Secretory immunoglobulin purification from whey by chromatographic techniques

Area of Science:

• Biochemistry
• Immunology
• Biotechnology

Background:

• Secretory immunoglobulins (SIg) are crucial components of the mucosal immune system.
• SIg hold significant potential as therapeutic drug candidates.
• Existing platform technologies for SIg purification are lacking.

Purpose of the Study:

• To develop a simple, efficient, and generic chromatographic purification process for SIg.
• To establish a scalable method for obtaining highly pure, biologically active SIg.
• To create a adaptable process for purifying recombinant SIg species.

Main Methods:

• Utilized animal whey as a model system for SIg purification.
• Employed a two-step anion-exchange chromatography strategy.
• Optimized a key step using a small-porous anion exchanger in flow-through mode.

Main Results:

• Achieved SIg purity exceeding 95% using the developed anion-exchange process.
• The flow-through anion-exchange step enhanced purity from 66% to 89% with 88% yield.
• Overall yields ranged from 39% to 44% for SIgA and SIgM, depending on elution method.

Conclusions:

• The proposed chromatographic process enables preparative-scale purification of biologically active SIg from animal whey.
• This method provides a foundation for purifying recombinant SIg, expanding therapeutic possibilities.
• The developed process is efficient, scalable, and adaptable for future SIg purification needs.