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

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 %)....

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Bibliographic Details
Published in:Journal of food science and technology 2015-07, Vol.52 (7), p.4135-4145
Main Authors: Johnston, Stuart P., Nickerson, Michael T., Low, Nicholas H.
Format: Article
Language:English
Subjects:
Canola oil
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Emulsion polymerization
Food
Food Science
Legumes
Molecular weight
Nutrition
Original
Original Article
Physicochemical properties
Proteins
Seeds
Studies
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Summary: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 to ~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 isolate-genipin 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 %).
ISSN:0022-1155
0975-8402
DOI:10.1007/s13197-014-1523-3