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The formation of enzyme-substrate complex, often in connection with the adsorption of the enzyme leading to either partial immobilisation in which the enzymes are adsorbed on a colloid or total immobilisation in which the enzyme is adsorbed on a rigid immobile phase is the concern of some researchers. The interest in immobilised substrate common in biological system is not very common. The objectives of this theoretical research are the rederivation of the equations of association and dissociation of reactants in the presence of adsorbents, insoluble larger macro-or supra-molecule and elucidation of why such equations are important and generalisable. The derivations produced two different equations that describe mathematically the net flux of either the substrate where the enzyme is adsorbed or the net flux of the enzyme where the substrate is adsorbed. The derivation also produced equations of translational velocities, given the probabilities that reactions occur following complex formation or that an escape of bullet molecules or dissociation reactions occur. In conclusion two different equations need separate derivation for association and dissociation of reactants. The needs for the flux of reactants have both biological and industrial relevance, respectively due to importance of time-dependent digestive processes and for the optimisation of the production of desired products of enzymatic action. The equations describing net flux seem generalisable in that information about the physicochemical properties of both crowding agent and immobilisers may not be needed for calculations.

gsc biological and pharmaceutical sciences

Association-dissociation equations, distinct from Michaelis-Menten equation for the quantification of the net flux of reactants with or without immobiliser.