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Updated: Aug 15, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
Optimization of single-step purification of alkaline protease using different hydrophobic ligands
H V Adikane1, R S Barhate, D M Thakar
1Chemical Engineering Division, National Chemical Laboratory, Pune, India. hva@che.ncl.res.in
Abstract:
The adsorption and desorption pattern of alkaline protease was studied using different aliphatic and aromatic hydrophobic ligands. Overall, higher adsorption was obtained on ligands coupled to 6% cross-linked gel than the 4% gel. The highest adsorption was obtained on butyl (94%) and phenyl (98.4%) of 6% cross-linked gel. The adsorption was dependent on concentration and nature of the ligand. In a single-step operation, almost 20-fold purification with 40% yield of the enzyme was obtained using all the optimized experimental parameters.
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