How Glycine Buffer Improves mAb Purification and Stability

 The use of glycine elution buffer for Protein A resulted in superior HCP removal which resulted in an improved polysorbate stability in the formulated antibody. 

An Easy Fix to Tough Problems

In a recent study published in Biotechnology & Bioengineering, Boehringer Ingelheim researchers uncovered a surprisingly potent ally in monoclonal antibody (mAb) purification: glycine buffer. Compared to the industry-standard acetate, glycine not only improved host cell protein (HCP) clearance but also enhanced polysorbate stability—critical for drug shelf life and safety.

 

The Findings:

Glycine buffer led to lower HCP and DNA levels post-virus inactivation and depth filtration.
It enabled 80–95% removal of PLBL2, a high-risk CHO-derived lipase, during anion exchange chromatography.
Final drug substances showed significantly improved PS20 stability over 4 weeks at room temperature.

 

The Study:

It leveraged the CHO PLBL2 ELISA Kit (E-65PLB) from Immunology Consultants Laboratory (ICL Inc.) to quantify residual PLBL2, a critical impurity linked to immunogenicity and formulation degradation.
Automated on the Octet HTX system, ICL’s kit provided precise, reproducible measurements that validated glycine’s impact across multiple mAbs.

 

Why It Matters:

This work offers a scalable, low-conductivity solution for improving impurity clearance, reducing troubleshooting and extending formulation stability. It’s a win for process efficiency and product quality.

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