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

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Abstract

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 %).

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Acknowledgments

The authors gratefully acknowledge the financial support provided by the Saskatchewan Agriculture Development Fund.

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  1. Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK, S7N 5A8, Canada

    Stuart P. Johnston, Michael T. Nickerson & Nicholas H. Low

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  1. Stuart P. Johnston
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Correspondence to Nicholas H. Low.

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Johnston, S.P., Nickerson, M.T. & Low, N.H. The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin. J Food Sci Technol 52, 4135–4145 (2015). https://doi.org/10.1007/s13197-014-1523-3

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  • DOI: https://doi.org/10.1007/s13197-014-1523-3

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