Gelation of Whey Protein Isolate Aggregates in Mixtures ... · 37 nm 77 nm. Title: Présentation...

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Gelation of Whey Protein Isolate Aggregates in Mixtures with Sodium Caseinate Introduction Whey protein isolate is derived from milk whey.Its main component is β-lactoglobulin. Heating solutions of WPI leads to formation of aggregates of different morphologies and sizes. The aggregates of WPI are known for their ability to form gels in the presence of Ca 2+ (cold gelation). Here we study the kinetics of the gelation process (1) and how mixing the aggregates with sodium caseinate influences their gelation properties and the structure of the gels (2). Results The size of the WPI aggregates (37 nm or 77 nm) does not influence the gelation speed, nor the modulus of the gels. Increasing the temperature increases the gelation rate, but not the gel stiffness. Gelation is an activated process with activation energy E a = 220 kJ/mol. Increasing the number of calcium ions per protein (R) increases the gelation rate, but not the gel stiffness. Increasing the protein concentration increases both the gelation rate and the gel stiffness. The gel structure is independent of the Ca concentration, but the gels are more heterogeneous at lower protein concentrations. Anna Kharlamova*,Taco Nicolai*, Christophe Chassenieux Université du Maine, IMMM UMR CNRS 6283, Avenue O. Messiaen 72085 Le Mans cedex 9 France The structure of the gels is not influenced by the addition of sodium caseinate. Aggregate size Ca 2+ per protein Protein concentration 1 2 Conclusions Bba association and the Regional council of Brittany and Pays de la Loire are acknowledged for funding this work through the interregional PROFIL project, carried out by the association ‘Pole Agronomique Ouest’. The rate of gelation of whey protein aggregates increases with increasing Ca concentration and increasing temperature, but the gels have the same structure and stiffness. The structure and stiffness vary with the aggregate concentration, but not their size. Whey protein aggregates have interesting functional properties allowing their use as ‘clean label’ texturizing ingredients (thickeners and gelling agents). *[email protected], [email protected] 16 th Food Colloids Conference Wageningen, April 10 – 13, 2016 Temperature Master curve Pure WPI aggregates Addition of sodium caseinate to WPI aggregates simply slows down their gelation, but does not influence the gel modulus. Activation energy controlling the WPI gelation is not influenced by the addition of sodium caseinate. Mixtures with sodium caseinate Mixing sodium caseinate and WPI aggregates allows control over the viscosity at constant protein concentration. 10 g/L WPI 20 g/L WPI 30 g/L WPI 40 g/L WPI Arrhenius plot 40 g/L WPI agg. (37 nm) R = 6 Time (s) 10 2 10 3 10 4 10 5 G' (Pa) 10 -1 10 0 10 1 10 2 10 3 0 sc 20 sc 40 sc 60 sc 37 nm aggregates R = 8 Time (s) 10 0 10 1 10 2 10 3 10 4 10 5 G' (Pa) 10 -1 10 0 10 1 10 2 10 3 10 4 20 g/L wpi 40 g/L wpi Time (s) 10 3 10 4 10 5 10 6 G' (Pa) 10 -1 10 0 10 1 10 2 10 3 60 o C 55 o C 50 o C 45 o C 40 o C 35 o C T -1 (10 -3 K -1 ) 2,9 3,0 3,1 3,2 3,3 3,4 Shift factor 10 -3 10 -2 10 -1 10 0 10 1 10 2 10 3 20 g/L wpi 37 nm R=8 20 g/L wpi 77 nm R=8 40 g/L wpi 37 nm R=4 40 g/L wpi 37 nm R=6 40 g/L wpi 37 nm R=8 40 g/L wpi 77 nm R=4 40 g/L wpi 77 nm R=8 E A = 220 kJ/mol 20 g/L WPI agg. (37 nm) R=6 T -1 (10 -3 K -1 ) 2,8 2,9 3,0 3,1 3,2 3,3 Shift factor 10 -3 10 -2 10 -1 10 0 10 1 10 2 10 3 0 sc 20 sc 40 sc 60 sc 40 µm 20 g/L WPI agg. + 20 g/L sodium caseinate + 60 g/L sodium caseinate 40 µm Gels with 20 g/L WPI aggregates (32 nm) and R=9 40 g/L WPI agg. (37 nm) Time (s) 10 0 10 1 10 2 10 3 10 4 10 5 10 6 G' (Pa) 10 -1 10 0 10 1 10 2 10 3 10 4 R=4 R=6 R=8 WPI agg. + SC, total protein 90 g/L % WPI agg. 0 20 40 60 80 100 Viscosity (Pa.s) 10 -3 10 -2 10 -1 10 0 pH 6.0 pH 6.3 pH 6.6 pH 6.9 20 o C 60 o C 40 g/L WPI agg. (37 nm) R=4 Time (s) 10 2 10 3 10 4 10 5 G' (Pa) 10 -1 10 0 10 1 10 2 10 3 20 g/L WPI agg. R=8 Time (s) 10 2 10 3 10 4 10 5 G' (Pa) 10 -1 10 0 10 1 10 2 37 nm 77 nm

Transcript of Gelation of Whey Protein Isolate Aggregates in Mixtures ... · 37 nm 77 nm. Title: Présentation...

