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Title: Thermostability of soluble and immobilized alpha-amylase from bacillus-licheniformis
Authors: Decordt, S ×
Vanhoof, Kristel
Hu, J
Maesmans, G
Hendrickx, Marc
Tobback, Paul #
Issue Date: Jan-1992
Publisher: John wiley & sons inc
Series Title: Biotechnology and Bioengineering vol:40 issue:3 pages:396-402
Abstract: In view of a possible application of the alpha-amylase from Bacillus licheniformis as a time-temperature integrator for evaluation of heat processes, 11 thermal inactivation kinetics of the dissolved and covalently immobilized enzyme were studied in the temperature range 90-108-degrees-C. The D-values (95-degrees-C) for inactivation of alpha-amylase, dissolved in tris-HCl buffer, ranged from 6 to 157 min, depending on pH, ionic strength, and Ca2+ and enzyme concentration. The z-value fluctuated between 6.2 and 7.6-degrees-C. On immobilization of the alpha-amylase by covalent coupling with glutaraldehyde to porous glass beads, the thermoinactivation kinetics became biphasic under certain circumstances. For immobilized enzyme, the D-values (95-degrees-C) ranged between 17 and 620 min, depending largely on certain environmental conditions. The z-value fluctuated between 8.1 and 12.9-degrees-C. In each case of biphasic inactivation, the z-value of the stable fraction (with the higher D-values) was lower than the z-value of the labile fraction.
ISSN: 0006-3592
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Quantum Chemistry and Physical Chemistry Section
Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

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