Journal article

Interfacial and emulsifying properties of lentil protein isolate

M Joshi, B Adhikari, P Aldred, JF Panozzo, S Kasapis, CJ Barrow

Food Chemistry | ELSEVIER SCI LTD | Published : 2012

Abstract

The dynamic interfacial tension (DIFT) at oil-water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas>LPI>..

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University of Melbourne Researchers

Grants

Funding Acknowledgements

The authors are grateful to Bruce Armstrong and Delina Muscat (University of Ballarat) for their help in some of the experiments. The first author gratefully acknowledges the Aus-AID for the Australian Leadership Award scholarship which enabled this work to be carried out. The authors also gratefully acknowledge support for this Project from the Australian Government Collaborative Research Network (CRN) fund.