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Tailored texturizers from natural origin


Key words Texturing agent, stabilizer, natural, tailored, custom-made, biopolymer, protein, polysaccharide, complex coacervation, microparticle, nanoparticle, fibre, encapsulation
Latest version 2013/09/05
Completed by INRA - IATE

How does it work?

Primary objective Design of tailored texturing ingredients based on biopolymers self-assembly
Working principle When two biopolymers carrying opposite charges are mixed together, they interact through these opposite charges and form complexes (1,2). These complexes further rearrange to finally produce sub-micron or micron sized particles (1,3). The technology is based on the formation of colloidal particles through self-assembly of biopolymers thanks to energetically weak interactions, especially electrostatic interactions. The mechanism is called complex coacervation (1,2).

Specific particles with specific texturing and stabilizing properties can be designed depending on the biopolymer pair (polysaccharide-polysaccharide or polysaccharide-protein or protein-protein) and on process parameters such as pH, ionic strength, solvent affinity, biopolymer molar ratio, total biopolymer concentration, shear and temperature (3-10).

This enables one to precisely design texturing ingredients, depending on the food matrix they will be added to, and what texturing and stabilizing effects are expected.

Additional effects Possible soluble fibre effect (some biopolymers are natural soluble fibres).

Stabilization of hydrophobic compounds.

Controlled delivery of biomolecules, minerals and probiotic cells (encapsulation).

Important process parameters temperature, pH, salt concentration, biopolymer characteristics (molecular weight, charge density, solvent affinity, total biopolymer concentration, molar ratio between biopolymers)
Important product parameters Any protein or electrically charged polysaccharide can be used.

What can it be used for?

Products Biopolymer pairs already investigated include acacia gum-whey proteins, xanthan gum-whey proteins, pectin-whey proteins, under investigation are acacia gum-plant proteins.

The final products in which the texturizers are used include dairy products, bakery products, dressings, confectionaries, alcoholic and non-alcoholic drinks, sweets

Operations Biopolymer structuring
Solutions for short comings Development of new highly multifunctional ingredients

What can it NOT be used for?

Products Meat & poultry products, crisps, crackers
Operations Chopping, frying
Other limitations Existence of patents on ice-cream applications with exclusive exploitation
Risks or hazards no


Maturity Possible scale-up problems associated to control of chemical conditions in large volumes
Modularity /Implementation This technology can be easily inserted in an existing production line
Consumer aspects No study so far. Biopolymers are already used individually as food ingredients
Legal aspects Patents
Environmental aspects Green technology: low energy input for the synthesis of these ingredients (self-assembly)

Further Information

Institutes INRA - BIA, KU Leuven LFT, AgroSup Dijon - PAM
Companies Unilever, Alland & Robert, Nestlé Research Centre
References 1. Turgeon S.L., Beaulieu M., Schmitt C. and Sanchez C. 2007. Protein-polysaccharide complexes and coacervates. Current Opinion in Colloid and Interface Science, 12, 166-178.

2. Turgeon S.L., Beaulieu M., Schmitt C. and Sanchez C. 2003. Protein-polysaccharide interactions: Phase-ordering kinetics, thermodynamic and structural aspects. Current Opinion in Colloid and Interface Science, 8, 401-414.

3. Schmitt C., Aberkane L. and Sanchez C. 2009. Protein-polysaccharide complexes and coacervates. In Handbook of Hydrocolloids, 2nd Ed., G.O. Phillips & P.A. William eds, Woodhead Publishing Limited, Ch. 16, pp.420-476.

4. Aberkane L., Jasniewski J., Gaiani C., Hussein R., Scher J. and Sanchez C. 2012. Structuration mechanism of β-lactoglobulin- Acacia gum assemblies in presence of quercetin. Food Hydrocolloids 29, 9-20.

5. Aberkane L., Jasniewski J., Gaiani C., Scher J. and Sanchez C. 2010. Thermodynamic characterization of Acacia gum - β-lactoglobulin complex coacervation. Langmuir, 26, 12523-12533.

6. Laneuville S.I., Sanchez C., Turgeon S.L., Hardy J. and Paquin P. 2006. Gelation of native β-lactoglobulin induced by electrostatic attractive interaction with xanthan gum. Langmuir, 22, 7351-7357.

7. Mekhloufi G., Sanchez C., Renard D., Guillemin S. and Hardy J. 2005. pH-induced structural transitions during complexation and coacervation of b-lactoglobulin and Acacia gum. Langmuir, 21, 386-394.

8. Girard M., Sanchez C., Laneuville S., Turgeon S.L. and Gauthier S.F. 2004. Associative phase separation of b-lactoglobulin/pectins solutions: A kinetic studiy by small angle static light scattering. Colloids and Surfaces B-Biointerfaces, 35, 15-22.

9. Sanchez C., Mekhloufi G., Schmitt C., Renard D., Robert P., Lehr C.-M., Lamprecht A., and Hardy J. 2002. Self-assembly of b-lactoglobulin and acacia gum in aqueous solvent : Phase-ordering kinetics and structure. Langmuir, 18, 10323-10333.

10. Schmitt C., Sanchez C., Lamprecht A., Renard D., Lehr C.M., de Kruif K.G. and Hardy J. 2001. Study of b-lactoglobulin-acacia gum complex coacervation by diffusing wave spectroscopy and confocal laser scanning microscopy. Colloids and Surfaces B : Biointerfaces, 20, 267-280.

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Created by Hte inra on 10 December 2012, at 11:23