The Kinetics of Amylolysis. Part II. Determination of Reactive and Non‐Reactive Enzyme Substrate Encounters in beta‐Amylolysis

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Abstract
The ratio of the reactive and non‐reactive enzyme substrate encounters was determined from the data of measurements obtained at the β‐amylolysis of amylose of DP = 250 labelled with 14C at its non‐reducing chain end, taking into account the self‐inhibiting effect of the inner segments of the amylose chain. During the β‐amylolysis the number of bond splittings was 14.6 per effective enzyme substrate encounters, and only 0.405 when also the inactive encounters are taken into account, under the chosen experimental conditions.From these values and from the kinetic constants, the actual rate constants of the formation and dissociation of both reactive and inactive enzyme substrate complexes were determined.