Recovery of free enzymes from product liquors by bio-affinity adsorption: Trypsin binding by immobilised soybean inhibitor
- P. J. HallingAffiliated withDepartment of Chemical and Biochemical Engineering, University College London
- , P. DunnillAffiliated withDepartment of Chemical and Biochemical Engineering, University College London
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Soybean trypsin inhibitor immobilised to sub-micron ferrite particles functions as an affinity adsorbent for trypsin and the adsorbed enzyme may be recovered following elution in dilute acid. Trypsin can be adsorbed from casein solutions that is has digested. Equilibrium is reached in under 2 min with an effective dissociation constant as low as 10−7 M, allowing recoveries of more than 90% of added enzyme under realistic conditions.
These results suggest that bioaffinity adsorbents could be used to recover an enzyme that has converted a macromolecular substrate. The operation of such a process is discussed, and some interactions are described that could be used with suitably high affinity adsorbents for other enzymes.
- Recovery of free enzymes from product liquors by bio-affinity adsorption: Trypsin binding by immobilised soybean inhibitor
European journal of applied microbiology and biotechnology
Volume 6, Issue 3 , pp 195-205
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