The influence of water activity on thermal stability of horseradish peroxidase

The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation...

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Bibliographic Details
Main Author: Hendrickx, M. (author)
Other Authors: Saraiva, J. (author), Lyssens, J. (author), Oliveira, J. (author), Tobback, P. (author)
Format: article
Language:eng
Published: 2011
Subjects:
Online Access:http://hdl.handle.net/10400.14/6648
Country:Portugal
Oai:oai:repositorio.ucp.pt:10400.14/6648