Hydrocolloids Structure and Properties The building blocks for structure Timothy J. Foster

18 month Meeting, Unilever Vlaardingen, March 29‐31, 2010 Manufactured Materials Foams Emulsions

Natural Materials This shows a layer of onion (Allium) cells. Targeting Hydrocolloids For Specific Applications:

Approach

Material Ingredient Properties

Microstructure

Oral Process Response Packaging Distribution Storage

Process Controlled oral response Process (mouth/gut) Controlling Structure (taste, flavour, texture)

CONSTRUCTION DECONSTRUCTION

Designed texture/ Ingredient In body functionality Ingredient appearance/ (enzymes) behaviour

Interaction with body mucins Reconstruction (associative and new phase separation)

Microstructure changes as a Impact on / of starting function of enzyme action materials / structures Re-assembly of structures as a function of digestion breakdown products and body secretions (micelle formation, delivery vehicles) Single Biopolymer systems Hydrocolloid Structure/ Function Need:

- define biopolymer primary structure

- understand the nature of the interaction / rates

- understand the solvent effects

- measure material properties

- test influence of primary structure variation and changes in environmental conditions on mechanical properties. Hydrocolloid Materials & Function

Gelling Thickening Emulsification Pectin • Gelatin Alginate Alginate • Milk proteins Starch • Egg proteins Agar LBG Carrageenan • Soya proteins Guar gum Gellan • Pea proteins Gelatin Xanthan • Gum Arabic Milk proteins Egg proteins Hydrocolloid Materials & Function

Gelling Thickening Emulsification •Pectin •Pectin •Gum Arabic • Alginate • Alginate • Propylene glycol Alginate •Starch •Starch • Sugarbeet pectin •Agar •LBG • OSA starch • Carrageenan •Guar Gum •Gellan • Xanthan •Curdlan • lamda Carrageenan • Celluosics • Cellulosics •Succinoglycan• Beta • Scleroglucan •Mixtures Protein structure A protein is a polymer of amino acids

• Primary structure –amino acid sequence • Secondary structure –spatial structure through interactions between amino acids that are near along the amino acid chain (e.g. α‐helix, β‐sheet) • Tertiary structure –spatial structure through interactions between amino acids that are far away along the amino acid chain • Quaternary structure – association of different amino acid sequences (e.g. haemoglobin) Protein

Protein Structure: Backbone random coils beta sheet alpha helix Charge Determines Properties: Interfacial properties foams emulsions Gel forming Structure of globular proteins

β‐lactoglobulin (β‐lg) dimeric form at neutral pH

α‐lactalbumin (α‐la) bovine serum albumin (BSA)

Color caption: α-Helix β-Sheets Cysteines Turbid Gels …what do they look like?

• How do they differ? H

CH2OH 6CH OH O 2 OH 5 O H H H OH 4 1 OH OH OH OH OH H H 3 2 H H OH H

CH2OH CH2OH CH2OH O O O H H OH OH H OH OH H OH

OH OH H H OH H H H OH H H H

H H H OH OH OH Gulose Interactions • Glycosidic linkage H H CH2OH OH O OH OH OH H H H OH OH OH O OH CH2OH H H H

H H CH2OH OH O OH OH OH H H +H20 H OH O O OH CH2OH H HH Structure / Functionality Sources of hydrocolloids Botanical starch, , galactomannans, pectin, gum arabic, karaya, tragacanth, beta glucan Seaweeds agar, carrageenan, alginate Animal gelatin, , hyaluronan Bacterial xanthan, gellan, Structural Features

•Linear – (homo- and hetero-) • Linear – branched – (homo- and hetero-) • Branched – (homo- and hetero-) • Ordered helices – (single, double, triple)

Polysaccharide thickeners

• The most efficient thickeners are;

•Linear, • High molecular mass •Charged Alternative Hydrocolloids Aloe Gum Cashew Gum Gum Ghatti Gum Karaya Oat gum Okra Gum Gum Tragacanth Caramania Gum (almond) Cassia Gum Cassava Starch Cherry Gum Chia Gum Chickpea Flour Cocoyam Flour Combretum Gum Cowpea protein /starch Cyclodextrins Detarium microcarpum polysaccharide Fenugreek gum Flaxseed Gum Gleditsia macracantha Hsian-tsao Leaf gum (Taiwan/China) Lesquerella Gum Lichenin Lucaena galactomannan Lupin Protein Manna Gum Moussul Gum (Plum) Opuntia Ficus Portulaca Oleracea Prickly Pear Psyllium gum Quince seed gum Rice Flour Rye bran (beta d glucan / arabinoxylan) Sassa Gum Sorghum flour Soy Bean Polysaccharide Tamarind gum Tara Gum Tremella Aurantia Poysaccharide Tropical Yam Yellow Mustard Gum Typical Solution Properties Hydrocolloid Structure/ Function

Need:

- define biopolymer primary structure

- understand the nature of the interaction / rates

- understand the solvent effects

- measure material properties

- test influence of primary structure variation and changes in environmental conditions on mechanical properties. Galactomannans • Galactomannans include guar gum, locust bean gum (carob), fenugreek, cassia and tara gum. •They have a high molecular mass (~ in excess of 500kDa) and consist of β 1,4 linked mannose residues with galactose units linked α 1,6.