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Gelation of Whey Protein Isolate Aggregates in Mixtures with Sodium Caseinate

Introduction Whey protein isolate is derived from milk whey. Its main component is β-lactoglobulin. Heating solutions of WPI leads toformation of aggregates of different morphologies and sizes. The aggregates of WPI are known for their ability to formgels in the presence of Ca2+ (cold gelation).Here we study the kinetics of the gelation process (1) and how mixing the aggregates with sodium caseinate influencestheir gelation properties and the structure of the gels (2).

Results

• The size of the WPI aggregates (37 nm or 77 nm)does not influence the gelation speed, nor themodulus of the gels.

• Increasing the temperature increases the gelationrate, but not the gel stiffness. Gelation is anactivated process with activation energy Ea = 220kJ/mol.

• Increasing the number of calcium ions per protein(R) increases the gelation rate, but not the gelstiffness.

• Increasing the protein concentration increasesboth the gelation rate and the gel stiffness.

• The gel structure is independent of the Caconcentration, but the gels are moreheterogeneous at lower protein concentrations.

Anna Kharlamova*, Taco Nicolai*, Christophe ChassenieuxUniversité du Maine, IMMM UMR CNRS 6283, Avenue O. Messiaen 72085 Le Mans cedex 9 France

• The structure of the gels is not influencedby the addition of sodium caseinate.

Aggregate size Ca2+ per proteinProtein

concentration

1

2

Conclusions

Bba association and the Regional council of Brittany and Pays de la Loire are acknowledged for funding this work through the interregional PROFIL project, carried out by theassociation ‘Pole Agronomique Ouest’.

• The rate of gelation of whey protein aggregates increases with increasing Ca concentration and increasing temperature,but the gels have the same structure and stiffness.• The structure and stiffness vary with the aggregate concentration, but not their size.• Whey protein aggregates have interesting functional properties allowing their use as ‘clean label’ texturizing ingredients(thickeners and gelling agents).

*[email protected], [email protected]

16th

Food

Col

loid

s C

onfe

renc

eW

agen

inge

n, A

pril

10 –

13,

2016

Temperature Master curvePure WPI aggregates

• Addition of sodium caseinate to WPI aggregatessimply slows down their gelation, but does notinfluence the gel modulus.• Activation energy controlling the WPI gelation isnot influenced by the addition of sodium caseinate.

Mixtures with sodium caseinate

• Mixing sodium caseinateand WPI aggregatesallows control over theviscosity at constantprotein concentration.

10 g/L WPI 20 g/L WPI 30 g/L WPI 40 g/L WPI

Arrhenius plot

40 g/L WPI agg. (37 nm)R = 6

Time (s)102 103 104 105

G' (

Pa)

10-1

100

101

102

103

0 sc20 sc40 sc60 sc

37 nm aggregates R = 8

Time (s)100 101 102 103 104 105

G' (

Pa)

10-1

100

101

102

103

104

20 g/L wpi40 g/L wpi

Time (s)103 104 105 106

G' (

Pa)

10-1

100

101

102

103

60 oC 55 oC50 oC45 oC40 oC35 oC

T-1 (10-3 K-1)2,9 3,0 3,1 3,2 3,3 3,4

Shift

fact

or

10-3

10-2

10-1

100

101

102

103

20 g/L wpi 37 nm R=820 g/L wpi 77 nm R=840 g/L wpi 37 nm R=440 g/L wpi 37 nm R=640 g/L wpi 37 nm R=840 g/L wpi 77 nm R=440 g/L wpi 77 nm R=8

EA = 220 kJ/mol

20 g/L WPI agg. (37 nm)R=6

T-1 (10-3 K-1)2,8 2,9 3,0 3,1 3,2 3,3

Shift

fact

or

10-3

10-2

10-1

100

101

102

1030 sc20 sc40 sc60 sc

40 µm

20 g/L WPI agg. + 20 g/L sodium caseinate

+ 60 g/L sodium caseinate

40 µm

Gels with 20 g/L WPI aggregates (32 nm) and R=9

40 g/L WPI agg. (37 nm)

Time (s)100 101 102 103 104 105 106

G' (

Pa)

10-1

100

101

102

103

104

R=4R=6R=8

WPI agg. + SC, total protein 90 g/L

% WPI agg.0 20 40 60 80 100

Visc

osity

(Pa.

s)

10-3

10-2

10-1

100pH 6.0pH 6.3pH 6.6pH 6.9

20 oC

60 oC

40 g/L WPI agg. (37 nm) R=4

Time (s)102 103 104 105

G' (

Pa)

10-1

100

101

102

103

20 g/L WPI agg. R=8

Time (s)102 103 104 105

G' (

Pa)

10-1

100

101

102

37 nm77 nm