Optimization of single-step purification of alkaline protease using different hydrophobic ligands.
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.
Adikane
H V
HV
Chemical Engineering Division, National Chemical Laboratory, Pune, India. hva@che.ncl.res.in
Barhate
R S
RS
Thakar
D M
DM
Nene
S N
SN
D000327:Adsorption; D002846:Chromatography, Affinity / Q000379:methods*; D020092:Conidiobolus / Q000201:enzymology; D010450:Endopeptidases / Q000302:isolation & purification*; D008024:Ligands
D008024:Ligands; D010450:Endopeptidases