Immobilising enzymes

Mind Map by E P, updated more than 1 year ago
Created by E P almost 5 years ago


A Levels Biology Mind Map on Immobilising enzymes, created by E P on 04/21/2015.

Resource summary

Immobilising enzymes
1 Adsorption
1.1 Enzyme molecules are mixed with the immobilising support and bind to it due to a combination of hydrophobic interactions and ionic links
1.1.1 Adsorbing gents used include porous carbon, glass beads, clays and resins Because the bonding forces are not particularly strong, some enzymes can become detached. However, provided the enzyme molecules are held so that their active site is not changed and displayed, adsorption can give very high reaction rates.
2 Covalent bonding
2.1 Enzyme molecules are covalently bonded to a support, often by covalently linking enzymes together to an absolute material (clay) using a cross-linking agent like gluteraldehyde or sepharose.
2.2 This method does not immobilise a large quantity of enzyme but binding is very strong so there is very little leakage of enzyme from the support.
3 Entrapment
3.1 Enzymes may be trapped in a bead network or in a cellulose fibre network.
3.1.1 However reaction rates can be reduced because substrate molecules need to get through the trapping barrier. This means the active site is less easily available than with adsorbed or covalently bonded enzymes
3.2 The enzymes are trapped in their natural state.
4 Membrane separation
4.1 Enzymes may be physically separated by a partially permeable membrane.
4.1.1 Most simply, the enzyme solution is held at one side of the membrane whilst substrate solution is passed slong the other side. Product molecules are small enough to pass back through the membrane.
4.1.2 Substrate molecules are small enough to pass through the membrane so that the reaction can take place.
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