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Title: High pressure, thermal, and combined pressure-temperature stabilities of alpha-amylases from Bacillus species
Authors: Weemaes, C ×
DeCordt, S
Goossens, K
Ludikhuyze, Linda
Hendrickx, Marc
Heremans, Karel
Tobback, Paul #
Issue Date: Jan-1996
Publisher: John wiley & sons inc
Series Title: Biotechnology and Bioengineering vol:50 issue:1 pages:49-56
Abstract: Three different a-amylases from Bacillus subtilis, B. amyloliquefaciens, and B. licheniformis, were mutually compa red with respect to thermal stability, pressure stability, and combined pressure-temperature stability. Measurements of residual enzyme activity and residual denaturatio n enthalpy showed that the alpha-amylase from B. licheniformis has by far the highest thermostability and that the two other alpha-amylases have thermostabilities of the same order of magnitude. FTIR spectroscopy showed that changes in the conformation of the alpha-amylases from B. amyloliquefaciens, B. subtilis, and B. licheniformis due to pressure occurred at about 6.5, 7.5, and 11 kbar, respectively. It seemed that, for the enzymes studied, thermal stability was correlated with pressure stability. As to the resistance under combined heat and high pressure, the alpha-amylase from B. licheniformis was much more stable than the alpha-amylases from B. amyloliquefaciens and B. subtilis, the latter two being about equally stable. It appears that under high pressure and/or temperature, B. licheniformis alpha-amylase is the most resistant among the three enzymes studied. (C) 1996 John Wiley & Sons, Inc.
ISSN: 0006-3592
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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