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Modulating the textural characteristics of whey protein nanofibril gels with different concentrations of calcium chloride

Published online by Cambridge University Press:  12 February 2016

Toktam Farjami ,
Ashkan Madadlou  and
Mohsen Labbafi
Toktam Farjami
Affiliation:
Department of Food Science and Engineering, University College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran
Ashkan Madadlou*
Affiliation:
Department of Food Science and Engineering, University College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran
Mohsen Labbafi
Affiliation:
Department of Food Science and Engineering, University College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran
*
*For correspondence; e-mail: a.madadlou@ut.ac.ir
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Abstract

Protein nanofibrils with 10–20 nm diameters were formed by heating whey protein solution at pH 2·0. Nanofibrils solution was deacidified slowly through dialysis followed by adding different amounts of CaCl2 (0–80 mM) into the dialysis water resulting in formation of a soft viscoelastic gel over time. The gel fabricated from the nanofibrils solution dialyzed against distilled water with 0 mM CaCl2 had zero ash content. Fourier transform infra-red spectroscopy revealed a change in the pattern of hydrogen bond formation in gel network by calcium chloride. The higher the ash content of gels, the lower was the storage modulus and fracture stress of samples. Gels with higher ash contents had a more porous microstructure which was attributed to the diminished hydrophobic interactions and hydrogen bonding among nanofibrils by the action of chloride. Higher ash contents also led to higher water holding capacity of gels which was attributed to the influence of the strongly hydrated calcium ions that interacted with the non-charged regions of proteins via site-specific interactions.

Keywords

Whey proteinscold-set gelnanofibrilchloride
Type
Research Article
Information
Journal of Dairy Research , Volume 83 , Issue 1 , February 2016 , pp. 109 - 114
Copyright
Copyright © Proprietors of Journal of Dairy Research 2016 

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References

Akkermans, C, van der Goot, AJ, Venema, P, van der Linden, E & Boom, RM 2008a Formation of fibrillar whey protein aggregates: influence of heat and shear treatment, and resulting rheology. Food Hydrocolloids 22 1315–1325CrossRefGoogle Scholar
Akkermans, C, van der Goot, AJ, Venema, P, van der Linden, E, & Boom, RM 2008b Properties of protein fibrils in whey protein isolate solutions: microstructure, flow behaviour and gelation. International Dairy Journal 18 1034–1042CrossRefGoogle Scholar
Barth, A 2007 Infrared spectroscopy of proteins. Biochimica et Biophysica Acta General Subjects 1767 1073–1101CrossRefGoogle ScholarPubMed
Beauchamp, DL & Khajehpour, M 2012 The effect of lithium ions on the hydrophobic effect: does lithium affect hydrophobicity differently than other ions? Biophysical Chemistry 163–164 35–43CrossRefGoogle ScholarPubMed
Bolder, G, Hendrickx, H, Sagis, LMC & van der Linden, E 2006 Fibril assemblies in aqueous whey protein mixtures. Journal of Agricultural and Food Chemistry 54 4229–4234CrossRefGoogle ScholarPubMed
Chen, L, Remondetto, GE & Subirade, M 2006 Food protein-based materials as nutraceutical delivery systems. Trends in Food Science & Technology 17 272–283CrossRefGoogle Scholar
Donato, L, Schmitt, C, Bovetto, L & Rouvet, M 2009 Mechanism of formation of stable heat-induced b-lactoglobulin microgels. International Dairy Journal 19 295–306CrossRefGoogle Scholar
Garti, N & McClements, DJ 2012 Encapsulation Technologies and Delivery Systems for Food Ingredients and Nutraceuticals. Cambridge: Woodhead Publishing LimitedCrossRefGoogle Scholar
Hughes, VA & Dunstan, DE 2009 Amyloid fibrils – self-assembling proteins. In Modern Biopolymer Science, pp. 559–594 (Eds Kasapis, S, Norton, I & Ubbink, J). San Diego: Academic PressCrossRefGoogle Scholar
Jackson, M & Mantsch, HH 1995 The use and misuse of FTIR spectroscopy in the determination of protein structure. Critical Reviews in Biochemistry and Molecular Biology 30 95–120CrossRefGoogle ScholarPubMed
Kong, J & Yu, S 2007 Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica 39 549–559CrossRefGoogle ScholarPubMed
Kovács, A & Varga, Z 2006 Halogen acceptors in hydrogen bonding. Coordination Chemistry Reviews 250 710–727CrossRefGoogle Scholar
Kuhn, KR, Cavallieri, ALF & Cunha, RL 2011 Cold-set whey protein–flaxseed gum gels induced by mono or divalent salt addition. Food Hydrocolloids 25 1302–1310CrossRefGoogle Scholar
Loveday, SM, Su, J, Rao, MA, Anema, SG & Singh, H 2011 Effect of calcium on the morphology and functionality of whey protein nanofibrils. Biomacromolecules 12 3780–3788CrossRefGoogle ScholarPubMed
Loveday, SM, Su, J, Rao, MA, Anema, SG & Singh, H 2012 Whey protein nanofibrils: Kinetic, rheological and morphological effects of group IA and IIA cations. International Dairy Journal 26 133–140CrossRefGoogle Scholar
Lund, M, Vacha, R & Jungwirth, P 2008 Specific ion-binding to macromolecules: effects of hydrophobicity and ion pairing. Langmuir 24 3387–3391CrossRefGoogle ScholarPubMed
Nicolai, T & Durand, D 2013 Controlled food protein aggregation for new functionality. Current Opinion in Colloid & Interface Science 18 249–256CrossRefGoogle Scholar
Nicolai, T, Britten, M & Schmitt, C 2011 β-Lactoglobulin and WPI aggregates: formation, structure and applications. Food Hydrocolloids 25 1945–1962CrossRefGoogle Scholar
Sadeghi, S, Madadlou, A & Yarmand, M 2014 Microemulsification-cold gelation of whey proteins for nanoencapsulation of date palm pit extract. Food Hydrocolloids 35 590–596CrossRefGoogle Scholar
Sedlák, E, Stagg, L & Wittung-Stafshede, P 2008 Effect of Hofmeister ions on protein thermal stability: roles of ion hydration and peptide groups? Archives of Biochemistry and Biophysics 479 69–73CrossRefGoogle ScholarPubMed
van der Linden, E & Foegeding, EA 2009 Gelation: principles, models and applications to proteins. In Modern Biopolymer Science, pp. 29–91 (Eds Kasapis, S, Norton, I & Ubbink, J). San Diego: Academic PressCrossRefGoogle Scholar
Vardhanabhuti, B, Foegeding, EA, McGuffey, MK, Daubert, CR & Swaisgood, HE 2001 Gelation properties of dispersions containing polymerized and native whey protein isolate. Food Hydrocolloids 15 165–175CrossRefGoogle Scholar
Veerman, C, Baptist, H, Sagis, LMC & van der Linden, E 2003a A new multistep Ca2+-induced cold gelation process for β-lactoglobulin. Journal of Agricultural and Food Chemistry 51 3880–3885CrossRefGoogle ScholarPubMed
Veerman, C, Sagis, LMC, Heck, J & van der Linden, E 2003b Mesostructure of fibrillar bovine serum albumin gels. International Journal of Biological Macromolecules 31 139–146CrossRefGoogle ScholarPubMed
Zangi, R, Hagen, M & Berne, BJ 2007 Effect of ions on the hydrophobic interaction between two plates. Journal of the American Chemical Society 129 4678–4686CrossRefGoogle ScholarPubMed