Next Genera*on Milk Protein Ingredients for Infant Formula and Clinical Food Applica*on Richa Singh 1, Shane V. Crowley 2, Mike Molitor 3, John A. Lucey 1, 3 Mark R. Etzel 1,4 1 Department of Food Science, University of Wisconsin- Madison, WI, USA 2 School of Food and NutriNonal Sciences, University College Cork, Cork, Ireland 3 Centre for Dairy Research, University of Wisconsin- Madison, WI, USA 4 Department of Chemical and Biological Engineering, University of Wisconsin- Madison, WI, USA 1
Infant formula: Fundamentals of ingredient requirements Components Human milk (%, w/w) Bovine milk (%, w/w) Difference Carbohydrate 7.2 4.8 +50% Fat 4.2 4.0 +5% Ash 0.2 0.7-71% Protein 0.9 3.4-74% Whey : Casein rano 60:40 20:80 Human milk Protein ComposiNon High α- LA High β- CN Li^le α- CN No β- LG 2
Objectives OpNmising producnon and purity of β- casein concentrate(bcc) and serum protein concentrate(spc) during membrane fracnonanon Next GeneraNon milk protein ingredients for infant formula and clinical food applicanon using charged membrane 3
How to improve beta casein purity? Hypothesis Optimising β-cn aggregation by controlling ionic strength and protein concentration improves the purity of both Beta casein concentrate(bcc) and Serum protein concentrate(spc) ingredients. 4
High ionic strength destabilize β-casein at 26 C Turbidity at 26 C (NTU) 1200 1000 800 600 400 200 0 0 1 2 3 4 5 Solids content of UFP used to dilute SPC (%) β- CN- enriched SPC diluted to 1.2% protein in ultrafiltranon permeate(ufp) and warmed to 26 C/30 min UFP diluted to different total solids 0-5% Turbidity increased with ionic strength(µ), but SPC diluted in 3-5% UFP formed precipitates Presence of ions can promote β- CN aggreganon, but high µ can result in destabilisanon 5
Process flow diagram for optimised membrane filtration trial UF permeate (5.0% solids) skim milk MF (<5 C) MF retentate (micellar casein) DF water skim milk MF (<5 C) MF retentate (micellar casein) DF water MF permeate (β- CN and whey proteins) UF UF permeate (<0.7% solids) DF water MF permeate (β- CN and whey proteins) UF UF permeate (2.5% solids) UF retentate UF retentate, (1.2% protein) DF water MF (26 C) permeate removed connnuously MF retentate (β- casein) UF permeate (2.5% solids) MF (26 C) permeate total recycle, constant C p and µ MF retentate (β- casein) DF water MF permeate (whey proteins, 0.1% solids) UF UF DF water MF permeate (whey proteins) UF UF SPC BCC SPC BCC Spray- dry Spray- dry Spray- dry Spray- dry SPC powder BCC powder SPC powder BCC powder Process 1 NOTE: MF: MicrofiltraNon; UF: UltrafiltraNon; DF: DiafiltraNon Process 2 6
Optimal C p and µ results in increased purity of BCC and SPC powders ParNcles size distribunon shows large aggregates of β- CN which remained stable during fracnonanon at 26 C OpNmal C p and µ resulted in large β- casein aggregates Larger β- CN aggregates caused more retennon during MF, resulnng in less β- CN in SPC and more in BCC SPC produced by the opnmised process 2 had a casein content (11% of protein) NOTE: Cp: Protein concentranon; µ: Ionic strength 7
Objectives OpNmising producnon of β- casein and co- products during membrane fracnonanon Next GeneraNon Milk Protein Ingredients for Infant Formula and Clinical Food ApplicaNon 8
How to mimic human milk protein composition in infant formula? Protein Bovine milk Human milk Isoelectric point Molecular weight (g L -1 ) (ph) (kda) β-cn 8.6 3.9 4.8 23.9 β-lg 3.2 0 5.2 18.3 α-la 1.2 2.5 4.3 14.2 Purified SPC Charged membrane β- CN NaLve whey Charged membrane α- LA β- LG β- CN & α- LA β- LG OpNon 1 OpNon 2 9
Hypothesis Fractionating the principal whey protein (α-lactalbumin) and casein (βcasein) present in human milk from β-casein-enriched native whey using charged membranes, based on differences in their respective isoelectric points, is theoretically possible. 10
Objective & Benefits Objective ProducNon of a β- lactoglobulin- depleted, β- casein- and α- lactalbumin- enriched protein base Applications Infant formula Medical food applicanons. Benefits Amino acid profile closer to human milk, (high tryptophan) May allow reducnon in protein levels of current formulae Process will generate a separate funcnonal protein stream (β- LG) 11
Future direction! OpNmizing the selecnvity of the charged membrane fracnonanon process by modulanon of crincal parameters, ph Ionic strength Temperature Membrane charge Permeate flux 12
Acknowledgement Dr. John Lucey, Dr. Mark Etzel, Mike Molitor, Shane V. Crowley Lucey- Lab members Dairy Management Inc. 13
Thank You Questions? 14