The Effect of pH and NaCl Levels on the Physicochemical and Emulsifying Properties of a Cruciferin Protein Isolate

Cheung, Lamlam; Wanasundara, Janitha P. D.; Nickerson, Michael T.

doi:10.1007/s11483-013-9323-2

Cited by 66 publications

(35 citation statements)

References 35 publications

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“…The surface charge (or zeta potential) of the oilseed protein concentrates as a function of pH is given in Table 3. The isoelectric point of canola protein was similar to what has been reported for a cruciferin protein isolate (Cheung, Wanasundara, & Nickerson, 2014) and canola protein isolate with the addition of NaCl (Kim et al, 2016). Due to the limited number of data points collected, these values represent an imprecise approximation of the pI only.…”

Section: Physicochemical Propertiessupporting

confidence: 77%

Effect of pH and defatting on the functional attributes of safflower, sunflower, canola, and hemp protein concentrates

Galves

Stone

Szarko³

et al. 2019

Cereal Chem

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Background and objectives The effect of defatting four oilseed protein concentrates (safflower, sunflower, canola, and hemp) on the surface and functional properties of the proteins was investigated as a function of pH (pH 3, 5, 7). The functionality of commercial protein concentrates (soy, faba bean, lentil, pea, northern great bean, whey) already in the marketplace was also tested for comparative purposes. Findings Defatting with hexane increased the protein content from 77.3% to 92.9% for safflower, 67.5 to 75.5% for sunflower, 58.0–66.0% for canola, and 71.0–83.2% for hemp. The approximate isoelectric point (pI) of safflower increased with defatting (5.4–5.8), whereas for canola the pI decreased with defatting (4.7–4.3), and sunflower and hemp protein concentrates had similar pI for defatted or full fat. Certain functional properties were improved with defatting, whereas others showed the opposite trend; this was highly dependent on protein type and pH. Conclusions The oilseed concentrates were comparable to the concentrates in the marketplace with canola and sunflower proteins having the greatest oil‐holding capacity and defatted safflower having the highest foaming capacity of all the proteins tested. Significance and novelty Based on their functionality, the oilseed protein concentrates have potential to be used by the food ingredient industry.

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Section: Physicochemical Propertiessupporting

confidence: 77%

Effect of pH and defatting on the functional attributes of safflower, sunflower, canola, and hemp protein concentrates

Galves

Stone

Szarko³

et al. 2019

Cereal Chem

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“…Presence of phytates in canola protein isolate composed of cruciferin and napin (70% globulin, 30% albumin and ∼1% phytic acid) may cause stable electrostatic protein-phytate complexes thus reduces surface activity of protein molecules (Krause and Schwenke, 2001) and enhance interface stabilization. Working with somewhat pure protein, Wu and Muir (2008) and Cheung et al (2014) showed cruciferin (>80% purity) possesses better emulsifying ability than napin (Cheung et al, 2015). Wijesundera et al (2013) demonstrated that canola protein extracted at alkaline pH (12) and recovered by precipitating at pH 6.5 can stabilize O/W emulsions.…”

