Complex coacervation of pea protein isolate and alginate polysaccharides

Klemmer, Karla Jenna; Waldner, Landon L.; Stone, Andrea K.; Low, Nicholas H.; Nickerson, M.T.

doi:10.1016/j.foodchem.2011.07.114

Cited by 153 publications

(78 citation statements)

References 16 publications

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“…Surface characteristics All isolates, regardless of cultivar, had similar isoelectric points (zeta potential=0 mV) with values ranging between 4.6 and 4.9 mV, which were comparable to other reported values for pea protein isolates (1,7,26,(31)(32)(33)(34). In this study, the surface charge of each isolate was determined at pH 7.0 (Table 3) and ranged from −23.05 to −26.75 mV.…”

Section: Resultssupporting

confidence: 85%

Functional properties of protein isolates from different pea cultivars

Stone

Avarmenko

Warkentin

et al. 2015

Food Sci Biotechnol

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Surface characteristics and functional attributes of protein isolates prepared from different pea cultivars using isoelectric precipitation were investigated. Protein levels of isolates ranged from 81-89% with isoelectric points occurring between pH 4.7-4.9. Surface hydrophobicity values differed among cultivars with CDC Dundurn and CDC Striker isolates having the lowest and highest values, respectively. Protein solubility values at pH 7.0 varied with MFR042 and CDC Dundurn isolates displaying the lowest (approximately 54%) and highest (approximately 76%) values, respectively. No significant (p>0.05) differences existed between cultivar isolates for water hydration and oil holding capacity values. Cooper and CDC Dundurn isolates had significantly (p<0.05) lower emulsifying activity indices (EAI) (approximately 31-33 m 2 /g) than the other cultivars. Emulsifying stability index values were all similar. EAI values were positively correlated with surface hydrophobicity values and negatively correlated with solubility values. Varietal differences for the functional attributes of solubility and emulsification were identified.

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Section: Resultssupporting

confidence: 85%

Functional properties of protein isolates from different pea cultivars

Stone

Avarmenko

Warkentin

et al. 2015

Food Sci Biotechnol

View full text Add to dashboard Cite

show abstract

“…Turbidimetric and UV absorption measurements have shown that in the case of the homopolymer in water a phase separation occurs, due to the formation of insoluble BSA/PMAPTAC complexes, as a result of Coulombic interactions in accordance with literature [4,8,11,29]. Potentiometric measurements corroborate this conclusion, showing proton release as a result of Coulombic interactions of the polycation with the BSA carboxylate groups.…”

Section: Discussionsupporting

confidence: 82%

Complexation of bovine serum albumin with cationic polyelectrolytes at pH 7.40 – Formation of soluble complexes

Asimakopoulos

Staikos

2015

European Polymer Journal

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“…pH is vital for proteinÀpolysaccharide coacervate formation. Complex formation generally occurs between the pK a of the polysaccharide and the pI of the protein (Schmitt and Turgeon, 2011;Klemmer et al, 2012). For example, α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) are important whey proteins with isoelectric points of pH 4.80 and 5.34, respectively.…”

Section: Parameters Influencing the Formation Of Coacervatesmentioning

confidence: 99%

“…For example, with an LPI/GA system, the addition of GA pushed the pI of LPI from pH 4.70 to 3.17, and as the LPI/GA ratio increased, critical pH values shifted upwards until reaching the 1:1 mixing ratio, afterwards becoming relatively ratio independent (Aryee and Nickerson, 2012). With the PPI/AL system, as mixing ratios increase from 4:1 and 8:1, critical pH values shifted upwards too (Klemmer et al, 2012). The same trend was observed with the PPI/Ch system, as the PPIÀCh mixing ratio increased from 1:1 to 12.5:1, critical pH values shifted upwards, and progressively behaved similar to those for PPI alone.…”

Section: Parameters Influencing the Formation Of Coacervatesmentioning

confidence: 99%