Abstract
In this work, milk protein concentrate (MPC) was made using wide-pore negatively charged ultrafiltration membranes. The charged membranes were used for a six-fold volume concentration of skim milk and subsequent diafiltration to mimic the industrial MPC process. The charged 100 kDa membranes had at least a four-fold higher permeate flux at the same protein recovery as unmodified 30 kDa membranes, which are currently used in the dairy industry to make MPC. By placing a negative charge on the surface of an ultrafiltration membrane, the negatively charged proteins were rejected by electrostatic repulsion and not simply size-based sieving. Mass balance models of concentration and diafiltration were developed and the calculations matched the experimental observations. This is the first study to use wide-pore charged tangential-flow membranes for MPC manufacturing. Additionally, a unique mass balance model was applied, which accurately predicted experimental results.
Highlights
Dairy protein ingredients are ubiquitous in snack foods and infant formula, foods for the elderly, and foods for fitness enthusiasts
The goal was to operate at a higher permeate flux without exceeding the sieving coefficients of the 30 kDa unmodified polyethersulfone (PES) membrane used in industry
Using wide pore charged membranes and permeate flux control made at least a six-fold concentration of skim milk possible
Summary
Dairy protein ingredients are ubiquitous in snack foods and infant formula, foods for the elderly, and foods for fitness enthusiasts. Specific milk proteins like β-casein, alpha-lactalbumin (ALA), lactoferrin and lactoperoxidase are used in humanized infant formula [1]. The properties and uses of different milk proteins can be found elsewhere [2,3,4,5,6,7,8]. Skim milk contains approximately 8.6% in total solids, of which proteins account for 3.2% and lactose, ash, non-protein nitrogen (NPN) and small molecules comprise the other 5.4% [8]. Skim milk consists of approximately 35–37% protein. The milk protein is grouped into casein and the serum proteins, which range in molecular mass from 14.4–150 kDa [3]
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