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Evaluation of modified chitosan as matrix for hydrophobic interaction chromatography

Paper ID Volume ID Publish Year Pages File Format Full-Text
35848 45110 2008 7 PDF Available
Title
Evaluation of modified chitosan as matrix for hydrophobic interaction chromatography
Abstract

Chitosan beads were modified with glutaraldehyde and modified chitosan was investigated as matrix for hydrophobic interaction chromatography. The influence of temperature, type of salt and its ionic strength on the adsorption of α-galactosidase was studied. α-Galactosidase was found to bind in presence of high concentration of ammonium sulphate (3 M, w/v) and 90% of the bound enzyme was eluted with decreasing salt concentration in presence of 10% ethylene glycol. Attempt was made to purify α-galactosidase from modified chitosan, α-galactosidase showed 1.7-fold purification with 43.96% recovery of enzyme activity. The SDS–PAGE analysis of enzyme showed considerable purification and its molecular weight was found to be 63–64 kDa. Unlike other chromatographic matrices, the prepared chitosan beads were used five times. The results showed that purification and recovery of the enzyme did not change even when column size was increased.

Keywords
Chitosan; Glutaraldehyde; Hydrophobic interaction chromatography; Aspergillus oryzae; Ionic strength; Purification
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Evaluation of modified chitosan as matrix for hydrophobic interaction chromatography
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 6, June 2008, Pages 647–653
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
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