•The M:G ratio is ~2:1 for guar, 3:1 for tara and 4:1 for locust bean gum. •The galactose units are not evenly distributed along the chain. LBG Structure / Functionality

•LBG can be fractionated wrt temperature of solubility. •Cold soluble LBG (30C) has a higher G/ M than that soluble at high temperature (80C). •LBG soluble at 80C has a galactose content of 16.6%, and gels at ambient temperature. •Cold soluble LBG does NOT gel even when frozen & thawed. •Not necessary for ice to be present, a non‐ionic interaction, dependent on solvent quality. - The distribution of galactose sidechains is all important in dictating functionality.

Gelation Rate Gelation Rate Gelation Rate

1.0 1.3 2.0 20 50 65 -8 10 [LBG] (%) Temperature

- Self association is kinetically controlled as a function of the number of available junction zones Properties of Hydrocolloids Load (KN). 0.06

0.05 Typical polymer gel

0.04 3%Gelatin properties Dependent on Solvent quality, 0.03 3%Agar Polymer fine structure, Junction 0.02 zone type / quantity 0.01

0 0 10203040506070 Strain (%). Effect of Shear during Gelation: Fluid gel Particle formation •Composite properties are dependent upon the number and size of particles produced. •This in turn is dependent upon the polymer used, the polymer concentration and the shear field.

Storage Modulus of Agar Gels Formed G'(Pa) Quiescently and Under Shear 1,000,000 Quiescent Measurement Temperature = 10C

Sheared 100,000

10,000

1,000

SPREADABLE 100 SPOONABLE POURABLE

10 012345 [Agar] • Due to the colloidal nature of their properties they provide better dilution characteristics than their molecular counterparts.

Viscosity (Pas) 1

Xanthan

0.1 Fluid gel

0.01 0.1 1 Level of Dilution Mixed Biopolymers

Aqueous-based two-phase systems

Microstructure

o/w emulsion water-in-water emulsion

25 μm Phase Separation phenomena is used in the creation of food products.

1.2

1.0 75% LBG / 25% PR 50% LBG / 50% PR 25% LBG / 75% PR

0.8

0.6 *

LBG (WT%) 0.4 * 0.2 *

0.0 024 6 8 10 12 14 16 18 20 MICELLAR CASEIN (WT%) Phase diagram measured at 5C Top phase: Gelatin Aqueous-based two-phase systems

Example: Aqueous mixture of gelatin and

For charged polymers (polyelectrolytes) salt (type and concentration) as well as pH are important parameters. Bottom phase: Maltodextrin Influence of varying polymer characteristics Phase separation driven by molecular ordering of one of the biopolymers.

12 Isothermal Binodal Evolution Owing to Ordering 10

o 20 C LH1 / SA2 No Salt 8

δ [SA2] / δt = 0.4 % / min 6

4 [LH1] / % w/w [LH1] /

2

0 02468101214 [SA2] / % w/w

• Schematic phase diagram showing the binodal as a function of ordering at 20 °C 1.5 16 14 20oC 12 1.0 Process effects τ 10 / cm Structure induced phase separation. 8 % Helix -1 • Measure of gelatin helices required % Helix 6 % Helix 0.5 to induce phase separation in a 4% 4 Turbidity LH1e:4% SA2 mixture , in water, Turbidity 2 when quenched to 20oC (top) and

0 0.0 246810 25oC (bottom). t / min • Morphology when quenched to 20oC.

1.5 16 o 14 25 C 29min 12 τ 1.0

% Helix / cm 10 4min Turbidity

8 -1 1min % Helix 6 0.5 4 2 0 0.0 10 20 30 40 50 t / min Process effects on mixed biopolymer systems. Effect of shear during cooling / gelation of the gelatin

Gelling biopolymer forms the dispersed phase. Structures based on aqueous-based two-phase systems

Scheme developed by Tolstoguzov*

*V Tolstoguzov Journal of Texture Studies 11, 3 (1980) 199-215 Gel particle suspensions

Modification of (shear) rheology: Effect of fibre alignment 10

50 μm relative viscosity

Dispersed phase volume: 20% 1 0.01 0.1 1 10 100

shear stress [Pa] Gel particle suspensions

Deposition: Non-food example

κ-carragenan fibres deposited on a hair. Spherical particles of the same composition wash off during rinse.

SEM micrograph by M Kirkland WO2003061607 A1

Ice Cream

Milk Protein LBG Air Ice 0.0016 Comparative Properties 0.0014 0.0012 0.001 0.0008 0.0006

Load (kN) 0.0004 0.0002 0 -0.0002 0 20 40 60 80 100 Displacement (mm) Conventional Maras Formulation Formulation

Short texture GB 9930531 Extensible texture ie. snaps US 20010031304 ie. stretches Hydrocolloid functionality in Maras Ice Cream

160% 140% 120% 100% 80% 60% 40% 20% % mean strain to failure 0% Sahlep Guar Xanthan CMC LBG Gelatin Carrageenan

Prior Art formulations

All products here compared at 30% Overrun Conclusion

•The fine structure of hydrocolloids plays a role in their properties (viscosity and gelation) •Influence of process can alter the functionality (single and mixed systems) • Hydrocolloid:Hydrocolloid interactions determine the gross properties of composites Point of dilution STRUCTURE RETENTION

4000

3500 STRUCTURE CREATION 3000

2500

2000

Viscosity / cP Viscosity 1500 150 um 1000

500 150 um

0 0 300 600 900 1200 1500 1800 2100 2400 2700 Time / s Acknowledge ALL past and present colleagues for support and stimulation