Effects of pH and Salt Concentration on Functional Properties of Pumpkin Seed Protein Fractions

The effects of pH, salt concentration, and temperature on the adsorption of a water-soluble insect cuticular protein to chitin have been investigated. The adsorption is dependent upon pH, decreasing rapidly as the pH increases from the region of the isoelectric point of the protein. Increase in salt concentration decreases adsorption but the adsorption appears to be little influenced by changes in temperature. Tyrosine-rich protein fractions are preferentially adsorbed. The adsorption is partly irreversible and an increase to pH 9 is necessary before all the adsorbed protein can be removed. It is concluded that there is only a weak bonding between the chitin and the water-soluble cuticular protein.

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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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Effects of pH and salt concentration on functional properties of rambutan (Nephelium lappaceum L.) seed albumin concentrate

International Journal of Food Science & Technology ◽

10.1111/ijfs.13087 ◽

2016 ◽

Vol 51 (5) ◽

pp. 1212-1219 ◽

Cited By ~ 4

Author(s):

Huynh Thanh Hai Vuong ◽

Ngoc Minh Chau Tran ◽

Thi Thu Tra Tran ◽

Nu Minh Nguyet Ton ◽

Van Viet Man Le

Keyword(s):

Functional Properties ◽

Salt Concentration ◽

Nephelium Lappaceum ◽

Effects Of Ph

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Determining the effect of pH-shifting treatment on the solubility of pumpkin seed protein isolate

Eastern-European Journal of Enterprise Technologies ◽

10.15587/1729-4061.2021.242334 ◽

2021 ◽

Vol 5 (11 (113)) ◽

pp. 29-34

Author(s):

Dan Gao ◽

Anna Helikh ◽

Zhenhua Duan

Keyword(s):

Particle Size ◽

Zeta Potential ◽

Functional Properties ◽

Soluble Protein ◽

Seed Protein ◽

Average Particle Size ◽

Protein Isolate ◽

Average Particle ◽

Pumpkin Seed ◽

Ph Shifting

Pumpkin seed protein is a high-quality plant protein, which has all essential amino acids for the human body and can also supply essential amino acid histidine for children. When it is introduced to food products, it needs to meet some functional properties, such as solubility, emulsifying ability, foaming ability, and so on. Among them, solubility is very important because it has a great influence on other functional properties of protein. In this study, pH-shifting treatment, which is a novel method to modify protein, is applied to improve the solubility of pumpkin seed protein isolate (PSPI). PSPI treated by pH-shifting treatment was investigated at different pH values (pH 2, pH 4, pH 6, pH 8, pH 10, and pH 12), which were labeled as PSPI 2, PSPI 4, PSPI 6, PSPI 8, PSPI 10, and PSPI 12, respectively. Compared to that of control PSPI (45.6 %), only the solubility of PSPI 8 (55.5 %) showed increased (p<0.05) value, while the solubility of PSPI 2 (13.7 %), PSPI 4 (10.8 %), PSPI 10 (41.8 %), and PSPI 12 (13.4 %) showed decreased (p<0.05) value. Then the average particle size, zeta potential of the soluble protein in PSPI were analyzed, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed. PSPI 2, PSPI 4, and PSPI 12 showed decreased (p<0.05) average particle size after the pH-shifting process. And PSPI 2, and PSPI 12 showed decreased (p<0.05) zeta potential. While other samples didn’t show any significant difference in these two indicators. Besides, the molecular weight of the increased abundance of soluble protein bands was observed at 33 kDa and 25 kDa of PSPI 8. As the solubility of PSPI 8 increased (p<0.05) significantly, it might suggest the PSPI after pH-shifting treatment under pH 8 has more advantages to be used in the food industry

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Functional properties of sesame (Sesamum indicum Linn) seed protein fractions

Food Production, Processing and Nutrition ◽

10.1186/s43014-020-00047-5 ◽

2021 ◽

Vol 3 (1) ◽

Author(s):

Atinuke O. Idowu ◽

Adeola M. Alashi ◽

Ifeanyi D. Nwachukwu ◽

Tayo N. Fagbemi ◽

Rotimi E. Aluko

Keyword(s):

Functional Properties ◽

Seed Protein ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Sesame Seed ◽

Water Soluble ◽

Protein Fractions ◽

Wide Ph Range ◽

Food Applications ◽

Ph Range

Abstract This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications. Sesame seed protein fractions were prepared according to their solubility: water-soluble (albumin), salt-soluble (globulin), alkaline-soluble (glutelin) and ethanol-soluble (prolamin). Globulin was the most abundant fraction, consisting of 91% protein, followed by glutelin, albumin and prolamin in decreasing order. Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed polypeptides of sizes ≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19, 85 and 100 kDa. Prolamin had polypeptide sizes 20, 40 and 100 kDa. The albumin and globulin fractions had higher intrinsic fluorescence intensity (FI) values than the glutelin. Albumin had a higher solubility (ranging from 80 to 100%) over a wide pH range when compared with the other fractions. Water holding capacity (g/g) reduced from 2.76 (glutelin) to 1.35 (prolamin) followed by 0.42 (globulin) and 0.08 (albumin). Oil holding capacity (g/g) reduced from: 4.13 (glutelin) to 2.57 (globulin) and 1.56, 1.50 for albumin and prolamin respectively. Gelling ability was stronger for prolamin and glutelin than albumin and globulin, while higher emulsion (p < 0.05) quality was obtained for prolamin and albumin than for glutelin and globulin. Graphical abstract

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