Title: Convenience of immobilized bacillus-licheniformis alpha-amylase as time temperature-integrator (tti)
Authors: Decordt, Sf ×
Hendrickx, Marc
Maesmans, Gj
Tobback, Paul #
Issue Date: Feb-1994
Publisher: John wiley & sons ltd
Series Title: Journal of chemical technology and biotechnology vol:59 issue:2 pages:193-199
Abstract: For the immobilization of Bacillus licheniformis alpha-amylase to porous glass beads, the performances of three possible linking agents, glutaric dialdehyde, benzoquinone and s-trichlorotriazine were assessed in respect of the protein yield, the enzymic activity and the thermostability of the immobilized enzyme. These three properties are to be evaluated in view of the possible use of the enzyme preparations as time-temperature-integrators (TTIs) for assessing the severity of heat pasteurization or sterilization processes of food or pharmaceuticals. All three linkers improved the enzyme's resistance to irreversible heat inactivation to a similar extent and in each case biphasic inactivation kinetics were observed, whereas the dissolved B. licheniformis alpha-amylase showed a simple first order decay. The immobilization yield, measured as protein per carrier weight, did not differ markedly for the three linkers, although the enzymic activity of the glutaric dialdehyde-linked enzyme was lower than that of the benzoquinone- and s-trichlorotriazine-linked preparations.
ISSN: 0268-2575
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
× 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