Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10236018 | Process Biochemistry | 2011 | 5 Pages |
Abstract
Chymotrypsin was purified from an activated homogenate of bovine pancreas by adsorption onto non-soluble alginate beads in 25Â mM Tris-acetate-5Â mM CaCl2 buffer at different adsorbate-adsorbent ratios and the pH values were assayed. Under all the experimental conditions, the enzyme has a positive net electrical charge whereas alginate is negatively charged. After performing steps of washing and desorption in 25Â mM Tris-acetate-500Â mM CaCl2 buffer pH 7.0, chymotrypsin was purified 9 times with an enzyme recovery of 62%. The eluate fractions resulted in two bands in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The method allows purification with suitable values from a raw sample like pancreas homogenate without a previous clarification step.
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Authors
DarÃo Spelzini, Beatriz Farruggia, Guillermo Picó,