Heat Stability, Solubility, and Functionality of Whey Protein: Tonya C. Schoenfuss, University of Minnesota

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1 Heat Stability, Solubility, and Functionality of Whey Protein: Tonya C. Schoenfuss, University of Minnesota

2 Milk Proteins Caseins Random Coil Poor in sulfur AA's Present in a colloidal suspension Generally stable to heat Non crystalline Distinct hydrophobic and hydrophilic regions Insoluble at ph 4.6 (when warm) Whey Proteins Ordered protein structure Higher in sulfur AA's Soluble in milk Easily denatured by heat Can crystallize (to see structure) Balanced distribution of hydrophobic/hydrophilic regions Soluble at 4.6, and at their isoelectric points in native state

3 Whey Proteins Brown Fundamentals of Dairy Chemistry

4 What Functional Properties Do We Desire in Whey Proteins? Solubility Gel formation (or not) Emulsification Water binding

5 β-lactoglobulin 50% of the protein in the serum phase Present as dimers (associates with itself) ph dependant Monomer <3, >8 Dimer Octomer 3 to 5.1 Easily denatured by heat starting at 73 C (163 F) reversible dissociation of oligomers to monomers can form aggregates Two disulphide bonds & 1 free sulfhydryl group With skim milk UHT treatment (148 C (298 F), 2.5 seconds), half of the β-lac complexes w/ Κ-casein Two main genetic variants (A&B), that vary in their heat sensitivity and tendency to form octomers vary at two amino acids. Cows with the BB-allele have less β-lactoglobulin and increased casein Probably the most allergenic of the milk proteins (not present in human milk)

6 B-lactoglobulin B, red box indicates where A & B differ (Asp64 & Val118) Farrell et al JDS 87:

7

8 Sulfhydryl groups buried until heating Beta-barrel fold that internally binds Vit. A, fatty acids and other lipophilic compounds J.J. Adams et al Journal of Structural Biology 154:

9 β-lac Dimer Association Hydrogen bonds between two β-lac monomers Brownlow et al Structure 5:

10 Another View Edwards et al Chpt. 6 in Milk Proteins: from Expression to Food. Academic Press

11 α-lactalbumin High in cysteine 4 disulfide bonds, no free sulfhydryl group Rich in tryptophan 49% of the aa sequence identical to chicken eggwhite lysozyme Interacts with β-1,4- galactosyltransferase ltransferase to modify its structure to synthesize lactose

12 Ca 2+ binding site α-lactalbumin Edwards et al Chpt. 6 in Milk Proteins: from Expression to Food. Academic Press

13 α-lactalbumin B Farrell et al JDS 87:

14 Effect of Heat on Whey Proteins Whey proteins denature complex with casein (K-casein) Issue for most cheese makes reduces gel strength and lengthens coagulation time Increase viscosity and water holding Can precipitate at their isoelectric point if heat denatured (way ricotta is made)

15

16 Interaction w/ Caseins How We Classify Powder Treatments Powder Class Temp/Time Whey Protein Nitrogen Low Heat 75C/15 s Not less than 6.0 mg/g Medium Heat 85C/20 s mg/g Not more than 1.5 High Heat 124C/30s mg/g As you heat, whey protein interacts with casein, and you have less in the whey fraction by this test

17 Effect of ph of Heating on Solubility Used WPI Varied ph and temp and measured solubility Least soluble if heated at around 4.5 Pelegrine & Gasparetto Lebensm.Wiss. u-technol. 38:77 80

18 Effect of Ionic Strength on Effects Solubility Small amounts of NaCl can salt-in protein and increase solubility Whey Proteins

19 Effect of Ionic Strength on Whey Protein Solubility at ph 4.6 WPI from ion exchange min solubility at ph 5.2, membrane derived at 4.6 (mainly denaturation effect). WPC s Authors recommend ionic strength of 0.1 when testing solubility at ph 4.6 A&B genetic variants β-lac will behave differently because of charge density de Wit and van Kessel. Food Hydrocolloids 1996, 10:

20 Genetic Variants Can Affect Interaction w/ K-casein O Sullivan et al. Lait (1999) 79, AA had higher sulfhydryl content than BB indicating less denaturation ti

21 Thermal Stability Measured by DSC for Genetic Variants Imifidon at al. 1991J Dairy Sci 74: Study also measured the in:teractions with K-casein genetic variants Concluded the substitution of Gly 64 and Ala 118 for Asp and Val in β-lg AA rendered the structural integrity of β-lg BB more resistant to heat in the presence of CaCl

22 Solubility and gel strength at failure for 20% (w/w) WPC gels in 0.6 M NaCI, 0.1 M Na phosphate buffer, ph 7. The protein most denatured (least soluble) was β- lactoglobulin As denaturation increased: Red. solubility Red. gel strength Emulsification index increased w/ denaturation to 41% soluble than decreased Beuschel et al J Food Sci , 634.

23 Modification of Whey Gels from WPI (BiPro) Using Whey Particles Made microparticulates Blended microparticulates w/ unparticulated WPI & heated at 90 C for 30 min Above 11% WPI w/o particles, saw gelling The particulates reduced the elastic behavior of the gels i.e. softer gels Found particulates to be an inactive filler gel Saglam et al Food Hydrocolloids 38: State diagram of whey protein in continous phase vs whey particles Total protein in system Filled squares are gelled samples

24 Relationship Between Whey Protein Denaturation on Acid Gel Firmness and Syneresis Looked at different heating regimes Heated only before powder manufacture Heated only after reconstitution Heated both before and after constitution McKenna and Anema IDF Special Issue 9303, pp

25 Sedimentation/Aggregation of Protein in High Protein Beverages Villumsen et al LWT - Food Science and Technology Compared heat treatment of WPI and storage temps for 6 months for storage induced aggregation 70g protein/l at ph 3.0 Suggested the aggregated spot contained glycomacropeptide that self-assembled or proteolytic fragments of β-lg or α-la

26 Take-aways β-lactoglobulin the most heat sensitive protein & responsible for much of the functionality effects (good and bad) observed Changes in functional properties due to: denaturation ionic strength ph Just measuring degree of denaturation doesn t always correlate with functional properties Selective denaturation ti can improve functionality when reduction in gel strength is desired Other proteins in the whey might be affecting stability

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