Emulsifying properties of proteins extracted from Australian canola meal

Tan, Siong H.; Mailer, Rodney J.; Blanchard, Christopher L.; Agboola, Samson

doi:10.1016/j.lwt.2013.12.040

Cited by 46 publications

(23 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Oleosin has an isoelectric point (IP) of 6.5 and the precipitation pH in the present study (pH 5) is closer to oleosins' IP compared to the pH used in the study reported by Tan et al The rather low emulsifying capacity could be due to high molecular weight polypeptides (<250 kDa) remaining in the isolate [30]. In addition, the presence of disulphide bonds in canola protein isolates could further reduce the overall flexibility of the high molecular weight polypeptide giving the lower emulsifying capacity [30].…”

Section: Emulsifying Propertiessupporting

confidence: 50%

“…The particle size distributions were relatively narrow with a span of about 1. The reported average droplet size (d 43 ) was smaller compared to values reported by Tan et al [30], a study in which emulsions were produced with an acid-precipitated isolate of cold-pressed canola as emulsifier (these emulsions had a droplet size of d 43 around 60 µm). The difference between the present study and the study reported by Tan et al might be due to the use of a different acidic pH.…”

Section: Emulsifying Propertiesmentioning

confidence: 59%

See 1 more Smart Citation

Protein Recovery from Rapeseed Press Cake: Varietal and Processing Condition Effects on Yield, Emulsifying Capacity and Antioxidant Activity of the Protein Rich Extract

Östbring

Tullberg

Burri

et al. 2019

Foods

View full text Add to dashboard Cite

Protein was recovered from five varieties and a mixed blend of cold-pressed rapeseed press cake by leaching and precipitation in a water-based process, and the protein recovery yield varied from 26-41% depending on variety. Exposure for heat during protein recovery severely reduced the rapeseed proteins' ability to stabilize the oil-water interface of emulsion droplets. Protein extract from Lyside had the best emulsifying properties of the varieties investigated. Oxidation rate was assessed by the Thiobarbituric Acid Reactive Substances (TBARS) method and rapeseed protein extracts from Epure and Festivo had higher capacity to delay oxidation compared with soy lecithin. There are possibilities to broaden the use of rapeseed whereby recovered rapeseed protein can be used as a plant-based multifunctional ingredient with emulsifying capacity and which has a delaying effect on oxidation.

show abstract

Section: Emulsifying Propertiessupporting

confidence: 50%

Section: Emulsifying Propertiesmentioning

confidence: 59%

Protein Recovery from Rapeseed Press Cake: Varietal and Processing Condition Effects on Yield, Emulsifying Capacity and Antioxidant Activity of the Protein Rich Extract

Östbring

Tullberg

Burri

et al. 2019

Foods

View full text Add to dashboard Cite

show abstract

“…A high initial surface coverage in the monolayers is generated by albumins favouring more intramolecular short-range interactions. Tan et al (2014a) have studied albumin and globulin fractions of canola separately and showed that proteins in these fractions are capable of forming emulsions at pH 4, 7 and 9 and exhibit higher emulsifying capacity (1000-1800 ml/g) than canola protein isolate (mixture of proteins found in albumin and globulin fractions) obtained by alkali extraction and precipitation at pH 4 (500-800 ml/g) or commercial soy protein isolate (500-1500 mL/g). The emulsions formed with these proteins had average droplet size of 18-30 µm with an exceptionally large droplet size for globulin stabilized emulsions at pH 4 (80 µm).…”

Section: Oil/water (O/w) Emulsionsmentioning

confidence: 99%

Canola/rapeseed protein-functionality and nutrition

Wanasundara¹,

McIntosh²,

Perera³

et al. 2016

OCL

136

103

View full text Add to dashboard Cite

-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...

show abstract

“…A range of studies have been devoted to the emulsifying properties of canola/rapeseed meals, canola protein isolates, their composition and characterisation (Khattab & Arntfield, 2009;Tan et al, 2014), as well as concentrates (Aluko et al, 2005) and their enzymatic hydrolysates (Vioque et al, 2000). These previous studies used different extraction (alkaline and water) and processing methods such as heat (boiling and roasting) and hydrolysis (chemical and enzymatic modifications) in addition to determining the effects of pH and time on emulsion stability (Alashi et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

Alashi

Blanchard

Mailer

et al. 2018

Int J of Food Sci Tech

Self Cite

View full text Add to dashboard Cite

Summary The aim of this work was to enhance emulsification properties of canola proteins through enzymatic proteolysis and pH variaton. Canola protein isolate (CPI) and hydrolysates (CPHs) were used to form emulsions at pH 4.0, 7.0 and 9.0 followed by storage at 4 or 25 °C for 7 days. Controlled enzymatic hydrolysis led to increased peptide bond cleavage with time (0.23 g/100 g in CPI to 7.18 g/100 g after 24‐h Alcalase hydrolysis). Generally, oil droplet sizes were smaller for emulsions made at pH 9.0, which suggest better quality than those made at pH 4.0 and 7.0. Trypsin hydrolysate emulsions were the most physically stable at pH 7.0 and 9.0; in contrast, the pepsin hydrolysate emulsions were unstable at all conditions. The results suggest that selective enzymatic hydrolysis could play an important role in enhancing successful incorporation of canola proteins and peptides into food systems as protein emulsifiers.

show abstract

Emulsifying properties of proteins extracted from Australian canola meal

Cited by 46 publications

References 20 publications

Protein Recovery from Rapeseed Press Cake: Varietal and Processing Condition Effects on Yield, Emulsifying Capacity and Antioxidant Activity of the Protein Rich Extract

Protein Recovery from Rapeseed Press Cake: Varietal and Processing Condition Effects on Yield, Emulsifying Capacity and Antioxidant Activity of the Protein Rich Extract

Canola/rapeseed protein-functionality and nutrition

Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

Contact Info

Product

Resources

About