Effect of pyrogallic acid (1,2,3-benzenetriol) polyphenol-protein covalent conjugation reaction degree on structure and antioxidant properties of pumpkin (Cucurbita sp.) seed protein isolate

Twelve high-quality chia protein hydrolysates (CPHs) were produced from chia protein isolate (CPI) in a pilot plant of vegetable proteins. To obtain functional hydrolysate, four CPHs were hydrolyzed by the action of Alcalase, an endoprotease, and the other eight CPHs were hydrolyzed by the action of Flavourzyme, an exoprotease. Alcalase-obtained CPHs showed significant antihypertensive properties particularly, the CPH obtained after 15 min of hydrolysis with Alcalase (CPH15A), which showed a 36.2% hydrolysis degree. In addition, CPH15A increased the antioxidant capacity compared to CPI. The CPH15A physicochemical composition was characterized and compared to chia defatted flour (CDF) and CPI, and its techno-functional properties were determined by in vitro experiments through the analysis of its oil absorption capacity, as well as the capacity and stability of foaming and emulsifying, resulting in an emulsifier and stabilizer better than the intact protein. Therefore, the present study revealed that CPH15A has potent antihypertensive and antioxidant properties and can constitute an effective alternative to other plant protein ingredients sources that are being used in the food industry.

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Antioxidant and antihypertensive activities of wonderful cola (Buchholzia coriacea) seed protein and enzymatic protein hydrolysates

Journal of Food Bioactives ◽

10.31665/jfb.2018.3156 ◽

2018 ◽

Vol 3 ◽

pp. 133-143 ◽

Cited By ~ 5

Author(s):

Oluwole S. Ijarotimi ◽

Sunday A. Malomo ◽

Adeola M. Alashi ◽

Ifeanyi D. Nwachukwu ◽

Tayo N. Fagbemi ◽

...

Keyword(s):

Blood Pressure ◽

Protein Hydrolysate ◽

Antioxidant Properties ◽

Radical Scavenging ◽

Protein Isolate ◽

Active Inhibitor ◽

Spontaneously Hypertensive ◽

Reducing Ability ◽

Peptide Fractions

The aim of this work was to produce wonderful cola protein hydrolysate fractions with in vitro antioxidant properties coupled with blood pressure-reducing ability when orally administered to spontaneously hypertensive rats (SHRs). Wonderful cola protein isolate (WCI) was hydrolyzed with pancreatin to produce a hydrolysate (WCH), which was subjected to ultrafiltration separation using 1, 3, 5, and 10 kDa molecular weight cut-off membranes to obtain <1, 1–3, 3–5 and 5–10 kDa peptide fractions, respectively. The <1 and 1–3 kDa fractions had higher contents of arginine when compared to the 3–5 and 5–10 kDa peptides. The WCH and <1 kDa peptide fraction had significantly (p < 0.05) better DPPH radical scavenging (55–67%) and metal chelation (83–93%) activities but lower hydroxyl radical scavenging power (10–32%) than the WCI (46, 46 and 63%, respectively). The <1 kDa had significantly (p < 0.05) higher in vitro inhibition (80%) of angiotensin converting enzyme (ACE) activity while the 5–10 kDa was the most active inhibitor (90%) of renin activity. All peptide fractions so produced had better systolic and diastolic blood pressure-lowering effects than WCH and WCI. However, the <1 kDa fraction produced significantly (p < 0.05) stronger systolic (−33 mmHg) and diastolic (−30 mmHg) blood pressure reductions 6 h after oral gavage to SHRs. Thus, wonderful cola proteins contain encrypted bioactive peptides that may be used to formulate antioxidant and antihypertensive products.

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Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate

Food Chemistry ◽

10.1016/j.foodchem.2011.03.116 ◽

2011 ◽

Vol 128 (4) ◽

pp. 902-908 ◽

Cited By ~ 120

Author(s):

Abayomi P. Adebiyi ◽

Rotimi E. Aluko

Keyword(s):

Pisum Sativum ◽

Functional Properties ◽

Seed Protein ◽

Protein Isolate ◽

Field Pea ◽

Protein Fractions ◽

Pisum Sativum L

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Effect of Xanthan and Arabic Gums on Foaming Properties of Pumpkin (Cucurbita pepo) Seed Protein Isolate

Journal of Food Research ◽

10.5539/jfr.v3n1p87 ◽

2013 ◽

Vol 3 (1) ◽

pp. 87 ◽

Cited By ~ 1

Author(s):

Quirino Dawa ◽

Yufei Hua ◽

Moses Vernonxious Madalitso Chamba ◽

Kingsley George Masamba ◽

Caimeng Zhang

Keyword(s):

Sodium Chloride ◽

Salt Concentration ◽

Seed Protein ◽

Foam Stability ◽

Chloride Concentration ◽

Egg White ◽

Protein Isolate ◽

Foaming Properties ◽

Ph Optimum ◽

Pumpkin Seed

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 (p < 0.05) 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 (p < 0.05) 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.

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