽  
Author(s):  
Rocío Morales ◽  
Karina D. Martínez ◽  
Víctor M. Pizones Ruiz-Henestrosa ◽  
Ana M.R. Pilosof

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 3 (1) ◽  
pp. 87 ◽  
Author(s):  
Quirino Dawa ◽  
Yufei Hua ◽  
Moses Vernonxious Madalitso Chamba ◽  
Kingsley George Masamba ◽  
Caimeng Zhang

<p>Understanding how foaming properties of proteins are affected by factors such as pH, salt concentration and temperature is essential in predicting their performance and utilisation. In this study, the effects of pH and salt concentration were studied on the foaming properties of pumpkin seed protein isolate (PSPI) and PSPI- xanthan (XG)/Arabic (GA) gum blends. The foaming properties of the PSPI-GA/XG blends were also compared with egg white. Foam stability (FS) was significantly affected by pH with PSPI: GA (25:4) and PSPI: XG (25:1) having a significantly higher stability at pH 2 with the lowest foam stability at pH 4. Sodium chloride (0.2-1.0 M) did not significantly affect foaming properties although PSPI: GA (25:4) had the highest FC (89.33 ± 3.24%) and FS (76.83 ± 1.53 min) at 0.2 M sodium chloride concentration. The foaming capacity (FC) of PSPI: GA (25:4) blend (128.00 ± 0.91%) was significantly higher (<em>p </em><em>&lt; </em>0<em>.</em>05) than that of egg white (74.00 ± 1.33%) but its FS was significantly lower. It was further revealed that the FC of egg white (74.00 ± 1.33%) was comparable to the PSPI:XG (25:1) blend (74.00 ± 1.46%) but the FS for egg white (480.00 ± 2.67 min) was significantly higher (<em>p </em><em>&lt; </em>0<em>.</em>05) than the FS (116.21 ± 0.86 min) of PSPI:XG (25:1). The foaming properties of PSPI and PSPI-xanthan (XG)/Arabic (GA) blends were significantly affected by pH. Optimum foaming properties, PSPI:XG (25:1) and PSPI:GA (25:4) were observed at pH 2 and heat treatment temperature of 80 ºC.</p>


2020 ◽  
Vol 27 (1) ◽  
pp. 3-12
Author(s):  
Prasanth KS Pillai ◽  
Yulinglong Ouyang ◽  
Andrea K Stone ◽  
Michael T Nickerson

This research examines changes to the functional (solubility, emulsifying and foaming) properties of pea protein isolate when complexed with commercial citrus pectin of different structural attributes. Specifically, a high methoxy (P90; degree of esterification: 90.0%; degree of blockiness: 64.5%; galacturonic acid content 11.4%) and low methoxy (P29; degree of esterification: 28.6%; degree of blockiness: 31.1%; galacturonic acid: 70%) pectin at their optimum mixing ratios with pea protein isolate (4:1 pea protein isolate to P90; 10:1 pea protein isolate to P29) were assessed at the pHs associated with critical structure forming events during the complexation process (soluble complexation (pHc), pH 6.7 and 6.1; insoluble complex formation (pHϕ1), pH 4.0 and 5.0; maximum complexation (pHopt), pH 3.5 and 3.8; dissolution of complexes, pH 2.4 and 2.1; for admixtures of pea protein isolate–P90 and pea protein isolate–P29, respectively). Pea protein isolate solubility was improved from 41 to 73% by the presence of P90 at pH 6.0 and was also moderately increased at pH 4.0 and pH 5.0 by P90 and P29, respectively. The emulsion stability of both pea protein isolate–pectin complexes was higher than the homogeneous pea protein isolate at all critical pHs except pHopt as well as pHc for pea protein isolate–P29 only. P90, with the higher level blockiness and esterification, displayed better foaming properties at the maximal complexation pH when complexed with pea protein isolate than pea protein isolate–P29 or pea protein isolate alone. However at pHϕ2, pea protein isolate–P29 admixtures produced foams with 100% stability, increasing pea protein isolate foam stability by 85%. The enhanced functionality of pea protein isolate–pectin complexes based on the type of pectin used at critical pHs indicates they may be useful biopolymer ingredients in plant protein applications.


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