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Inactivation of alpha-amylase from Bacillus amyloliquefaciens at low moisture c...

Saraiva, J.; De Cordt, S.; Hendrickx, M.; Oliveira, J.; Tobback, P.

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.


Changing the thermostability of Bacillus licheniformis a-amylase

De Cordt, S.; Saraiva, J.; Hendrickx, M.; Maesmans, G.; Tobback, P.

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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