Abstract
This work is focused on physicochemical and emulsifying properties of pea (PP), chickpea (CP) and lentil (LP) proteins. We evaluated the molecular weight distributions, surface net charge, free sulfhydryl group (SH) and disulfide bond (SS) contents, protein solubility and thermal stability of the protein isolates. Their emulsifying properties (droplet size distribution, flocculation, coalescence and creaming) were also determined as function of pH values. The three protein isolates exhibit similar physicochemical properties, including good solubility and high thermal stability despite a high degree of denaturation. In addition, we analysed the influence of pH on stability of oil-in-water (O/W; 10 wt%/90 wt%) emulsions stabilized by the legume protein isolates. Concerning emulsifying ability and stability, the most unfavourable results for all three protein isolates relate to their isoelectric point (pI = 4.5). A significant improvement in emulsion stability takes place as the pH value departs from the pI. Overall, this study indicates that pea, chickpea and lentil proteins have great potential as food emulsifiers.
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J.I. Boye, S. Aksay, S. Roufik, S. Ribéreau, M. Mondor, E. Farnworth, S.H. Rajamohamed, Food Res Int 43, 537–546 (2010)
P. Watts, in Pulse Foods: Processing, Quality and Nutraceutical Applications, ed. by B.K. Tiwari, A. Gowen, B. McKenna (Elservier, Amsterdam, 2011), p. 437
C. Bassett, J. Boye, R. Tyler, B.D. Oomah, Food Res Int 43, 397–398 (2010)
M. Carbonaro, P. Maselli, A. Nucara, Food Res Int (2014). doi:10.1016/j.foodres.2014.11.007
H. Junrong, A.S. Henk, J.G.S. Jeroen, J. Zhengyu, S. Ellen, G.J.V.S. Alphons, Food Chem 101, 1338–1345 (2007)
A. Gharsallaoui, E. Cases, O. Chambin, R Food Biophys 4, 273–280 (2009)
A.R. Taherian, M. Mondor, J. Labranche, H. Drolet, D. Ippersiel, F. Lamarche, Food Res Int 44, 2505–2514 (2011)
N. Wang, R. Toews, Food Res Int 44, 2515–2523 (2011)
J. Han, J.A.M. Janz, M. Gerlat, Food Res Int 43, 627–633 (2010)
Z. Pietrasik, J.A.M. Janz, Food Res Int 43, 602–608 (2010)
L.P.D. Marchais, M. Foisy, S. Mercier, S. Villeneuve, M. Mondor, Procedia Food Sci 1, 1425–1430 (2011)
F. Zare, C.P. Champagne, B.K. Simpsonc, V. Orsat, J.I. Boye, LWT Food Sci Technol 45, 155–160 (2012)
R. Toews, N. Wang, Food Res Int 52, 445–451 (2013)
C.H. Tang, LWT Food Sci Technol 41, 1380–1388 (2008)
E.M. Papalamprou, G.I. Doxastakis, V. Kiosseoglou, V.J. Sci, Food Agric 90, 304–313 (2010)
A.C. Karaca, N. Low, M. Nickerson, Food Res Int 44, 2742–2750 (2011)
E.Y. Ladjal, M. Chibane, Int Food Res J 22, 987–996 (2015)
U.K. Laemmli, Nature 227, 680–685 (1970)
C.H. Tang, X. Sun, J. Agric, Food Chem 58, 6395–6402 (2010)
C.F. Chau, P.C.K. Cheung, Food Chem 61, 429–433 (1998)
M.M. Bradford, Anal Biochem 72, 248–254 (1976)
H.N. Liang, C.H. Tang, Food Hydrocoll 33, 309–319 (2013)
K. Shevkani, N. Singh, A. Kaur, J.C. Rana, Food Hydrocoll 43, 679–689 (2015)
S. He, B.K. Simpson, M.O. Ngadi, Y. Ma, Food Chem 173, 397–404 (2015)
J.L. Mession, M.L. Chihi, N. Sok, R. Saurel, Food Hydrocoll 46, 233–243 (2015)
Y. Tian, J.B. Du, J. Appl Clin, Pediatrics 19, 1499–1501 (2007)
S. Damodaran, in Food Protein – Properties and Characterisation, ed. by S. Nakai, W. Molder (VCH, Neew York, 1996), pp. 167–234
C.H. Tang, X. Sun, S.W. Yin, Food Hydrocoll 23, 1771–1778 (2009)
C.H. Tang, X. Sun, Food Hydrocoll 25, 315–324 (2011)
S.W. Yin, J.C. Chen, S.D. Sun, C.H. Tang, X.Q. Yang, Q.B. Wen, J.R. Qi, Food Chem 128, 420–426 (2011)
Y.N. Sreerama, V.B. Sashikala, V.M. Pratape, V. Singh, Food Chem 131, 462–468 (2012)
I.A. Wani, D.S. Sogi, B.S. Gill, LWT Food Sci Technol 60, 848–854 (2015)
V. Kiosseoglou, A. Paraskevopoulou, in Functional and Physicochemical Properties of Pulse Proteins, ed. by B.K. Tiwari, A. Gowen, B. McKenna (Elsevier, Amsterdam, 2011), p. 91
L. Shen, C.H. Tang, Food Hydrocoll 36, 278–286 (2014)
J.F. Zayas, in Functionality of Proteins in Food, ed. by J.F. Zayas (Springer, Berlin Heidelberg, 1997), pp. 6–75
C. Chung, D.J. McClements, Food Struct. 1, 106–126 (2014)
Acknowledgments
The authors wish to thank Béjaia University and the University of Seville for technical support. The authors are also grateful to the Microscopy and Microanalysis research services of the University of Seville (CITIUS-Universidad de Sevilla) for providing full access to their facilities and assistance with the experiments.
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• Physicochemical characterization of pea, chickpea and lentil protein isolates;
• Good solubility, high thermal stability and high degree of denaturation
• Emulsifying properties are pH dependent with good results at pH values away from pI
• Investigated legume proteins could be useful as emulsifiers in food formulations
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Ladjal-Ettoumi, Y., Boudries, H., Chibane, M. et al. Pea, Chickpea and Lentil Protein Isolates: Physicochemical Characterization and Emulsifying Properties. Food Biophysics 11, 43–51 (2016). https://doi.org/10.1007/s11483-015-9411-6
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DOI: https://doi.org/10.1007/s11483-015-9411-6