Section: Oil/water (O/w) Emulsionsmentioning

confidence: 99%

Canola/rapeseed protein-functionality and nutrition

Wanasundara¹,

McIntosh²,

Perera³

et al. 2016

OCL

136

103

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-Protein rich meal is a valuable co-product of canola/rapeseed oil extraction. Seed storage proteins that include cruciferin (11S) and napin (2S) dominate the protein complement of canola while oleosins, lipid transfer proteins and other minor proteins of non-storage nature are also found. Although oil-free canola meal contains 36-40% protein on a dry weight basis, non-protein components including fibre, polymeric phenolics, phytates and sinapine, etc. of the seed coat and cellular components make protein less suitable for food use. Separation of canola protein from non-protein components is a technical challenge but necessary to obtain full nutritional and functional potential of protein. Process conditions of raw material and protein preparation are critical of nutritional and functional value of the final protein product. The storage proteins of canola can satisfy many nutritional and functional requirements for food applications. Protein macromolecules of canola also provide functionalities required in applications beyond edible uses; there exists substantial potential as a source of plant protein and a renewable biopolymer. Available information at present is mostly based on the protein products that can be obtained as mixtures of storage protein types and other chemical constituents of the seed; therefore, full potential of canola storage proteins is yet to be revealed.Keywords: Canola / rapeseed storage proteins / cruciferin / napin / protein digestibility / functional properties Résumé -Protéines de canola et de colza : fonctionnalités et nutrition. Les tourteaux riches en protéines repré-sentent un coproduit de valeur de l'extraction de l'huile de canola/colza. Dans la graine, les protéines de stockage, notamment la cruciférine (11S) et la napine (2S), dominent la fraction protéique du canola, mais des oléosines, des protéines de transfert de lipides et d'autres protéines mineures non dédiées au stockage sont également présentes. Bien que le tourteau de canola déshuilé contienne 36-40 % de protéines sur poids sec, la présence de composants non protéiques, dont les fibres, les polymères phénoliques, les phytates, la sinapine, etc. issus de l'enveloppe de la graine et des composants cellulaires rendent les protéines moins appropriées à une utilisation en alimentation humaine. Cette revue présente les connaissances actuelles en termes de valeur nutritionnelle et fonctionnelle des protéines issues des graines de canola. La séparation des protéines de canola des composants non protéiques représente un défi technique mais nécessaire pour libérer totalement le potentiel nutritionnel et fonctionnel de la protéine. Les protéines de stockage de canola peuvent satisfaire un grand nombre d'exigences nutritionnelles et fonctionnelles pour des applications alimentaires. Les macromolécules protéiques de canola offrent également des fonctionnalités requises dans les applications dépassant les seules utilisations alimentaires ; un potentiel important existe en tant que source de protéines végétales et de biopol...

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“…This indicates a salting‐out effect of the protein present in CRP, rather than a salting‐in effect of NaCl expected for globulin proteins. This finding is in contrast to previous results, showing an increased solubility by the addition of 50 and 100 m m NaCl (Cheung et al ., ). Different factors can result in the contradicting behaviour of CRP assessed in this study.…”

Section: Resultsmentioning

confidence: 97%

“…(), reporting that varying solubility at similar pH values is found. Different laboratory‐scale studies have analysed the possibility to enhance the solubility of rapeseed protein by, for example, partial hydrolysis (Vioque et al ., , ) and the addition of NaCl (Cheung et al ., , ).…”

Section: Introductionmentioning

confidence: 99%

Solubility of a cruciferin‐rich protein product purified from rapeseed pressed cake (Brassica napus L.) by an aqueous processing method

Rehder

Sulewska

Markedal

et al. 2017

Int J of Food Sci Tech

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Summary Pressed cake from rapeseed (Brassica napus L.) is a promising plant protein source not yet utilised for human consumption due to the presence of antinutrients such as glucosinolates. Protein solubility is a crucial parameter influencing the functionality and thereby the applicability of proteins as food ingredients. A novel cruciferin‐rich rapeseed protein product was produced by an aqueous processing method in pilot plant scale. Intact glucosinolates were conserved by this procedure and largely removed from the protein products. Protein solubility in this product was examined when dispersed in 50 mm phosphate buffer, pH 8.0 with varying NaCl concentration (0–500 mm). Unexpectedly, a salting‐out effect was observed of the globulin proteins, as 15.9 ± 0.6% protein was in solution at 500 mm added NaCl, whereas 21.5 ± 1.1% was solubilised without added NaCl; whether the observed effects originates from lipid and fibre constituents in the product remains to be resolved.

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The Effect of pH and NaCl Levels on the Physicochemical and Emulsifying Properties of a Cruciferin Protein Isolate

Cited by 66 publications

References 35 publications

Effect of pH and defatting on the functional attributes of safflower, sunflower, canola, and hemp protein concentrates

Effect of pH and defatting on the functional attributes of safflower, sunflower, canola, and hemp protein concentrates

Canola/rapeseed protein-functionality and nutrition

Solubility of a cruciferin‐rich protein product purified from rapeseed pressed cake (Brassica napus L.) by an aqueous processing method

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