The thermal inactivation characteristics of dehydrated a-amylase in solid state at various moisture contents was studied at temperatures between 135 and 150°C. The inactivation kinetics show a first order decay. The enzyme was found to be more thermostable than in aqueous solution. The z-value dependency with moisture content has shown some fluctuactions, having an absolut minimum of 19°C at 23.9% moisture.
We applied "solvent engineering" (i.e. variation of environmental conditions) to and/or irnrnobilized Baci//us licheniforrnis a-amylase covalently onto porous glass beads. In this way, important alterations in its thermostability characteristics (kinactrE Ainactw) ere achieved.
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