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Scale-up of native beta-lactoglobulin affinity separation process.

H K Vyas¹, J M Izco, R Jiménez-Flores

¹Dairy Products Technology Center, California Polytechnic State University, San Luis Obispo 93407, USA.

Journal of Dairy Science

|August 31, 2002

Summary

This study scaled up affinity separation of beta-lactoglobulin using all-trans-retinal on calcium bio-silicate. The fluidized bed column method achieved high purity and recovery, proving suitable for industrial application.

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Area of Science:

Biochemistry
Chemical Engineering
Separation Science

Background:

Beta-lactoglobulin is a major whey protein.
Efficient separation methods are needed for industrial applications.
Native protein purification requires gentle techniques.

Purpose of the Study:

To scale up affinity separation of native beta-lactoglobulin.
To evaluate different mixing methods for immobilized all-trans-retinal on calcium bio-silicate.
To optimize beta-lactoglobulin separation from industrial sweet whey.

Main Methods:

Pilot-scale affinity separation using immobilized all-trans-retinal on calcium bio-silicate.
Comparison of three mixing methods: packed column, stirred tank, and fluidized bed column.
Adsorption and desorption at varying pH and buffer concentrations, followed by ultrafiltration and freeze-drying.

Main Results:

The fluidized bed column and stirred tank methods yielded beta-lactoglobulin purity greater than 95%.
Recovery rates were 0.65 g/kg for the packed column, and 2.88 g/kg for both stirred tank and fluidized bed columns.
The packed column showed significantly lower purity and recovery due to insufficient fluid-solid contact.

Conclusions:

The fluidized bed column method is the most effective for scaling up beta-lactoglobulin affinity separation.
Gentle mixing in the fluidized bed column enhances interaction efficiency.
This method shows promise for industrial-scale purification of native beta-lactoglobulin.