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Keywords = steric mass action (SMA) isotherm

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15 pages, 3243 KiB  
Article
Optimization of Lactoperoxidase and Lactoferrin Separation on an Ion-Exchange Chromatography Step
by Naeimeh Faraji, Yan Zhang and Ajay K. Ray
Separations 2017, 4(2), 10; https://doi.org/10.3390/separations4020010 - 23 Mar 2017
Cited by 13 | Viewed by 7011
Abstract
Lactoperoxidase (LP), which is a high-value minor whey protein, has recently drawn extensive attention from research scientists and industry due to its multiplicity of function and potential therapeutic applications. In this study, the separation and optimization of two similar-sized proteins, LP and lactoferrin [...] Read more.
Lactoperoxidase (LP), which is a high-value minor whey protein, has recently drawn extensive attention from research scientists and industry due to its multiplicity of 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. A two-step optimization strategy was developed for the separation of LP and LF. Optimization was started with central composite design-based experiments to characterize the influences of different decision variables, namely, flow rate, length of gradient, and final salt concentration in the linear elution gradient step on the yield of LP. This was followed by a more accurate optimization of ion-exchange chromatography (IEC) separation of LP and LF based on an experimentally verified chromatographic model. 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 with improved product purity. Full article
(This article belongs to the Special Issue Ion Chromatography)
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