Free Access
Issue
Lait
Volume 80, Number 1, January-February 2000
New applications of membrane technology in the dairy industry
Page(s) 121 - 127
DOI https://doi.org/10.1051/lait:2000113
DOI: 10.1051/lait:2000113

Lait 80 (2000) 121-127

Shear separation: a promising method for protein fractionation

Mark F. Hurwitz ${^{\rm a}}$, John D. Brantley ${^{\rm b}}$

${^{\rm a}}$Process Equipment Development Department, Pall Corporation, Cortland, New York, 13045, USA
${^{\rm b}}$10 Deer Drive, Sound Beach NY, 11789, USA

Abstract:

Shear Separation is a method of separating macromolecules suspended in a fluid by inducing hydrodynamic forces that depend on size. The forces are produced in the laminar sub-layer of a turbulent shear boundary layer adjacent to a porous membrane. The suspended particles are lifted away from the porous membrane, against the drag of the permeate flow, by the viscous part of the shear stress. We have found that the transmission rate of a protein through the membrane depends on the shear rate, the permeate rate, the protein size, and the protein shape, even when the pore size of the membrane is substantially larger than the largest of the proteins. As a result, this is a size and shape dependent separation of the macromolecules. The membrane functions as a surface upon which an extremely high shear laminar sub-layer at the membrane surface may be generated. The effect has been demonstrated on the bench scale with clean mixtures of cytochrome C and bovine serum albumin. The separation can be observed with membranes rated approximately $\rm 300~kg\cdot mol^{-1}$ molecular weight cut off (MWCO) or less. Using this technique, milk serum containing BSA and smaller proteins without fats, caseins or immunoglobulins has been produced from skimmed milk. In addition, the milk serum has been fractionated with transmission fractions of 18% for BSA, 33% for $\beta$-lactoglobulin, and 62% for $\alpha$-lactalbumin.

shear separation / fractionation / dairy / ultra-filtration / protein

Correspondence and reprints: M.-F. Hurwitz
mark-hurwitz@pall.com

Copyright INRA, EDP Sciences

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