Effect of pH on the functional behaviour of pea protein isolate–gum Arabic complexes

Liu, S.; Elmer, C.; Low, Nicholas H.; Nickerson, Michael T.

doi:10.1016/j.foodres.2009.07.022

Cited by 190 publications

(95 citation statements)

References 39 publications

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“…Foaming capacity (FC) and foam stability (FS) for 1.0 % (w/w) protein flour/concentrate solutions were determined according to Liu et al [14]. In brief, 15 mL of each protein solution was transferred to a 400-mL beaker for homogenization using an Omni Macro Homogenizer (Omni International, Marietta, GA, USA) with a 20-mm sawtooth probe at speed 4 (~7200 rpm) for 5 min.…”

Section: Foamingmentioning

confidence: 99%

Effect of genotype and environment on the surface characteristics and functionality of air-classified faba bean protein concentrates

Martínez

Stone

Yovchev

et al. 2016

Eur Food Res Technol

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Section: Foamingmentioning

confidence: 99%

Effect of genotype and environment on the surface characteristics and functionality of air-classified faba bean protein concentrates

Martínez

Stone

Yovchev

et al. 2016

Eur Food Res Technol

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“…Creaming stability refers to the ability of a protein stabilized emulsion to resist creaming, where oil droplets flocculate and coalescence, then migrate upwards due to the density difference from MQW (Damodaran 2005;Liu et al 2010;Can Karaca et al 2011). The ability of an emulsion to resist creaming is largely dependent on droplet size and density contrast between phases (McClements 2007).…”

Section: Creaming Stabilitymentioning

confidence: 99%

The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin

2014

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The physicochemical and emulsifying properties of legume protein isolates prepared from chickpea (CPI), faba bean (FPI), lentil (LPI) and soy (SPI) were investigated in the presence and absence of genipin. Solubility was highest for CPI (~94 %), followed by LPI (~90 %), FPI (~85 %) and SPI (~50 %). Surface characteristics revealed similar zeta potentials (~−47 mV) for CPI, LPI and FPI, but lower for SPI (~− 44 mV). Contrastingly, surface hydrophobicity was greatest for CPI (~137 arbitrary units, AU), followed by SPI/LPI (~70 AU) and FPI (~24 AU). A significant (from 16.73 tõ 8.42 mN/m) reduction in interfacial tension was observed in canola oil-water mixtures in the presence of non-crosslinked legume protein isolates. The extent of legume protein isolategenipin crosslinking was found to be similar for all isolates. Overall, creaming stability increased in the presence of genipin, with maximum stability observed for SPI (65 %), followed by FPI (61 %), LPI (56 %) and finally CPI (50 %).

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“…Foaming properties (overrun and half-life of foam) were determined according to Yang and Foegeding (2010) and Liu et al (2010) with some modifications. Lyophilised SPI (2 g) was dissolved in 198 g of deionised water containing different polyol concentrations (0~15% w/w) and stirred with a magnet bar for 2 h to a uniform dispersion at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

Pan¹,

Meng²,

Jiang³

et al. 2017

Czech J. Food Sci.

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Pan M., Meng X., Jiang L., Yu D., Liu T. (2017): Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate. Czech J. Food Sci., 35: 57-66.Effect of polyols (mannitol, sorbitol, and xylitol) at three concentrations (5, 10, and 15% w/w) on the structure of soy protein isolates (SPI) was investigated. Changes in foaming properties of SPI were then examined with the addition of polyols at different concentrations. The interactions between SPI and polyols resulted in a substantial decrease in protein surface hydrophobicity and intrinsic tryptophan fluorescence intensity, along with the covering of tyrosine. Furthermore, circular dichroism (CD) spectroscopy of SPI suggested that a more ordered and compact conformation was induced by polyols. Consequently, these structural changes led to lower foamability of SPI. An increase in the viscosity of SPI suspension seemed to be advantageous for improving the foam stability of SPI.

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Effect of pH on the functional behaviour of pea protein isolate–gum Arabic complexes

Cited by 190 publications

References 39 publications

Effect of genotype and environment on the surface characteristics and functionality of air-classified faba bean protein concentrates

Effect of genotype and environment on the surface characteristics and functionality of air-classified faba bean protein concentrates

The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

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