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Canola Proteins for Human Consumption: Extraction, Profile, and Functional Properties

Siong H. Tan, Rodney J. Mailer, Christopher L. Blanchard and 1 more

Journal of Food Science · 2010 · Review

doi:10.1111/j.1750-3841.2010.01930.x

Abstract

Canola protein isolate has been suggested as an alternative to other proteins for human food use due to a balanced amino acid profile and potential functional properties such as emulsifying, foaming, and gelling abilities. This is, therefore, a review of the studies on the utilization of canola protein in human food, comprising the extraction processes for protein isolates and fractions, the molecular character of the extracted proteins, as well as their food functional properties. A majority of studies were based on proteins extracted from the meal using alkaline solution, presumably due to its high nitrogen yield, followed by those utilizing salt extraction combined with ultrafiltration. Characteristics of canola and its predecessor rapeseed protein fractions such as nitrogen yield, molecular weight profile, isoelectric point, solubility, and thermal properties have been reported and were found to be largely related to the extraction methods. However, very little research has been carried out on the hydrophobicity and structure profiles of the protein extracts that are highly relevant to a proper understanding of food functional properties. Alkaline extracts were generally not very suitable as functional ingredients and contradictory results about many of the measured properties of canola proteins, especially their emulsification tendencies, have also been documented. Further research into improved extraction methods is recommended, as is a more systematic approach to the measurement of desired food functional properties for valid comparison between studies.

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    Not in our library

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    Yoshie-Stark Y, Wasche A. In vitro binding of bile acids by lupin protein isolates and their hydrolysates. Food Chem. 2004;88(2):179-84.

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    Zirwer D, Gast K, Welfle H, Schlesier B, Schwenke KD. Secondary structure of globulins from plant seeds: a re-evaluation from circular dichroism measurements. Int J Biol Macromols. 1985;7(2):105-8.

    Not in our library

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    Zum Felde T, Baumert A, Strack D, Becker HC, Mollers C. Genetic variation for sinapate ester content in winter rapeseed (Brassica napus L.) and development of NIRS calibration equations. Plant Breed. 2007;126(3):291-6.

    Not in our library

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