Enzyme‐catalyzed reactions occur at a wide range of moisture levels, including those corresponding to water activities (aw) well below unity. The model system of microcrystalline cellulose, sucrose and invertase was selected to study the behavior of invertase as functions of aw, time and temperature.
The results show that the Onset of reaction occurs below the anticipated mobilization for crystalline sucrose (aw 0.81) and that measurable reaction occurs at an aw as low as 0.58. The Maximum Extent of reaction is independent of moisture content at or above aw 0.75. The overall Rate of reaction for a given treatment fitted a first‐order kinetic model. Rate constants (a) obeyed Arrhenius plots (25° to 47°C) with activation energies (Ea) varying from 15.7 to 4.8 Kcal/mole for aw's from 0.58 to 0.90, respectively, (b) increased in direct proportion to enzyme concentration, and (c) increased strongly and nonlinearly with aw and moisture.
A model with two rate‐limiting steps has been postulated. At high moisture content, sucrose diffusion through a resistance shell confined to the vicinity of an invertase molecule is limiting. At low moisture content, aw and temperature may affect the conformation of the enzyme itself, or the diffusion coefficient in the rate‐controlling resistance shell.