Preprint Article Version 1 NOT YET PEER-REVIEWED

Optimization of Lactoperoxidase and Lactoferrin Separation on an Ion-Exchange Chromatography Step

Version 1 : Received: 11 January 2017 / Approved: 12 January 2017 / Online: 12 January 2017 (09:59:40 CET)

A peer-reviewed article of this Preprint also exists.

Faraji, N.; Zhang, Y.; Ray, A.K. Optimization of Lactoperoxidase and Lactoferrin Separation on an Ion-Exchange Chromatography Step. Separations 2017, 4, 10. Faraji, N.; Zhang, Y.; Ray, A.K. Optimization of Lactoperoxidase and Lactoferrin Separation on an Ion-Exchange Chromatography Step. Separations 2017, 4, 10.

Journal reference: Separations 2017, 4, 10
DOI: 10.3390/separations4020010

Abstract

Lactoperoxidase (LP), which is a high-value minor whey protein, has recently drawn extensive attention from research scientists and industry due to its multi-function and potential therapeutic applications. In this study, the separation and optimization of two similar-sized proteins, LP and lactoferrin (LF) were investigated using strong cation exchange column chromatography. Optimization was started with central composite design based experiments to characterize the importance of different decision variables. The three variables used in the optimization were flow rate, length of gradient and final salt concentration in the linear elution gradient step. The obtained empiric functional model represented the effect of the significant factors on the yield as the objective function. Afterwards, the calibrated mechanistic model was employed to predict accurate optimal set of variables. The optimal operating points were found and the results were compared with validation experiments. Predictions respecting yield confirmed a very good agreement with experimental results while keeping purity, a product quality characteristic, equal or above to a predefined value.

Subject Areas

cation exchange chromatography; minor milk protein; response surface modeling; simulation; steric mass action (SMA); optimization

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