Enzyme kinetic data for oxidation of phenolic substrates in an organic
-medium polyphenol oxidase biocatalytic system, were analysed by techn
iques relating specifically to nbn-aqueous biocatalysis. The results w
ere related to steric, hydrophobic, and electronic character in the su
bstrates; steric and hydrophobic character were found to influence the
kinetics. Molecular modelling and kinetic results together gave an es
timate of steric capacity in the binding site in the organic medium.