ITEM METADATA RECORD
Title: Increased susceptibility of beta-glucosidase from the hyperthermophile Pyrococcus furiosus to thermal inactivation at higher pressures
Authors: Bruins, Marieke E ×
Meersman, Filip
Janssen, Anja E. M
Heremans, Karel
Boom, Remko M #
Issue Date: Jan-2009
Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Journal vol:276 issue:1 pages:109-117
Abstract: The stability of beta-glucosidase from the hyperthermophile Pyrococcus furiosus was studied as a function of pressure, temperature and pH. The conformational stability was monitored using FTIR spectroscopy, and the functional enzyme stability was monitored by inactivation studies. The enzyme proved to be highly piezostable and thermostable, with an unfolding pressure of 800 MPa at 85 degrees C. The tentative pressure-temperature stability diagram indicates that this enzyme is stabilized against thermal unfolding at low pressures. The activity measurements showed a two-step inactivation mechanism due to pressure that was most pronounced at lower temperatures. The first part of this inactivation took place at pressures below 300 MPa and was not visible as a conformational transition. The second transition in activity was concomitant with the conformational transition. An increase in pH from 5.5 to 6.5 was found to have a stabilizing effect.
ISSN: 1742-464X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Imaging and Photonics
Chemistry - miscellaneous
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy

 




All items in Lirias are protected by copyright, with all rights reserved.

© Web of science