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