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Problem statement: The enzyme immobilization has experienced substantial growth in the recent past and an ever increasing amount of study has been reported on various aspects of immobilized enzymes. In most of these investigations, catalytic activities are found to be diminished as compared to the enzyme free in solution. Approach: Hydrophobic adsorbents were prepared containing L-leucine or citric acid, two positive allosteric effectors, for bovine liver Glutamate Dehydrogenase (GDH, EC 1.4.1.3) and heart mitochondrial Malate Dehydrogenase (MDH, EC 1.1.1.37 ), respectively. Results: Immobilized preparations of these well-defined allosteric enzymes indicated improved catalytic activities as compared with those involving use of the adsorbents without these activators. Conclusion/Recommendations: It is concluded that the regulatory proteins are Furthermore; they retain their natural capacity for undergoing the conformational transitions needed for enhanced catalytic activities. Adsorptive immobilization of these two allosteric proteins in activated conformation may serve as useful models in relation to design strategies for preparation of tailor-made enzyme carriers

Tailor-Made Enzyme Carriers: Preparation and Use of Adsorbents Specifically Designed to Immobilize Allosteric Enzymes in Activated Conformation